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https://en.wikipedia.org/wiki/Altitudinal%20zonation | Altitudinal zonation (or elevational zonation) in mountainous regions describes the natural layering of ecosystems that occurs at distinct elevations due to varying environmental conditions. Temperature, humidity, soil composition, and solar radiation are important factors in determining altitudinal zones, which consequently support different vegetation and animal species. Altitudinal zonation was first hypothesized by geographer Alexander von Humboldt who noticed that temperature drops with increasing elevation. Zonation also occurs in intertidal and marine environments, as well as on shorelines and in wetlands. Scientist C. Hart Merriam observed that changes in vegetation and animals in altitudinal zones map onto changes expected with increased latitude in his concept of life zones. Today, altitudinal zonation represents a core concept in mountain research.
Factors
A variety of environmental factors determines the boundaries of altitudinal zones found on mountains, ranging from direct effects of temperature and precipitation to indirect characteristics of the mountain itself, as well as biological interactions of the species. The cause of zonation is complex, due to many possible interactions and overlapping species ranges. Careful measurements and statistical tests are required prove the existence of discrete communities along an elevation gradient, as opposed to uncorrelated species ranges.
Temperature
Decreasing air temperature usually coincides with increasing elevat |
https://en.wikipedia.org/wiki/Debrisoquine | Debrisoquine is a derivative of guanidine. It is an antihypertensive drug similar to guanethidine. Debrisoquine is frequently used for phenotyping the CYP2D6 enzyme, a drug-metabolizing enzyme.
See also
The guanidine part of the molecule also appears in guanoxan and guanadrel.
The 7-bromo analog of Debrisoquine is called Guanisoquin.
References
Adrenergic release inhibitors
Antihypertensive agents
Guanidines
Tetrahydroisoquinolines |
https://en.wikipedia.org/wiki/Fibroblast%20growth%20factor%20receptor%204 | Fibroblast growth factor receptor 4 is a protein that in humans is encoded by the FGFR4 gene. FGFR4 has also been designated as CD334 (cluster of differentiation 334).
The protein encoded by this gene is a member of the fibroblast growth factor receptor family, where amino acid sequence is highly conserved between members and throughout evolution. FGFR family members differ from one another in their ligand affinities and tissue distribution. A full-length representative protein would consist of an extracellular region, composed of three immunoglobulin-like domains, a single hydrophobic membrane-spanning segment and a cytoplasmic tyrosine kinase domain. The extracellular portion of the protein interacts with fibroblast growth factors, setting in motion a cascade of downstream signals, ultimately influencing mitogenesis and differentiation. The genomic organization of this gene, compared to members 1-3, encompasses 18 exons rather than 19 or 20. Although alternative splicing has been observed, there is no evidence that the C-terminal half of the IgIII domain of this protein varies between three alternate forms, as indicated for members 1-3. This particular family member preferentially binds acidic fibroblast growth factor and, although its specific function is unknown, it is overexpressed in gynecological tumor samples, suggesting a role in breast and ovarian tumorigenesis. In a meta-analisis study, the functional polymorphism Gly388Arg (rs351855) of FGFR4 was observed to be s |
https://en.wikipedia.org/wiki/FKBP1A | Peptidyl-prolyl cis-trans isomerase FKBP1A is an enzyme that in humans is encoded by the FKBP1A gene. It is also commonly referred to as FKBP-12 or FKBP12 and is a member of a family of FK506-binding proteins (FKBPs).
Function
The protein encoded by this gene is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. This encoded protein is a cis-trans prolyl isomerase that binds the immunosuppressants FK506 (tacrolimus) and rapamycin (sirolimus). It interacts with several intracellular signal transduction proteins including type I TGF-beta receptor. It also interacts with multiple intracellular calcium release channels including the tetrameric skeletal muscle ryanodine receptor. In mouse, deletion of this homologous gene causes congenital heart disorder known as noncompaction of left ventricular myocardium. Multiple alternatively spliced variants, encoding the same protein, have been identified. The human genome contains five pseudogenes related to this gene, at least one of which is transcribed.
Interactions
FKBP1A has been shown to interact with:
GLMN,
ITPR1
KIAA1303,
Mammalian target of rapamycin,
RYR1, and
TGF beta receptor 1.
References
Further reading
EC 5.2.1 |
https://en.wikipedia.org/wiki/HNRNPK | Heterogeneous nuclear ribonucleoprotein K (also protein K) is a protein that in humans is encoded by the HNRNPK gene. It is found in the cell nucleus that binds to pre-messenger RNA (mRNA) as a component of heterogeneous ribonucleoprotein particles. The simian homolog is known as protein H16. Both proteins bind to single-stranded DNA as well as to RNA and can stimulate the activity of RNA polymerase II, the protein responsible for most gene transcription. The relative affinities of the proteins for DNA and RNA vary with solution conditions and are inversely correlated, so that conditions promoting strong DNA binding result in weak RNA binding.
RNA binding protein domains in other proteins that are similar to the RNA binding domain of protein K are called K-homology or KH domains.
Protein K has been the subject of study related to colorectal cancer, in which an RNA editing event inducing the expression of an isoform containing a point mutation was found to be specific to cancerous cells.
Function
This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA-binding proteins, and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm.
The hnRNP |
https://en.wikipedia.org/wiki/ITPR1 | Inositol 1,4,5-trisphosphate receptor type 1 is a protein that in humans is encoded by the ITPR1 gene.
Interactions
ITPR1 has been shown to interact with:
AHCYL1,
CA8,
EPB41L1
FKBP1A,
MRVI1,
PRKG1,
RHOA, and
TRPC4.
Caspr2,
See also
Inositol triphosphate
Inositol triphosphate receptor
References
Further reading
External links
GeneReviews/NCBI/NIH/UW entry on Spinocerebellar Ataxia Type 15
Ion channels |
https://en.wikipedia.org/wiki/OLR1 | Oxidized low-density lipoprotein receptor 1 (Ox-LDL receptor 1) also known as lectin-type oxidized LDL receptor 1 (LOX-1) is a protein that in humans is encoded by the OLR1 gene.
LOX-1 is the main receptor for oxidized LDL on endothelial cells, macrophages, smooth muscle cells, and other cell types. But minimally oxidized LDL is more readily recognized by the TLR4 receptor, and highly oxidized LDL is more readily recognized by the CD36 receptor.
Function
LOX-1 is a receptor protein which belongs to the C-type lectin superfamily. Its gene is regulated through the cyclic AMP signaling pathway. The protein binds, internalizes and degrades oxidized low-density lipoprotein.
Normally, LOX-1 expression on endothelial cells is low, but tumor necrosis factor alpha, oxidized LDL, blood vessel shear stress, and other atherosclerotic stimuli substantially increase LOX-1 expression.
LOX-1 may be involved in the regulation of Fas-induced apoptosis. Oxidized LDL induces endothelial cell apoptosis through LOX-1 binding. Other ligands for LOX-1 include oxidized high-density lipoprotein, advanced glycation end-products, platelets, and apoptotic cells.
The binding of platelets to LOX-1 causes a release of vasoconstrictive endothelin, which induces endothelial dysfunction.
This protein may play a role as a scavenger receptor.
Clinical significance
Binding of oxidized LDL to LOX-1 activates NF-κB, leading to monocyte adhesion to enthothelial cells (a pre-requisite for the macrophage foam |
https://en.wikipedia.org/wiki/Luke%20Foils%20the%20Villain | Luke Foils the Villain is a 1916 American short comedy film starring Harold Lloyd.
Cast
Harold Lloyd as Lonesome Luke
Snub Pollard
Gene Marsh
Bebe Daniels as Maizie Nut
See also
Harold Lloyd filmography
References
External links
1916 films
1916 comedy films
Silent American comedy films
American black-and-white films
Films directed by Hal Roach
1916 short films
American silent short films
Lonesome Luke films
American comedy short films
1910s American films |
https://en.wikipedia.org/wiki/Baculoviral%20IAP%20repeat-containing%20protein%203 | Baculoviral IAP repeat-containing protein3 (also known as cIAP2) is a protein that in humans is encoded by the BIRC3 gene.
cIAP2 is a member of the inhibitor of apoptosis family that inhibit apoptosis by interfering with the activation of caspases. The encoded protein inhibits apoptosis induced by serum deprivation but does not affect apoptosis resulting from exposure to menadione, a potent inducer of free radicals. The cIAP2 protein contains three BIR domains, a UBA domain, a CARD domain and a RING finger domain. Transcript variants encoding the same isoform have been identified.
Interactions
Baculoviral IAP repeat-containing protein 3 has been shown to interact with:
CASP9,
RIPK1,
TRAF1,
TRAF2, and
UBE2D2.
References
Further reading
External links
Oncogenes |
https://en.wikipedia.org/wiki/MRE11A | Double-strand break repair protein MRE11 is an enzyme that in humans is encoded by the MRE11 gene. The gene has been designated MRE11A to distinguish it from the pseudogene MRE11B that is nowadays named MRE11P1.
Function
This gene encodes a nuclear protein involved in homologous recombination, telomere length maintenance, and DNA double-strand break repair. By itself, the protein has 3' to 5' exonuclease activity and endonuclease activity. The protein forms a complex with the RAD50 homolog; this complex is required for nonhomologous joining of DNA ends and possesses increased single-stranded DNA endonuclease and 3' to 5' exonuclease activities. In conjunction with a DNA ligase, this protein promotes the joining of noncomplementary ends in vitro using short homologies near the ends of the DNA fragments. This gene has a pseudogene on chromosome 3. Alternative splicing of this gene results in two transcript variants encoding different isoforms.
Orthologs
Mre11, an ortholog of human MRE11, occurs in the prokaryote archaeon Sulfolobus acidocaldarius. In this organism the Mre11 protein interacts with the Rad50 protein and appears to have an active role in the repair of DNA damages experimentally introduced by gamma radiation. Similarly, during meiosis in the eukaryotic protist Tetrahymena Mre11 is required for repair of DNA damages, in this case double-strand breaks, by a process that likely involves homologous recombination. These observations suggest that human MRE11 is de |
https://en.wikipedia.org/wiki/RNA%20polymerase%20II%20subunit%20B4 | DNA-directed RNA polymerase II subunit RPB4 is an enzyme that in humans is encoded by the POLR2D gene.
This gene encodes the fourth-largest subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes. In yeast, this polymerase subunit is associated with the polymerase under suboptimal growth conditions and may have a stress protective role. A sequence for a ribosomal pseudogene is contained within the 3' untranslated region of the transcript from this gene.
References
Further reading |
https://en.wikipedia.org/wiki/PPP1CA | Serine/threonine-protein phosphatase PP1-alpha catalytic subunit is an enzyme that in humans is encoded by the PPP1CA gene.
Function
The protein encoded by this gene is one of the three catalytic subunits of protein phosphatase 1 (PP1). PP1 is a serine/threonine specific protein phosphatase known to be involved in the regulation of a variety of cellular processes, such as cell division, glycogen metabolism, muscle contractility, protein synthesis, and HIV-1 viral transcription. Increased PP1 activity has been observed in the end stage of heart failure. Studies in both human and mice suggest that PP1 is an important regulator of cardiac function. Three alternatively spliced transcript variants encoding different isoforms have been found for this gene.
Interactive pathway map
Interactions
PPP1CA has been shown to interact with:
AKAP11,
BCL2-like 1,
BCL2L2,
BRCA1,
CDC5L,
Host cell factor C1,
KvLQT1,
LMTK2,
PHACTR3,
PPP1R15A,
PPP1R8,
PPP1R9B,
Protein kinase R, and
SMARCB1.
References
Further reading |
https://en.wikipedia.org/wiki/C-C%20chemokine%20receptor%20type%207 | C-C chemokine receptor type 7 is a protein that in humans is encoded by the CCR7 gene. Two ligands have been identified for this receptor: the chemokines (C-C motif) ligand 19 (CCL19/ELC) and (C-C motif) ligand 21 (CCL21). The ligands have similar affinity for the receptor, though CCL19 has been shown to induce internalisation of CCR7 and desensitisation of the cell to CCL19/CCL21 signals. CCR7 is a transmembrane protein with 7 transmembrane domains, which is coupled with heterotrimeric G proteins, which transduce the signal downstream through various signalling cascades. The main function of the receptor is to guide immune cells to immune organs (lymph nodes, thymus, spleen) by detecting specific chemokines, which these tissues secrete.
CCR7 has also recently been designated CD197 (cluster of differentiation 197).
Function
The protein encoded by this gene is a member of the G protein-coupled receptor family. This receptor was identified as a gene induced by the Epstein–Barr virus (EBV), and is thought to be a mediator of EBV effects on B lymphocytes. As stated above, the receptor guides immune cells to immune organs such as lymph nodes, which is needed for the development of both resistance and tolerance, but it is also important for development of T cells in thymus. The receptor is expressed mostly on adaptive immune cell types, namely thymocytes, naive T and B cells, regulatory T cells, central memory lymphocytes, but also dendritic cells. CCR7 has been shown to stimul |
https://en.wikipedia.org/wiki/Phospholipase%20D1 | {{DISPLAYTITLE:Phospholipase D1}}
Phospholipase D1 (PLD1) is an enzyme that in humans is encoded by the PLD1 gene, though analogues are found in plants, fungi, prokaryotes, and even viruses.
History
The possibility of PLD1 was first mentioned in 1947 by authors Hanahan and Chaikoff at Berkeley when describing a carrot enzyme that could "[split] choline from phospholipids." PLD was first derived in mammals in 1975 by Saito and Kanfer, who noted its activity in rats. PLD was first cloned from HeLa cell cDNA in 1995, while mammalian PLD1 was first cloned from a rat in 1997.
Function
Phosphatidylcholine (PC)-specific phospholipases D (PLDs) catalyze the hydrolysis of PC to produce phosphatidic acid (PA) and choline. A range of agonists acting through G protein-coupled receptors and receptor tyrosine kinases stimulate this hydrolysis. PC-specific PLD activity has been implicated in numerous cellular pathways, including membrane trafficking, signal transduction, platelet coagulation, mitosis, apoptosis, and the creation of cytoplasmic lipid droplets.
Membrane trafficking
PLD1 has been shown to associate at the plasma membrane, late endosome, early endosome, and the Golgi apparatus. There is evidence that PA is able to assist in negative membrane curvature due to its head group being smaller than in many other lipids. One experiment with PLD1 knockout showed a significant reduction in the number of exocytotic fusion events, implying a strong role in exocytosis.
Signal tran |
https://en.wikipedia.org/wiki/POLR2I | DNA-directed RNA polymerase II subunit RPB9 is an enzyme that in humans is encoded by the POLR2I gene.
This gene encodes a subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes. This subunit, in combination with two other polymerase subunits, forms the DNA binding domain of the polymerase, a groove in which the DNA template is transcribed into RNA. The product of this gene has two zinc finger motifs with conserved cysteines and the subunit does possess zinc binding activity.
References
Further reading |
https://en.wikipedia.org/wiki/Ryanodine%20receptor%202 | Ryanodine receptor 2 (RYR2) is one of a class of ryanodine receptors and a protein found primarily in cardiac muscle. In humans, it is encoded by the RYR2 gene. In the process of cardiac calcium-induced calcium release, RYR2 is the major mediator for sarcoplasmic release of stored calcium ions.
Structure
The channel is composed of RYR2 homotetramers and FK506-binding proteins found in a 1:4 stoichiometric ratio. Calcium channel function is affected by the specific type of FK506 isomer interacting with the RYR2 protein, due to binding differences and other factors.
Function
The RYR2 protein functions as the major component of a calcium channel located in the sarcoplasmic reticulum that supplies ions to the cardiac muscle during systole. To enable cardiac muscle contraction, calcium influx through voltage-gated L-type calcium channels in the plasma membrane allows calcium ions to bind to RYR2 located on the sarcoplasmic reticulum. This binding causes the release of calcium through RYR2 from the sarcoplasmic reticulum into the cytosol, where it binds to the C domain of troponin, which shifts tropomyosin and allows the myosin ATPase to bind to actin, enabling cardiac muscle contraction. RYR2 channels are associated with many cellular functions, including mitochondrial metabolism, gene expression and cell survival, in addition to their role in cardiomyocyte contraction.
Clinical significance
Deleterious mutations of the ryanodine receptor family, and especially the RYR2 r |
https://en.wikipedia.org/wiki/SFRS2 | Splicing factor, arginine/serine-rich 2 is a protein that in humans is encoded by the SFRS2 gene. MDS-associated splicing factor SRSF2 affects the expression of Class III and Class IV isoforms and perturbs granulopoiesis and SRSF2 P95H promotes Class IV splicing by binding to key ESE sequences in CSF3R exon 17, and that SRSF2, when mutated, contributes to dysgranulopoiesis.
Interactions
SFRS2 has been shown to interact with CDC5L and ASF/SF2.
References
Further reading
External links |
https://en.wikipedia.org/wiki/Zinc%20finger%20and%20BTB%20domain-containing%20protein%2016 | Zinc finger and BTB domain-containing protein 16 is a protein that in humans is encoded by the ZBTB16 gene.
Function
This gene is a member of the Krueppel C2H2-type zinc-finger protein family and encodes a zinc finger transcription factor that contains nine Kruppel-type zinc finger domains at the carboxyl terminus. This protein is located in the nucleus, is involved in cell cycle progression, and interacts with a histone deacetylase. Specific instances of aberrant gene rearrangement at this locus have been associated with acute promyelocytic leukemia (APL) and physiological roles have been identified in mouse Natural Killer T cells and gamma-delta T cells. Alternate transcriptional splice variants have been characterized in human.
Interactions
Zinc finger and BTB domain-containing protein 16 has been shown to interact with:
Angiotensin II receptor type 1,
BCL6,
BMI1,
Calcitriol receptor,
FHL2,
GATA1,
GATA2,
HDAC1,
HDAC4,
HDAC5,
HDAC6,
Heparin-binding EGF-like growth factor,
Nuclear receptor co-repressor 2,
Promyelocytic leukemia protein
RUNX1T1,
Retinoic acid receptor alpha,
SIN3A,
SIN3B, and
ZBTB32.
See also
Zbtb7
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/Bradykinin%20receptor%20B2 | {{DISPLAYTITLE:Bradykinin receptor B2}}
Bradykinin receptor B2 is a G-protein coupled receptor for bradykinin, encoded by the BDKRB2 gene in humans.
Mechanism
The B2 receptor is a G protein-coupled receptor, probably coupled to Gq and Gi. Gq stimulates phospholipase C to increase intracellular free calcium and Gi inhibits adenylate cyclase. Furthermore, the receptor stimulates the mitogen-activated protein kinase pathways. It is ubiquitously and constitutively expressed in healthy tissues.
The B2 receptor forms a complex with angiotensin converting enzyme (ACE), and this is thought to play a role in cross-talk between the renin-angiotensin system (RAS) and the kinin–kallikrein system (KKS). The heptapeptide angiotensin (1-7) also potentiates bradykinin action on B2 receptors.
Kallidin also signals through the B2 receptor. An antagonist for the receptor is Hoe 140 (icatibant).
Function
The 9 amino acid bradykinin peptide elicits several responses including vasodilation, edema, smooth muscle spasm and nociceptor stimulation.
Gene
Alternate start codons result in two isoforms of the protein.
See also
Bradykinin receptor
References
Further reading
External links
G protein-coupled receptors |
https://en.wikipedia.org/wiki/CDC25A | M-phase inducer phosphatase 1 also known as dual specificity phosphatase Cdc25A is a protein that in humans is encoded by the cell division cycle 25 homolog A (CDC25A) gene.
Function
CDC25A is a member of the CDC25 family of dual-specificity phosphatases.
Dual-specificity protein phosphatases remove phosphate groups from phosphorylated tyrosine and serine / threonine residues. They represent a subgroup of the tyrosine phosphatase family (as opposed to the serine/threonine phosphatase family).
All mammals examined to date have three homologues of the ancestral Cdc25 gene (found e.g. in the fungus species S. pombe), designated Cdc25A, Cdc25B, and Cdc25C. In contrast, some invertebrates harbour two (e.g., the Drosophila proteins String and Twine) or four (e.g., C. elegans Cdc-25.1 - Cdc-25.4) homologues.
CDC25A is required for progression from G1 to the S phase of the cell cycle, but also plays roles in later cell cycle events. In particular, it is stabilized in metaphase cells and is degraded upon metaphase exit akin to Cyclin B. It is competent to activate the G1/S cyclin-dependent kinases CDK4 and CDK2 by removing inhibitory phosphate groups from adjacent tyrosine and threonine residues; it can also activate Cdc2 (Cdk1), the principal mitotic Cdk.
Involvement in cancer
CDC25A is specifically degraded in response to DNA damage, resulting in cell cycle arrest. Thus, this degradation represents one axis of a DNA damage checkpoint, complementing induction of p53 and |
https://en.wikipedia.org/wiki/NFATC1 | Nuclear factor of activated T-cells, cytoplasmic 1 is a protein that in humans is encoded by the NFATC1 gene.
Function
The product of this gene is a component of the nuclear factor of activated T cells DNA-binding transcription complex. This complex consists of at least two components: a preexisting cytosolic component that translocates to the nucleus upon T cell receptor (TCR) stimulation, and an inducible nuclear component. Proteins belonging to this family of transcription factors play a central role in inducible gene transcription during immune response. The product of this gene is an inducible nuclear component. It functions as a major molecular target for the immunosuppressive drugs such as ciclosporin. Five transcript variants encoding distinct isoforms have been identified for this gene. Different isoforms of this protein may regulate inducible expression of different cytokine genes.
Interactions
NFATC1 has been shown to interact with PIM1.
See also
NFAT
References
Further reading
External links
Transcription factors
Human proteins |
https://en.wikipedia.org/wiki/Neuroblastoma%20RAS%20viral%20oncogene%20homolog | NRAS is an enzyme that in humans is encoded by the NRAS gene. It was discovered by a small team of researchers led by Robin Weiss at the Institute of Cancer Research in London. It was the third RAS gene to be discovered, and was named NRAS, for its initial identification in human neuroblastoma cells.
Function
The N-ras proto-oncogene is a member of the Ras gene family. It is mapped on chromosome 1, and it is activated in HL60, a promyelocytic leukemia line. The order of nearby genes is as follows: cen—CD2—NGFB—NRAS—tel.
The mammalian Ras gene family consists of the Harvey and Kirsten Ras genes (HRAS and KRAS), an inactive pseudogene of each (c-Hras2 and c-Kras1) and the N-Ras gene. They differ significantly only in the C-terminal 40 amino acids. These Ras genes have GTP/GDP binding and GTPase activity, and their normal function may be as G-like regulatory proteins involved in the normal control of cell growth.
The N-Ras gene specifies two main transcripts of 2 kb and 4.3 kb. The difference between the two transcripts is a simple extension through the termination site of the 2 kb transcript. The N-Ras gene consists of seven exons (-I, I, II, III, IV, V, VI). The smaller 2 kb transcript contains the VIa exon, and the larger 4.3 kb transcript contains the VIb exon which is just a longer form of the VIa exon. Both transcripts encode identical proteins as they differ only the 3′ untranslated region.
Mutations
Mutations which change amino acid residues 12, 13 or 61 activate |
https://en.wikipedia.org/wiki/RAP1A | Ras-related protein Rap-1A is a protein that in humans is encoded by the RAP1A gene.
Function
The product of this gene belongs to the family of Ras-related proteins. These proteins share approximately 50% amino acid identity with the classical RAS proteins and have numerous structural features in common. The most striking difference between RAP proteins and RAS proteins resides in their 61st amino acid: glutamine in RAS is replaced by threonine in RAP proteins. The product of this gene counteracts the mitogenic function of RAS because it can interact with RAS GAPs and RAF in a competitive manner. Two transcript variants encoding the same protein have been identified for this gene.
Interactions
RAP1A has been shown to interact with:
C-Raf,
MLLT4,
PDE6D,
RALGDS,
RAPGEF2, and
TSC2.
References |
https://en.wikipedia.org/wiki/Death%20receptor%204 | Death receptor 4 (DR4), also known as TRAIL receptor 1 (TRAILR1) and tumor necrosis factor receptor superfamily member 10A (TNFRSF10A), is a cell surface receptor of the TNF-receptor superfamily that binds TRAIL and mediates apoptosis.
Function
The protein encoded by this gene is a member of the TNF-receptor superfamily. This receptor is activated by tumor necrosis factor-related apoptosis inducing ligand (TNFSF10/TRAIL), and thus transduces cell death signal and induces cell apoptosis.
Studies with FADD-deficient mice suggested that FADD, a death domain containing adaptor protein, is required for the apoptosis mediated by this protein.
Interactions
TNFRSF10A has been shown to interact with DAP3.
References
Further reading
TNF receptor family
Clusters of differentiation |
https://en.wikipedia.org/wiki/Lymphoid%20enhancer-binding%20factor%201 | Lymphoid enhancer-binding factor 1 (LEF1) is a protein that in humans is encoded by the LEF1 gene. It's a member of T cell factor/lymphoid enhancer factor (TCF/LEF) family.
Function
Lymphoid enhancer-binding factor-1 (LEF1) is a 48-kD nuclear protein that is expressed in pre-B and T cells. It binds to a functionally important site in the T-cell receptor-alpha (TCRA) enhancer and confers maximal enhancer activity. LEF1 belongs to a family of regulatory proteins that share homology with high mobility group protein-1 (HMG1).
Clinical significance
LEF1 is highly overexpressed and associated with disease progression and poor prognosis in B-cell chronic lymphocytic leukemia and other kinds of malignancies like colorectal cancer. It is also a promising potential drug target.
Interactions
Lymphoid enhancer-binding factor 1 has been shown to interact with:
ALX4,
AML-1,
Catenin beta-1/β-catenin/CTNNB1, including transgenically,
EP300,
MITF
PIAS4,
SMAD2, and
SMAD3.
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/Baculoviral%20IAP%20repeat-containing%20protein%202 | Baculoviral IAP repeat-containing protein 2 (also known as cIAP1) is a protein that in humans is encoded by the BIRC2 gene.
Function
cIAP1 is a member of the Inhibitor of Apoptosis family that inhibit apoptosis by interfering with the activation of caspases.
Interactions
BIRC2 has been shown to interact with:
CASP9,
DIABLO,
GSPT1,
HSP90B1,
HTRA2,
RIPK1,
RIPK2
TNFSF14,
TRAF1,
TRAF2, and
UBC.
References
Further reading
External links
Proteins
Microbiology |
https://en.wikipedia.org/wiki/EIF4EBP1 | Eukaryotic translation initiation factor 4E-binding protein 1 (also known as 4E-BP1) is a protein that in humans is encoded by the EIF4EBP1 gene. inhibits cap-dependent translation by binding to translation initiation factor eIF4E. Phosphorylation of 4E-BP1 results in its release from eIF4E, thereby allows cap-dependent translation to continue thereby increasing the rate of protein synthesis.
Phosphorylation
Phosphorylated 4E-BP1 is thought to be a marker of upstream signaling (mTOR) activation. 4E-BP1 has seven phospho-sites, the three most important of which are the initiation site Thr 37/Thr 46, the second site Thr 70, and the final site Ser65. Moreover, phosphorylation of Ser 65 and Thr 70 alone was not sufficient to block the inhibition of mRNA translation by 4E-BP1, suggesting that multiple phosphorylation events must be combined to increase the rate of protein synthesis.
Function
This gene encodes one member of a family of translation repressor proteins. The protein directly interacts with eukaryotic translation initiation factor 4E (eIF4E), which is a limiting component of the multisubunit complex that recruits 40S ribosomal subunits to the 5' end of mRNAs. Interaction of this protein with eIF4E inhibits complex assembly and represses translation. This protein is phosphorylated in response to various signals including UV irradiation and insulin signaling, resulting in its dissociation from eIF4E and activation of cap-dependent mRNA translation.
High level of pho |
https://en.wikipedia.org/wiki/MT-ND6 | MT-ND6 is a gene of the mitochondrial genome coding for the NADH-ubiquinone oxidoreductase chain 6 protein (ND6). The ND6 protein is a subunit of NADH dehydrogenase (ubiquinone), which is located in the mitochondrial inner membrane and is the largest of the five complexes of the electron transport chain. Variations in the human MT-ND6 gene are associated with Leigh's syndrome, Leber's hereditary optic neuropathy (LHON) and dystonia.
Structure
The MT-ND6 gene is located in human mitochondrial DNA from base pair 14,149 to 14,673. MT-ND6 is the only protein-coding gene located on the L-strand of the human mitogenome.
The encoded protein is 18 kDa and composed of 172 amino acids. MT-ND6 is one of seven mitochondrial genes encoding subunits of the enzyme NADH dehydrogenase (ubiquinone), together with MT-ND1, MT-ND2, MT-ND3, MT-ND4, MT-ND4L, and MT-ND5. Also known as Complex I, this enzyme is the largest of the respiratory complexes. The structure is L-shaped with a long, hydrophobic transmembrane domain and a hydrophilic domain for the peripheral arm that includes all the known redox centres and the NADH binding site. MT-ND6 and the rest of the mitochondrially encoded subunits are the most hydrophobic of the subunits of Complex I and form the core of the transmembrane region.
Function
The MT-ND6 product is a subunit of the respiratory chain Complex I that is believed to belong to the minimal assembly of core proteins required to catalyze NADH dehydrogenation and electron tran |
https://en.wikipedia.org/wiki/Mucin%205AC | Mucin-5AC (MUC-5AC) is a protein that in humans is encoded by the MUC5AC gene.
MUC-5AC is a large gel-forming glycoprotein. In the respiratory tract it protects against infection by binding to inhaled pathogens that are subsequently removed by mucociliary clearance. Overproduction of MUC-5AC can contribute to diseases such as asthma and chronic obstructive pulmonary disease, and has also been associated with greater protection against influenza infection.
Clinical relevance
This gene has been linked to mucus hypersecretion in the respiratory tract and is associated to chronic obstructive pulmonary disease (COPD).
References
External links
PDBe-KB provides an overview of all the structure information available in the PDB for Human Mucin-5AC
05AC |
https://en.wikipedia.org/wiki/MYB%20%28gene%29 | Myb genes are part of a large gene family of transcription factors found in animals and plants. In humans, it includes Myb proto-oncogene like 1 and Myb-related protein B in addition to MYB proper. Members of the extended SANT/Myb family also include the SANT domain and other similar all-helical homeobox-like domains.
Function
Viral
The Myb gene family is named after the eponymous gene in Avian myeloblastosis virus. The viral Myb (v-Myb, ) recognizes the sequence 5'-YAACKG-3'. It causes myeloblastosis (myeloid leukemia) in chickens. Compared to the normal animal cellular Myb (c-myb), v-myb contains deletions in the C-terminal regulatory domain, leading to aberrant activation of other oncogenes.
Animals
Myb proto-oncogene protein is a member of the MYB (myeloblastosis) family of transcription factors. The protein contains three domains, an N-terminal DNA-binding domain, a central transcriptional activation domain and a C-terminal domain involved in transcriptional repression. It may play a role in cell cycle regulation. Like the viral version, this gene is an oncogene, and rearrangements of the gene (often involving deletion in the C-terminal domain) causes cancer.
Plants
MYB factors represent a family of proteins that include the conserved MYB DNA-binding domain. Plants contain a MYB-protein subfamily that is characterised by the R2R3-type MYB domain.
In maize, phlobaphenes are synthesized in the flavonoids synthetic pathway from polymerisation of flavan-4-ols which e |
https://en.wikipedia.org/wiki/PDE4D | cAMP-specific 3',5'-cyclic phosphodiesterase 4D is an enzyme that in humans is encoded by the PDE4D gene.
Function
The PDE4D gene is complex and has at least 9 different isoforms that encode functional proteins. These proteins degrade the second messenger cAMP, which is a key signal transduction molecule in multiple cell types, including vascular cells (Dominiczak and McBride, 2003).[supplied by OMIM]
Interactions
PDE4D has been shown to interact with myomegalin and GNB2L1.
Clinical relevance
Mutations in this gene have been associated to cases of acrodysostosis.
This is the subtype of PDE4 that appears to be involved in the emetic and antidepressant effects of PDE4 inhibitors.
Furthermore, changes in expression of the isoform PDE4D7 have been proposed as prostate cancer biomarker.
References
Further reading |
https://en.wikipedia.org/wiki/Sodium-hydrogen%20antiporter%203%20regulator%201 | Sodium-hydrogen antiporter 3 regulator 1 is a regulator of Sodium-hydrogen antiporter 3. It is encoded by the gene SLC9A3R1. It is also known as ERM Binding Protein 50 (EBP50) or Na+/H+ Exchanger Regulatory Factor (NHERF1). It is believed to interact via long-range allostery, involving significant protein dynamics.
Mechanism
Members of the ezrin (VIL2; MIM 123900)-radixin (RDX; MIM 179410)-moesin (MSN; MIM 309845) (ERM) protein family are highly concentrated in the apical aspect of polarized epithelial cells. These cells are studded with microvilli containing bundles of actin filaments, which must attach to the membrane to assemble and maintain the microvilli. The ERM proteins, together with merlin, the NF2 (MIM 607379) gene product, are thought to be linkers between integral membrane and cytoskeletal proteins, and they bind directly to actin in vitro. Actin cytoskeleton reorganization requires the activation of a sodium/hydrogen exchanger (SLC9A3; MIM 182307). SLC9A3R1 is an ERM-binding protein.[supplied by OMIM]
Interactions
Sodium-hydrogen antiporter 3 regulator 1 has been shown to interact with:
ADRB2,
Beta-catenin,
CFTR,
GNAQ,
OPRK1,
PAG1,
PDGFRA,
PDGFRB,
PDZK1,
PTH1R,
SLC4A8,
YAP1, and
EZR
See also
Cystic fibrosis transmembrane conductance regulator
Ezrin
Moesin
Neutron spin echo
Radixin
Solute carrier family
References
Further reading
Solute carrier family |
https://en.wikipedia.org/wiki/VE-cadherin | Cadherin-5, or VE-cadherin (vascular endothelial cadherin), also known as CD144 (Cluster of Differentiation 144), is a type of cadherin. It is encoded by the human gene CDH5.
Function
VE-cadherin is a classical cadherin from the cadherin superfamily and the gene is located in a six-cadherin cluster in a region on the long arm of chromosome 16 that is involved in loss of heterozygosity events in breast and prostate cancer. The encoded protein is a calcium-dependent cell–cell adhesion glycoprotein composed of five extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail. Functioning as a classic cadherin by imparting to cells the ability to adhere in a homophilic manner, the protein may play an important role in endothelial cell biology through control of the cohesion and organization of the intercellular junctions.
Integrity of intercellular junctions is a major determinant of permeability of the endothelium, and the VE-cadherin-based adherens junction is thought to be particularly important. VE-cadherin is known to be required for maintaining a restrictive endothelial barrier – early studies using blocking antibodies to VE-cadherin increased monolayer permeability in cultured cells and resulted in interstitial edema and hemorrhage in vivo. A recent study has shown that TNFAIP3 (A20, a dual-ubiquitin editing enzyme) is essential for stability and expression of VE-cadherin. Deubiquitinase function of A20 was shown to remove ubiquitin |
https://en.wikipedia.org/wiki/L-2-hydroxyglutarate%20dehydrogenase | In enzymology, an L-2-hydroxyglutarate dehydrogenase () is an enzyme that catalyzes the chemical reaction
(S)-2-hydroxyglutarate + acceptor 2-oxoglutarate + reduced acceptor
Thus, the two substrates of this enzyme are (S)-2-hydroxyglutarate and acceptor, whereas its two products are 2-oxoglutarate and reduced acceptor.
Enzymes which preferentially catalyze the conversion of the (R) stereoisomer of 2-oxoglutarate also exist in both mammals and plants
and are named D-2-hydroxyglutarate dehydrogenase. L-2-hydroxyglutarate is produced by promiscuous action of malate dehydrogenase on 2-oxoglutarate; L-2-hydroxyglutarate dehydrogenase is an example of a metabolite repair enzyme that oxidizes L-2-hydroxyglutarate back to 2-oxoglutarate.
Nomenclature
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is (S)-2-hydroxyglutarate:acceptor 2-oxidoreductase. Other names in common use include:
(S)-2-hydroxyglutarate:(acceptor) 2-oxidoreductase
alpha-hydroxyglutarate dehydrogenase
alpha-hydroxyglutarate dehydrogenase (NAD specific)
alpha-hydroxyglutarate oxidoreductase
alpha-ketoglutarate reductase
hydroxyglutaric dehydrogenase
L-alpha-hydroxyglutarate dehydrogenase
L-alpha-hydroxyglutarate:NAD 2-oxidoreductase
Clinical significance
Deficiency in this enzyme in humans (L2HGDH) or in the model plant Arabidopsis thaliana (At3g56840) leads to accumulati |
https://en.wikipedia.org/wiki/GLB1 | Galactosidase, beta 1, also known as GLB1, is a protein which in humans is encoded by the GLB1 gene.
The GLB1 protein is a beta-galactosidase that cleaves the terminal beta-galactose from ganglioside substrates and other glycoconjugates. The GLB1 gene also encodes an elastin binding protein.
In corn (Zea mays), Glb1 is a gene coding for the storage protein globulin.
Clinical significance
GM1-gangliosidosis is a lysosomal storage disease that can be caused by a deficiency of β-galactosidase (GLB1). Some cases of Morquio syndrome B have been shown to be due to GLP1 mutations that cause patients to have abnormal elastic fibers.
Elastin receptor
The RNA transcript of the GLB1 gene is alternatively spliced and produces 2 mRNAs. The 2.5-kilobase transcript encodes the beta-galactosidase enzyme of 677 amino acids. The alternative 2.0-kb mRNA encodes a beta-galactosidase-related protein (S-Gal) that is only 546 amino acids long and that has no enzymatic activity. The S-Gal protein does bind elastin and fragments of elastin that are generated by proteolysis.
The S-Gal protein is a peripheral membrane protein that functions as part of an elastin receptor complex on the surface of cells. The elastin receptor complex includes S-Gal, neuraminidase and Cathepsin A. When elastin-derived peptides bind to the S-Gal protein then the associated neuraminidase enzyme activity is activated and responding cells can have altered signal transduction involving extracellular signal-regulated k |
https://en.wikipedia.org/wiki/2-oxo-acid%20reductase | In enzymology, a 2-oxo-acid reductase () is an enzyme that catalyzes the chemical reaction
a (2R)-hydroxy-carboxylate + acceptor a 2-oxo-carboxylate + reduced acceptor
Thus, the two substrates of this enzyme are (2R)-hydroxy-carboxylate and acceptor, whereas its two products are 2-oxo-carboxylate and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is (2R)-hydroxy-carboxylate:acceptor oxidoreductase. Other names in common use include (2R)-hydroxycarboxylate-viologen-oxidoreductase, HVOR, and 2-oxoacid reductase.
References
EC 1.1.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-hydroxycyclohexanone%20dehydrogenase | In enzymology, a 3-hydroxycyclohexanone dehydrogenase () is an enzyme that catalyzes the chemical reaction
3-hydroxycyclohexanone + acceptor cyclohexane-1,3-dione + reduced acceptor
Thus, the two substrates of this enzyme are 3-hydroxycyclohexanone and acceptor, whereas its two products are cyclohexane-1,3-dione and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is 3-hydroxycyclohexanone:acceptor 1-oxidoreductase.
References
EC 1.1.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/NUP98 | Nuclear pore complex protein Nup98-Nup96 is a protein that in humans is encoded by the NUP98 gene.
Function
Signal-mediated nuclear import and export proceed through the nuclear pore complex (NPC), which is composed of approximately 30 unique proteins collectively known as nucleoporins. The 98 kD nucleoporin is generated through a biogenesis pathway that involves synthesis and proteolytic cleavage of a 186 kD precursor protein. This cleavage results in the 98 kD nucleoporin as well as a 96 kD nucleoporin, both of which are localized to the nucleoplasmic side of the NPC. Rat studies show that the 98 kD nucleoporin functions as one of several docking site nucleoporins of transport substrates. The human gene has been shown to fuse to several genes following chromosome translocations in acute myelogenous leukemia (AML) and T-cell acute lymphocytic leukemia (T-ALL). This gene is one of several genes located in the imprinted gene domain of 11p15.5, an important tumor-suppressor gene region. Alterations in this region have been associated with the Beckwith-Wiedemann syndrome, Wilms tumor, rhabdomyosarcoma, adrenocortical carcinoma, and lung, ovarian, and breast cancer. Alternative splicing of this gene results in several transcript variants; however, not all variants have been fully described.
Interactions
NUP98 has been shown to interact with:
CREB-binding protein,
KPNB1,
NUP88,
RAE1, and
TNPO2.
References
Further reading
Nu |
https://en.wikipedia.org/wiki/4-hydroxymandelate%20oxidase | In enzymology, a 4-hydroxymandelate oxidase () is an enzyme that catalyzes the chemical reaction
(S)-2-hydroxy-2-(4-hydroxyphenyl)acetate + O2 4-hydroxybenzaldehyde + CO2 + H2O2
Thus, the two substrates of this enzyme are (S)-2-hydroxy-2-(4-hydroxyphenyl)acetate and O2, whereas its 3 products are 4-hydroxybenzaldehyde, CO2, and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is (S)-2-hydroxy-2-(4-hydroxyphenyl)acetate:oxygen 1-oxidoreductase. This enzyme is also called L-4-hydroxymandelate oxidase (decarboxylating). It has 2 cofactors: FAD, and Manganese.
References
EC 1.1.3
Flavoproteins
Manganese enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Alcohol%20dehydrogenase%20%28acceptor%29 | In enzymology, an alcohol dehydrogenase (acceptor) () is an enzyme that catalyzes the chemical reaction
a primary alcohol + acceptor an aldehyde + reduced acceptor
Thus, the two substrates of this enzyme are primary alcohol and acceptor, whereas its two products are aldehyde and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is alcohol:acceptor oxidoreductase. Other names in common use include primary alcohol dehydrogenase, MDH, quinohemoprotein alcohol dehydrogenase, quinoprotein alcohol dehydrogenase, quinoprotein ethanol dehydrogenase, and alcohol:(acceptor) oxidoreductase. This enzyme participates in 5 metabolic pathways: glycolysis / gluconeogenesis, 1,2-dichloroethane degradation, propanoate metabolism, butanoate metabolism, and methane metabolism. It employs one cofactor, PQQ.
Structural studies
As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , and .
See also
Alcohol dehydrogenase
References
EC 1.1.99
Pyrroloquinoline quinone enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Alcohol%20oxidase | In enzymology, an alcohol oxidase () is an enzyme that catalyzes the chemical reaction
a primary alcohol + O2 an aldehyde + H2O2
Thus, the two substrates of this enzyme are primary alcohol and O2, whereas its two products are aldehyde and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of the donor with oxygen as the acceptor. It employs one cofactor, FAD.
Name
The systematic name of this enzyme class is alcohol:oxygen oxidoreductase. This enzyme is also called methanol oxidase and ethanol oxidase. Sometimes, this enzyme is called short-chain alcohol oxidase (SCAO) to differentiate it from long-chain-alcohol oxidase (LCAO), aryl-alcohol oxidase (AAO) and secondary-alcohol oxidase (SAO).
Reaction
Alcohol oxidases catalyzes the oxidation of primary alcohols to their corresponding aldehydes. Unlike alcohol dehydrogenases, they are unable to catalyze the reverse reaction. This is reflected in their cofactor as well—unlike alcohol dehydrogenases, which use NAD+, alcohol oxidases use FAD. SCAO is capable of oxidizing alcohols with up to 8 carbons, but their primary substrates are methanol and ethanol.
Known inhibitors of this enzyme include H2O2, Cu2+, phenanthroline, acetamide, potassium cyanide, or cyclopropanone.
Properties
SCAO is an intracellular enzyme. Its common source are fungi and yeasts, but it has also been shown to be present in mollusks.
It appears as an octameric protein, except for SCAO from A. ochr |
https://en.wikipedia.org/wiki/Alkan-1-ol%20dehydrogenase%20%28acceptor%29 | In enzymology, an alkan-1-ol dehydrogenase (acceptor) () is an enzyme that catalyzes the chemical reaction
primary alcohol + acceptor aldehyde + reduced acceptor
Thus, the two substrates of this enzyme are primary alcohol and acceptor, whereas its two products are aldehyde and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is alkan-1-ol:acceptor oxidoreductase. Other names in common use include polyethylene glycol dehydrogenase, and alkan-1-ol:(acceptor) oxidoreductase. This enzyme participates in fatty acid metabolism. It employs one cofactor, PQQ.
References
EC 1.1.99
Pyrroloquinoline quinone enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aryl-alcohol%20oxidase | In enzymology, an aryl-alcohol oxidase () is an enzyme that catalyzes the chemical reaction
an aromatic primary alcohol + O2 an aromatic aldehyde + H2O2
Thus, the two substrates of this enzyme are aromatic primary alcohol and O2, whereas its two products are aromatic aldehyde and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is aryl-alcohol:oxygen oxidoreductase. Other names in common use include aryl alcohol oxidase, veratryl alcohol oxidase, and arom. alcohol oxidase.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 1.1.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Catechol%20oxidase%20%28dimerizing%29 | In enzymology, a catechol oxidase (dimerizing) () is an enzyme that catalyzes the chemical reaction
4 catechol + 3 O2 2 dibenzo[1,4]dioxin-2,3-dione + 6 H2O
Thus, the two substrates of this enzyme are catechol and O2, whereas its two products are [[dibenzo[1,4]dioxin-2,3-dione]] and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is catechol:oxygen oxidoreductase (dimerizing).
References
EC 1.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cellobiose%20dehydrogenase%20%28acceptor%29 | In enzymology, a cellobiose dehydrogenase (acceptor) () is an enzyme that catalyzes the chemical reaction
cellobiose + acceptor cellobiono-1,5-lactone + reduced acceptor
Thus, the two substrates of this enzyme are cellobiose and acceptor, whereas its two products are cellobiono-1,5-lactone and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is cellobiose:acceptor 1-oxidoreductase. Other names in common use include cellobiose dehydrogenase, cellobiose oxidoreductase, Phanerochaete chrysosporium cellobiose oxidoreductase, CBOR, cellobiose oxidase, cellobiose:oxygen 1-oxidoreductase, CDH, and cellobiose:(acceptor) 1-oxidoreductase. It employs sometimes one cofactor, FAD, but in most cases both a heme and a FAD located in separate domains. It makes the enzyme to one of the more complex extracellular oxidoreductases. It is produced by wood degrading organisms.
Structural studies
To date, structures of the separated dehydrogenase (DH) and cytochrome (CYT) domains were reported (PDB accession codes and ). In 2015, full-length structures of the enzyme were resolved for CDH from Crassicarpon hotsonii syn. Myriococcum thermophilum (ChCDH, PDB accession code 4QI6) and CDH from Neurospora crassa (NcCDH, PDB accession code 4QI7).
The mobility of the CYT domain prevented for a long time the crystallization and X-ray structure elucidation of |
https://en.wikipedia.org/wiki/Cholesterol%20oxidase | In enzymology, a cholesterol oxidase () is an enzyme that catalyzes the chemical reaction
cholesterol + O2 cholest-4-en-3-one + H2O2
Thus, the two substrates of this enzyme are cholesterol and O2, whereas its two products are cholest-4-en-3-one and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is cholesterol:oxygen oxidoreductase. Other names in common use include cholesterol- O2 oxidoreductase, 3beta-hydroxy steroid oxidoreductase, and 3beta-hydroxysteroid:oxygen oxidoreductase. This enzyme participates in bile acid biosynthesis.
The substrate-binding domain found in some bacterial cholesterol oxidases is composed of an eight-stranded mixed beta-pleated sheet and six alpha-helices. This domain is positioned over the isoalloxazine ring system of the FAD cofactor bound by the FAD-binding domain and forms the roof of the active site cavity, allowing for catalysis of oxidation and isomerisation of cholesterol to cholest-4-en-3-one.
Structural studies
As of late 2007, 14 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , and .
References
Further reading
Protein domains
EC 1.1.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Choline%20dehydrogenase | In enzymology, a choline dehydrogenase () is an enzyme that catalyzes the chemical reaction
choline + acceptor betaine aldehyde + reduced acceptor
Thus, the two substrates of this enzyme are choline and acceptor, whereas its two products are betaine aldehyde and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is choline:acceptor 1-oxidoreductase. Other names in common use include choline oxidase, choline-cytochrome c reductase, choline:(acceptor) oxidoreductase, and choline:(acceptor) 1-oxidoreductase. This enzyme participates in glycine, serine and threonine metabolism. It employs one cofactor, PQQ.
References
EC 1.1.99
Pyrroloquinoline quinone enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Choline%20oxidase | In enzymology, a choline oxidase () is an enzyme that catalyzes the chemical reaction
choline + O2 betaine aldehyde + H2O2
Thus, the two substrates of this enzyme are choline and O2, whereas its two products are betaine aldehyde and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is choline:oxygen 1-oxidoreductase. This enzyme participates in glycine, serine, and threonine metabolism. It employs one cofactor, FAD.
References
EC 1.1.3
Flavoproteins
Enzymes of known structure |
https://en.wikipedia.org/wiki/TPM1 | Tropomyosin alpha-1 chain is a protein that in humans is encoded by the TPM1 gene. This gene is a member of the tropomyosin (Tm) family of highly conserved, widely distributed actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells.
Structure
Tm is a 32.7 kDa protein composed of 284 amino acids. Tm is a flexible protein homodimer or heterodimer composed of two alpha-helical chains, which adopt a bent coiled coil conformation to wrap around the seven actin molecules in a functional unit of muscle. It is polymerized end to end along the two grooves of actin filaments and provides stability to the filaments. Human striated muscles express protein from the TPM1 (α-Tm), TPM2 (β-Tm) and TPM3 (γ-Tm) genes, with α-Tm being the predominant isoform in striated muscle. In human cardiac muscle the ratio of α-Tm to β-Tm is roughly 5:1.
Function
Tm functions in association with the troponin complex to regulate the calcium-dependent interaction of actin and myosin during muscle contraction. Tm molecules are arranged head-to-tail along the actin thin filament, and are a key component in cooperative activation of muscle. A three state model has been proposed by McKillop and Geeves, which describes the positions of Tm during a cardiac cycle. The blocked (B) state occurs in diastole when intracellular calcium is low and Tm blocks the myosin binding site on actin. The closed (C) state is when Tm is positioned on the inn |
https://en.wikipedia.org/wiki/D-2-hydroxy-acid%20dehydrogenase | In enzymology, a D-2-hydroxy-acid dehydrogenase () is an enzyme that catalyzes the chemical reaction
(R)-lactate + acceptor pyruvate + reduced acceptor
Thus, the two substrates of this enzyme are (R)-lactate and acceptor, whereas its two products are pyruvate and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is (R)-2-hydroxy-acid:acceptor 2-oxidoreductase. Other names in common use include D-2-hydroxy acid dehydrogenase, and (R)-2-hydroxy-acid:(acceptor) 2-oxidoreductase. It has 2 cofactors: FAD, and Zinc.
References
EC 1.1.99
Flavoproteins
Zinc enzymes
Enzymes of unknown structure
Protein families |
https://en.wikipedia.org/wiki/D-arabinono-1%2C4-lactone%20oxidase | In enzymology, a D-arabinono-1,4-lactone oxidase () is an enzyme that catalyzes the chemical reaction
D-arabinono-1,4-lactone + O2 D-erythro-ascorbate + H2O2
Thus, the two substrates of this enzyme are D-arabinono-1,4-lactone and O2, whereas its two products are D-erythro-ascorbate and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is D-arabinono-1,4-lactone:oxygen oxidoreductase. It employs one cofactor, FAD.
References
EC 1.1.3
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dehydrogluconate%20dehydrogenase | In enzymology, a dehydrogluconate dehydrogenase () is an enzyme that catalyzes the chemical reaction
2-dehydro-D-gluconate + acceptor 2,5-didehydro-D-gluconate + reduced acceptor
Thus, the two substrates of this enzyme are 2-dehydro-D-gluconate and acceptor, whereas its two products are 2,5-didehydro-D-gluconate and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is 2-dehydro-D-gluconate:acceptor 2-oxidoreductase. Other names in common use include ketogluconate dehydrogenase, alpha-ketogluconate dehydrogenase, 2-keto-D-gluconate dehydrogenase, and 2-oxogluconate dehydrogenase. It has 2 cofactors: FAD, and Flavoprotein.
References
EC 1.1.99
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-lactate%20dehydrogenase%20%28cytochrome%29 | In enzymology, a D-lactate dehydrogenase (cytochrome) () is an enzyme that catalyzes the chemical reaction
(D)-lactate + 2 ferricytochrome c pyruvate + 2 ferrocytochrome c
Thus, the two substrates of this enzyme are (D)-lactate and ferricytochrome c, whereas its two products are pyruvate and ferrocytochrome c.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is (D)-lactate:ferricytochrome-c 2-oxidoreductase. Other names in common use include lactic acid dehydrogenase, D-lactate (cytochrome) dehydrogenase, cytochrome-dependent D-(−)-lactate dehydrogenase, D-lactate-cytochrome c reductase, and D-(−)-lactic cytochrome c reductase. This enzyme participates in pyruvate metabolism. It employs one cofactor, FAD. This type of enzyme has been characterized in animals, fungi, bacteria and recently in plants
. It is believed to be important in the detoxification of methylglyoxal through the glyoxylase pathway
References
Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 557-565.
EC 1.1.2
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-lactate%20dehydrogenase%20%28cytochrome%20c-553%29 | In enzymology, a D-lactate dehydrogenase (cytochrome c-553) () is an enzyme that catalyzes the chemical reaction
(R)-lactate + 2 ferricytochrome c-553 pyruvate + 2 ferrocytochrome c-553
Thus, the two substrates of this enzyme are (R)-lactate and ferricytochrome c-553, whereas its two products are pyruvate and ferrocytochrome c-553.
This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-OH group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is (R)-lactate:ferricytochrome-c-553 2-oxidoreductase. This enzyme participates in pyruvate metabolism.
References
EC 1.1.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-mannitol%20oxidase | In enzymology, a -mannitol oxidase () is an enzyme that catalyzes the chemical reaction
mannitol + O2 mannose + H2O2
Thus, the two substrates of this enzyme are mannitol and O2, whereas its two products are mannose and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is mannitol:oxygen oxidoreductase (cyclizing). Other names in common use include mannitol oxidase, and D-arabitol oxidase.
References
EC 1.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-sorbitol%20dehydrogenase%20%28acceptor%29 | In enzymology, a D-sorbitol dehydrogenase (acceptor) () is an enzyme that catalyzes the chemical reaction
D-sorbitol + acceptor L-sorbose + reduced acceptor
Thus, the two substrates of this enzyme are D-sorbitol and acceptor, whereas its two products are L-sorbose and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is D-sorbitol:acceptor 1-oxidoreductase. This enzyme is also called D-sorbitol:(acceptor) 1-oxidoreductase. This enzyme participates in fructose and mannose metabolism. It employs one cofactor, FAD.
References
EC 1.1.99
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ecdysone%20oxidase | In enzymology, an ecdysone oxidase () is an enzyme that catalyzes the chemical reaction
ecdysone + O2 3-dehydroecdysone + H2O2
Thus, the two substrates of this enzyme are ecdysone and O2, whereas its two products are 3-dehydroecdysone and H2O2.
This enzyme may or may not belong to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is ecdysone:oxygen 3-oxidoreductase. This enzyme might also be called beta-ecdysone oxidase.
References
EC 1.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Fructose%205-dehydrogenase | In enzymology, a fructose 5-dehydrogenase () is an enzyme that catalyzes the chemical reaction
D-fructose + acceptor 5-dehydro-D-fructose + reduced acceptor
Thus, the two substrates of this enzyme are D-fructose and acceptor, whereas its two products are 5-dehydro-D-fructose and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is D-fructose:acceptor 5-oxidoreductase. Other names in common use include fructose 5-dehydrogenase (acceptor), D-fructose dehydrogenase, and D-fructose:(acceptor) 5-oxidoreductase.
References
EC 1.1.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Gluconate%202-dehydrogenase%20%28acceptor%29 | In enzymology, a gluconate 2-dehydrogenase (acceptor) () is an enzyme that catalyzes the chemical reaction
D-gluconate + acceptor 2-dehydro-D-gluconate + reduced acceptor
Thus, the two substrates of this enzyme are D-gluconate and acceptor, whereas its two products are 2-dehydro-D-gluconate and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is D-gluconate:acceptor 2-oxidoreductase. Other names in common use include gluconate oxidase, gluconate dehydrogenase, gluconic dehydrogenase, D-gluconate dehydrogenase, gluconic acid dehydrogenase, 2-ketogluconate reductase, D-gluconate dehydrogenase, 2-keto-D-gluconate-yielding, and D-gluconate:(acceptor) 2-oxidoreductase. This enzyme participates in pentose phosphate pathway. It employs one cofactor, FAD.
References
EC 1.1.99
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glucose%201-dehydrogenase%20%28FAD%2C%20quinone%29 | In enzymology, a glucose 1-dehydrogenase (FAD, quinone) () is an enzyme that catalyzes the chemical reaction
D-glucose + a quinone D-glucono-1,5-lactone + a quinol
Thus, the two substrates of this enzyme are D-glucose and a quinone, whereas its two products are D-glucono-1,5-lactone and a quinol.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is D-glucose:acceptor 1-oxidoreductase. Other names in common use include glucose dehydrogenase (Aspergillus), glucose dehydrogenase (decarboxylating), and D-glucose:(acceptor) 1-oxidoreductase. This enzyme participates in pentose phosphate pathway. It employs one cofactor, FAD.
References
EC 1.1.99
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glucose-fructose%20oxidoreductase | In enzymology, a glucose-fructose oxidoreductase () is an enzyme that catalyzes the chemical reaction
D-glucose + D-fructose D-gluconolactone + D-glucitol
Thus, the two substrates of this enzyme are D-glucose and D-fructose, whereas its two products are D-gluconolactone and D-glucitol.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is D-glucose:D-fructose oxidoreductase.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
References
EC 1.1.99
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glucoside%203-dehydrogenase | In enzymology, a glucoside 3-dehydrogenase () is an enzyme that catalyzes the chemical reaction
sucrose + acceptor 3-dehydro-alpha-D-glucosyl-beta-D-fructofuranoside + reduced acceptor
Thus, the two substrates of this enzyme are sucrose and acceptor, whereas its two products are 3-dehydro-alpha-D-glucosyl-beta-D-fructofuranoside and reduced acceptor.
This enzyme participates in galactose metabolism and starch and sucrose metabolism. It employs one cofactor, FAD.
Nomenclature
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is D-aldohexoside:acceptor 3-oxidoreductase. Other names in common use include D-glucoside 3-dehydrogenase, D-aldohexopyranoside dehydrogenase, D-aldohexoside:cytochrome c oxidoreductase, D-glucoside 3-dehydrogenase, hexopyranoside-cytochrome c oxidoreductase, and D-aldohexoside:(acceptor) 3-oxidoreductase.
References
EC 1.1.99
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycerol-3-phosphate%20oxidase | In enzymology, a glycerol-3-phosphate oxidase () is an enzyme that catalyzes the chemical reaction
sn-glycerol 3-phosphate + O2 glycerone phosphate + H2O2
Thus, the two substrates of this enzyme are sn-glycerol 3-phosphate and O2, whereas its two products are dihydroxyacetone phosphate (DHAP) and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is sn-glycerol-3-phosphate:oxygen 2-oxidoreductase. Other names in common use include glycerol phosphate oxidase, glycerol-1-phosphate oxidase, glycerol phosphate oxidase, L-alpha-glycerophosphate oxidase, alpha-glycerophosphate oxidase, and L-alpha-glycerol-3-phosphate oxidase. This enzyme participates in glycerophospholipid metabolism. It employs one cofactor, FAD.
References
EC 1.1.3
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycerol%20dehydrogenase%20%28acceptor%29 | In enzymology, a glycerol dehydrogenase (acceptor) () is an enzyme that catalyzes the chemical reaction
glycerol + acceptor glycerone + reduced acceptor
Thus, the two substrates of this enzyme are glycerol and acceptor, whereas its two products are glycerone and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is glycerol:acceptor 1-oxidoreductase. This enzyme is also called glycerol:(acceptor) 1-oxidoreductase. It employs one cofactor, PQQ.
References
EC 1.1.99
Pyrroloquinoline quinone enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/CCR1 | C-C chemokine receptor type 1 is a protein that in humans is encoded by the CCR1 gene.
CCR1 has also recently been designated CD191 (cluster of differentiation 191).
Function
This gene encodes a member of the beta chemokine receptor family, which belongs to G protein-coupled receptors. The ligands of this receptor include CCL3 (or MIP-1 alpha), CCL5 (or RANTES), CCL7 (or MCP-3), and CCL23 (or MPIF-1). Chemokines and their receptors, which mediate signal transduction, are critical for the recruitment of effector immune cells to the site of inflammation. Knockout studies of the mouse homolog suggested the roles of this gene in host protection from inflammatory response, and susceptibility to virus and parasite. This gene and other chemokine receptor genes, including CCR2, CCRL2, CCR3, CCR5 and CXCR1, are found to form a gene cluster on chromosome 3p.
Interactions
CCR1 has been shown to interact with CCL5.
References
Further reading
External links
Chemokine receptors
Clusters of differentiation |
https://en.wikipedia.org/wiki/Glycolate%20dehydrogenase | In enzymology, a glycolate dehydrogenase () is an enzyme that catalyzes the chemical reaction
glycolate + acceptor glyoxylate + reduced acceptor
Thus, the two substrates of this enzyme are glycolate and acceptor, whereas its two products are glyoxylate and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is glycolate:acceptor 2-oxidoreductase. Other names in common use include glycolate oxidoreductase, glycolic acid dehydrogenase, and glycolate:(acceptor) 2-oxidoreductase. This enzyme participates in glyoxylate and dicarboxylate metabolism.
References
EC 1.1.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Hexose%20oxidase | In enzymology, a hexose oxidase () is an enzyme that catalyzes the chemical reaction
D-glucose + O2 D-glucono-1,5-lactone + H2O2
Thus, the two substrates of this enzyme are D-glucose and O2, whereas its two products are D-glucono-1,5-lactone and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is D-hexose:oxygen 1-oxidoreductase. This enzyme participates in pentose phosphate pathway. It employs one cofactor, copper.
References
EC 1.1.3
Copper enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Hydroxyacid-oxoacid%20transhydrogenase | In enzymology, a hydroxyacid-oxoacid transhydrogenase () is an enzyme that catalyzes the chemical reaction
(S)-3-hydroxybutanoate + 2-oxoglutarate acetoacetate + (R)-2-hydroxyglutarate
Thus, the two substrates of this enzyme are (S)-3-hydroxybutanoate and 2-oxoglutarate, whereas its two products are acetoacetate and (R)-2-hydroxyglutarate.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is (S)-3-hydroxybutanoate:2-oxoglutarate oxidoreductase. This enzyme is also called transhydrogenase, hydroxy acid-oxo acid.
See also
D2HGDH
L2HGDH
2-hydroxyglutarate synthase
2-hydroxyglutarate dehydrogenase
Alpha-Hydroxyglutaric acid
2-Hydroxyglutaric aciduria
References
EC 1.1.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Hydroxyphytanate%20oxidase | In enzymology, a hydroxyphytanate oxidase () is an enzyme that catalyzes the chemical reaction
L-2-hydroxyphytanate + O2 2-oxophytanate + H2O2
Thus, the two substrates of this enzyme are L-2-hydroxyphytanate and O2, whereas its two products are 2-oxophytanate and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is L-2-hydroxyphytanate:oxygen 2-oxidoreductase. This enzyme is also called L-2-hydroxyphytanate:oxygen 2-oxidoreductase.
References
EC 1.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/E2F4 | Transcription factor E2F4 is a protein that in humans is encoded by the E2F4 gene.
Function
The protein encoded by this gene is a member of the E2F family of transcription factors. The E2F family plays a crucial role in the control of cell cycle and action of tumor suppressor proteins and is also a target of the transforming proteins of small DNA tumor viruses. This protein binds to all three of the tumor suppressor proteins pRB, p107 and p130, but with higher affinity to the last two. It plays an important role in the suppression of proliferation-associated genes, and its gene mutation and increased expression may be associated with human cancer.
Structure
The E2F proteins contain several evolutionally conserved domains found in most members of the family. These domains include a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids (Asp + Glu), and a tumor suppressor protein association domain which is embedded within the transactivation domain.
Interactions
E2F4 has been shown to interact with Smad3.
See also
E2F
References
Further reading
External links
PDBe-KB provides an overview of all the structure information available in the PDB for Human Transcription factor E2F4
Transcription factors |
https://en.wikipedia.org/wiki/Lactate%E2%80%94malate%20transhydrogenase | In enzymology, a lactate—malate transhydrogenase () is an enzyme that catalyzes the chemical reaction
(S)-lactate + oxaloacetate pyruvate + malate
Thus, the two substrates of this enzyme are (S)-lactate and oxaloacetate, whereas its two products are pyruvate and malate.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is (S)-lactate:oxaloacetate oxidoreductase. This enzyme is also called malate-lactate transhydrogenase. This enzyme participates in pyruvate metabolism. It employs one cofactor, nicotinamide D-ribonucleotide.
References
Further reading
EC 1.1.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Long-chain-alcohol%20oxidase | Long-chain alcohol oxidase is one of two enzyme classes that oxidize long-chain or fatty alcohols to aldehydes. It has been found in certain Candida yeast, where it participates in omega oxidation of fatty acids to produce acyl-CoA for energy or industrial use, as well as in other fungi, plants, and bacteria.
Mechanism
Long-chain alcohol oxidase catalyzes the chemical reaction
long-chain alcohol + O2 2 long-chain aldehyde + 2 H2O2
Thus, the two substrates of this enzyme are long-chain/fatty alcohol and O2, whereas its two products are long-chain/fatty aldehyde and hydrogen peroxide.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is long-chain-alcohol:oxygen oxidoreductase. Other names in common use include long-chain fatty alcohol oxidase, fatty alcohol oxidase, fatty alcohol:oxygen oxidoreductase, and long-chain fatty acid oxidase.
Structure
The enzyme is an octamer of ~46kD subunits (except in C. tropicalis, in which it is a dimer of subunits ~70kD). It is a Cytochrome c oxidase containing a covalently-bound heme group using the Cys-X-X-Cys-His motif. It also contains flavin to assist in oxidation-reduction. The enzyme is bound to the endoplasmic reticulum membrane.
Long-chain fatty alcohol oxidases vary between species in their specificity; some species have multiple different alcohol oxidases. They generally have a broad range of subs |
https://en.wikipedia.org/wiki/L-sorbose%20oxidase | In enzymology, a L-sorbose oxidase () is an enzyme that catalyzes the chemical reaction
L-sorbose + O2 5-dehydro-D-fructose + H2O2
Thus, the two substrates of this enzyme are L-sorbose and O2, whereas its two products are 5-dehydro-D-fructose and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is L-sorbose:oxygen 5-oxidoreductase.
References
EC 1.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Malate%20dehydrogenase%20%28quinone%29 | In enzymology, a malate dehydrogenase (quinone) (), formerly malate dehydrogenase (acceptor) (EC 1.1.99.16), is an enzyme that catalyzes the chemical reaction
(S)-malate + a quinone oxaloacetate + reduced quinone
Thus, the two substrates of this enzyme are (S)-malate and a quinone, whereas its two products are oxaloacetate and reduced quinone.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with a quinone as acceptor. The systematic name of this enzyme class is (S)-malate:quinone oxidoreductase. Other names in common use include FAD-dependent malate-vitamin K reductase, malate-vitamin K reductase, and (S)-malate:(quinone) oxidoreductase. This enzyme participates in pyruvate metabolism. It employs one cofactor, FAD.
References
EC 1.1.5
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Malate%20oxidase | In enzymology, a malate oxidase () is an enzyme that catalyzes the chemical reaction
(S)-malate + O2 oxaloacetate + H2O2
Thus, the two substrates of this enzyme are (S)-malate and O2, whereas its two products are oxaloacetate and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is (S)-malate:oxygen oxidoreductase. Other names in common use include FAD-dependent malate oxidase, malic oxidase, and malic dehydrogenase II. This enzyme participates in pyruvate metabolism. It employs one cofactor, FAD. The enzyme is commonly localized on the inner surface of the cytoplasmic membrane although another family member (malate dehydrogenase 2 (NAD)) is found in the mitochondrial matrix.
Mechanisms
Malate oxidase belongs to the family of malate dehydrogenases (EC 1.1.1.37) (MDH) that reversibly catalyze the oxidation of malate to oxaloacetate by means of the reduction of a cofactor. The most common isozymes of malate dehydrogenase use NAD+ or NADP+ as a cofactor to accept electrons and protons.
However, the main difference of malate oxidase is that it normally employs FAD as redox partner as alternative. Contrary to pyridine based NAD+/NADP+, FAD comprises a quinone moiety, which is reduced by the forward reaction. FAD is thereby converted to FADH2. In this case, malate oxidase is qualified as malate dehydrogenase (quinone).
In mutant strains of Esc |
https://en.wikipedia.org/wiki/Mannitol%20dehydrogenase%20%28cytochrome%29 | In enzymology, a mannitol dehydrogenase (cytochrome) () is an enzyme that catalyzes the chemical reaction
D-mannitol + ferricytochrome c D-fructose + ferrocytochrome c
Thus, the two substrates of this enzyme are D-mannitol and ferricytochrome c, whereas its two products are D-fructose and ferrocytochrome c.
This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-OH group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is D-mannitol:ferricytochrome-c 2-oxidoreductase. This enzyme is also called polyol dehydrogenase. This enzyme participates in pentose and glucuronate interconversions and fructose and mannose metabolism
References
EC 1.1.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-acylhexosamine%20oxidase | In enzymology, a N-acylhexosamine oxidase () is an enzyme that catalyzes the chemical reaction
N-acetyl-D-glucosamine + O2 N-acetyl-D-glucosaminate + H2O2
Thus, the two substrates of this enzyme are N-acetyl-D-glucosamine and O2, whereas its two products are N-acetyl-D-glucosaminate and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is N-acyl-D-hexosamine:oxygen 1-oxidoreductase. Other names in common use include N-acyl-D-hexosamine oxidase, and N-acyl-beta-D-hexosamine:oxygen 1-oxidoreductase.
References
EC 1.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Polyvinyl-alcohol%20dehydrogenase%20%28acceptor%29 | In enzymology, a polyvinyl-alcohol dehydrogenase (acceptor) () is an enzyme that catalyzes the chemical reaction
polyvinyl alcohol + acceptor oxidized polyvinyl alcohol + reduced acceptor
Thus, the two substrates of this enzyme are polyvinyl alcohol and acceptor, whereas its two products are oxidized polyvinyl alcohol and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is polyvinyl-alcohol:acceptor oxidoreductase. Other names in common use include PVA dehydrogenase, and polyvinyl-alcohol:(acceptor) oxidoreductase. It employs one cofactor, PQQ.
References
EC 1.1.99
Pyrroloquinoline quinone enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Polyvinyl-alcohol%20oxidase | In enzymology, a polyvinyl-alcohol oxidase () is an enzyme that catalyzes the chemical reaction
polyvinyl alcohol + O2 oxidized polyvinyl alcohol + H2O2
Thus, the two substrates of this enzyme are polyvinyl alcohol and O2, whereas its two products are oxidized polyvinyl alcohol and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is polyvinyl-alcohol:oxygen oxidoreductase. Other names in common use include dehydrogenase, polyvinyl alcohol, and PVA oxidase.
References
EC 1.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pyranose%20oxidase | In enzymology, a pyranose oxidase () is an enzyme that catalyzes the chemical reaction
D-glucose + O2 2-dehydro-D-glucose + H2O2
Thus, the two substrates of this enzyme are D-glucose and O2, whereas its two products are 2-dehydro-D-glucose and H2O2.
Pyranose oxidase is able to oxidize D-xylose, L-sorbose, D-galactose, and D-glucono-1,5-lactone, which have the same ring conformation and configuration at C-2, C-3 and C-4.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is pyranose:oxygen 2-oxidoreductase. Other names in common use include glucose 2-oxidase, and pyranose-2-oxidase. This enzyme participates in pentose phosphate pathway. It employs one cofactor, FAD.
Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , and .
Use in biosensors
Recently, pyranose oxidase has been gaining on popularity within biosensors. Unlike glucose oxidase, it can produce higher power output, given that it is not glycosylated, has more favorable value of Michaelis-Menten constants, and can catalytically convert both anomers of glucose. It reacts with a wider range of substrates. Pyranose oxidase does not cause an unwanted pH shift. It is also possible to easily express and produce it in high yields using E. coli.
References
Further reading
EC 1.1.3
Flavoproteins
Enzymes of kn |
https://en.wikipedia.org/wiki/Pyridoxine%204-oxidase | In enzymology, a pyridoxine 4-oxidase () is an enzyme that catalyzes the chemical reaction
pyridoxine + O2 pyridoxal + H2O2
Thus, the two substrates of this enzyme are pyridoxine and O2, whereas its two products are pyridoxal and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is pyridoxine:oxygen 4-oxidoreductase. Other names in common use include pyridoxin 4-oxidase, and pyridoxol 4-oxidase. This enzyme participates in vitamin B6 metabolism. It employs one cofactor, FAD.
References
EC 1.1.3
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pyridoxine%205-dehydrogenase | In enzymology, a pyridoxine 5-dehydrogenase () is an enzyme that catalyzes the chemical reaction
pyridoxine + acceptor isopyridoxal + reduced acceptor
Thus, the two substrates of this enzyme are pyridoxine and acceptor, whereas its two products are isopyridoxal and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is pyridoxine:acceptor 5-oxidoreductase. Other names in common use include pyridoxal-5-dehydrogenase, pyridoxol 5-dehydrogenase, pyridoxin 5-dehydrogenase, pyridoxine dehydrogenase, pyridoxine 5'-dehydrogenase, and pyridoxine:(acceptor) 5-oxidoreductase. This enzyme participates in vitamin B6 metabolism. It has 2 cofactors: FAD, and PQQ.
References
EC 1.1.99
Flavoproteins
Pyrroloquinoline quinone enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Importin%20subunit%20alpha-4 | Importin subunit alpha-4 also known as karyopherin subunit alpha-3 is a protein that in humans is encoded by the KPNA3 gene.
The transport of molecules between the nucleus and the cytoplasm in eukaryotic cells is mediated by the nuclear pore complex (NPC) which consists of 60–100 proteins and is probably 120 million daltons in molecular size. Small molecules (up to 70 kD) can pass through the nuclear pore by nonselective diffusion; larger molecules are transported by an active process. Most nuclear proteins contain short basic amino acid sequences known as nuclear localization signals (NLSs). KPNA3, encodes a protein similar to certain nuclear transport proteins of Xenopus and human. The predicted amino acid sequence shows similarity to Xenopus importin, yeast SRP1, and human RCH1 (KPNA2), respectively. The similarities among these proteins suggests that karyopherin alpha-3 may be involved in the nuclear transport system.
Interactions
KPNA3 has been shown to interact with KPNB1.
References
Further reading
Armadillo-repeat-containing proteins |
https://en.wikipedia.org/wiki/Monoamine%20oxidase%20B | Monoamine oxidase B, also known as MAOB, is an enzyme that in humans is encoded by the MAOB gene.
The protein encoded by this gene belongs to the flavin monoamine oxidase family. It is an enzyme located in the outer mitochondrial membrane. It catalyzes the oxidative deamination of biogenic and xenobiotic amines and plays an important role in the catabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues (such as dopamine). This protein preferentially degrades benzylamine and phenethylamine. Similar to monoamine oxidase A (MAOA), it also degrades dopamine [though some new research contradicts this, suggesting that MAOB does not directly degrade dopamine, but is responsible for GABA synthesis].
Structure and Function
Monoamine oxidase B has a hydrophobic bipartite elongated cavity that (for the "open" conformation) occupies a combined volume close to 700 Å3. hMAO-A has a single cavity that exhibits a rounder shape and is larger in volume than the "substrate cavity" of hMAO-B.
The first cavity of hMAO-B has been termed the entrance cavity (290 Å3), the second substrate cavity or active site cavity (~390 Å3) – between both an isoleucine199 side-chain serves as a gate. Depending on the substrate or bound inhibitor, it can exist in either an open or a closed form, which has been shown to be important in defining the inhibitor specificity of hMAO B. At the end of the substrate cavity is the FAD cofactor with sites for favorable amine bin |
https://en.wikipedia.org/wiki/MT-ND4 | MT-ND4 is a gene of the mitochondrial genome coding for the NADH-ubiquinone oxidoreductase chain 4 (ND4) protein. The ND4 protein is a subunit of NADH dehydrogenase (ubiquinone), which is located in the mitochondrial inner membrane and is the largest of the five complexes of the electron transport chain. Variations in the MT-ND4 gene are associated with age-related macular degeneration (AMD), Leber's hereditary optic neuropathy (LHON), mesial temporal lobe epilepsy (MTLE) and cystic fibrosis.
Structure
The MT-ND4 gene is located in human mitochondrial DNA from base pair 10,760 to 12,137. The MT-ND4 gene produces a 52 kDa protein composed of 459 amino acids. MT-ND4 is one of seven mitochondrial genes encoding subunits of the enzyme NADH dehydrogenase (ubiquinone), together with MT-ND1, MT-ND2, MT-ND3, MT-ND4L, MT-ND5, and MT-ND6. Also known as Complex I, this enzyme is the largest of the respiratory complexes. The structure is L-shaped with a long, hydrophobic transmembrane domain and a hydrophilic domain for the peripheral arm that includes all the known redox centres and the NADH binding site. MT-ND4 and the rest of the mitochondrially encoded subunits are the most hydrophobic of the subunits of Complex I and form the core of the transmembrane region.
An unusual feature of the human MT-ND4 gene is the 7-nucleotide gene overlap of its first three codons (5'-ATG CTA AAA-3' coding for amino acids Met-Leu-Lys) with the last three codons of the MT-ND4L gene (5'-CAA TGC TAA-3' |
https://en.wikipedia.org/wiki/Quinoprotein%20glucose%20dehydrogenase | In enzymology, a quinoprotein glucose dehydrogenase () is an enzyme that catalyzes the chemical reaction
D-glucose + ubiquinone D-glucono-1,5-lactone + ubiquinol
Thus, the two substrates of this enzyme are D-glucose and ubiquinone, whereas its two products are D-glucono-1,5-lactone and ubiquinol.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with a quinone or similar compound as acceptor. The systematic name of this enzyme class is D-glucose:ubiquinone oxidoreductase. Other names in common use include D-glucose:(pyrroloquinoline-quinone) 1-oxidoreductase, glucose dehydrogenase (PQQ-dependent), glucose dehydrogenase (pyrroloquinoline-quinone), and quinoprotein D-glucose dehydrogenase. This enzyme participates in pentose phosphate pathway. It employs one cofactor, PQQ.
References
Further reading
EC 1.1.5
Pyrroloquinoline quinone enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28R%29-pantolactone%20dehydrogenase%20%28flavin%29 | In enzymology, a (R)-pantolactone dehydrogenase (flavin) () is an enzyme that catalyzes the chemical reaction
(R)-pantolactone + acceptor 2-dehydropantolactone + reduced acceptor
Thus, the two substrates of this enzyme are (R)-pantolactone and acceptor, whereas its two products are 2-dehydropantolactone and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is (R)-pantolactone:acceptor oxidoreductase (flavin-containing). Other names in common use include 2-dehydropantolactone reductase (flavin), 2-dehydropantoyl-lactone reductase (flavin), and (R)-pantoyllactone dehydrogenase (flavin).
References
EC 1.1.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28S%29-2-hydroxy-acid%20oxidase | In enzymology, an (S)-2-hydroxy-acid oxidase () is an enzyme that catalyzes the chemical reaction
(S)-2-hydroxy acid + O 2-oxo acid + HO
Thus, the two substrates of this enzyme are (S)-2-hydroxy acid and O, whereas its two products are 2-oxo acid and HO.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is (S)-2-hydroxy-acid:oxygen 2-oxidoreductase. Other names in common use include glycolate oxidase, hydroxy-acid oxidase A, hydroxy-acid oxidase B, oxidase, L-2-hydroxy acid, hydroxyacid oxidase A, L-alpha-hydroxy acid oxidase, and L-2-hydroxy acid oxidase. This enzyme participates in glyoxylate and dicarboxylate metabolism. It employs one cofactor, FMN.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
References
EC 1.1.3
Flavoproteins
Enzymes of known structure |
https://en.wikipedia.org/wiki/Secondary-alcohol%20oxidase | In enzymology, a secondary-alcohol oxidase () is an enzyme that catalyzes the chemical reaction
a secondary alcohol + O2 a ketone + H2O2
Thus, the two substrates of this enzyme are secondary alcohol and O2, whereas its two products are ketone and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is secondary-alcohol:oxygen oxidoreductase. Other names in common use include polyvinyl alcohol oxidase, and secondary alcohol oxidase.
References
EC 1.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28S%29-mandelate%20dehydrogenase | In enzymology, (S)-mandelate dehydrogenase () (MDH), is an enzyme that catalyzes the chemical reaction.
Thus, the two substrates of this enzyme are (S)-2-hydroxy-2-phenylacetate and acceptor, whereas its two products are 2-oxo-2-phenylacetate and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors.
The systematic name of this enzyme class is (S)-2-hydroxy-2-phenylacetate:acceptor 2-oxidoreductase.
This enzyme transfers the electron pair from FMNH2 to a component of the electron transport chain, most probably ubiquinone [1,2]. It is part of a metabolic pathway in Pseudomonads that allows these
organisms to utilize mandelic acid, derivatized from the common soil metabolite amygdalin, as the sole source of carbon and energy. The enzyme has a large active-site pocket and preferentially binds
substrates with longer sidechains, e.g. 2-hydroxyoctanoate rather than 2-hydroxybutyrate. It also prefers substrates that, like (S)-mandelate, have beta unsaturation, e.g. (indol-3-yl)glycolate compared with
(indol-3-yl)lactate. Esters of mandelate, such as methyl (S)-mandelate, are also substrates.
Synonyms
(S)-mandelate dehydrogenase is also knows as: L-mandelate dehydrogenase, L-MDH, MDH, SManDH, and SMDH.
References
EC 1.1.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Thiamine%20oxidase | In enzymology, a thiamine oxidase () is an enzyme that catalyzes the chemical reaction
thiamine + 2 O2 + H2O thiamine acetic acid + 2 H2O2
The 3 substrates of this enzyme are thiamine, O2, and H2O, whereas its two products are thiamine acetic acid and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is thiamine:oxygen 5-oxidoreductase. Other names in common use include thiamin dehydrogenase, thiamine dehydrogenase, and thiamin:oxygen 5-oxidoreductase. This enzyme participates in thiamine metabolism. It employs one cofactor, FAD.
References
EC 1.1.3
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Vanillyl-alcohol%20oxidase | In enzymology, a vanillyl-alcohol oxidase () is an enzyme that catalyzes the chemical reaction
+ O2 + H2O2
Thus, the two substrates of this enzyme are vanillyl alcohol and O2, whereas its two products are vanillin and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is vanillyl alcohol:oxygen oxidoreductase. This enzyme is also called 4-hydroxy-2-methoxybenzyl alcohol oxidase. This enzyme participates in 2,4-dichlorobenzoate degradation. It employs one cofactor, FAD.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 1.1.3
Flavoproteins
Enzymes of known structure |
https://en.wikipedia.org/wiki/Vitamin-K-epoxide%20reductase%20%28warfarin-insensitive%29 | In enzymology, a vitamin-K-epoxide reductase (warfarin-insensitive) () is an enzyme that catalyzes the chemical reaction
3-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
Thus, the two substrates of this enzyme are 3-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone and oxidized dithiothreitol, whereas its two products are 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone and 1,4-dithiothreitol.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH or CH2 groups of donor with a disulfide as acceptor. The systematic name of this enzyme class is 3-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone:oxidized-dithi othreitol oxidoreductase.
References
EC 1.17.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/BAG1 | BAG family molecular chaperone regulator 1 is a protein that in humans is encoded by the BAG1 gene.
Function
The oncogene BCL2 is a membrane protein that blocks a step in a pathway leading to apoptosis or programmed cell death. The protein encoded by this gene binds to BCL2 and is referred to as BCL2-associated athanogene. It enhances the anti-apoptotic effects of BCL2 and represents a link between growth factor receptors and anti-apoptotic mechanisms. At least three protein isoforms are encoded by this mRNA through the use of alternative translation initiation sites, including a non-AUG site.
Clinical significance
BAG gene has been implicated in age related neurodegenerative diseases as Alzheimer's. It has been demonstrated that BAG1 and BAG 3 regulate the proteasomal and lysosomal protein elimination pathways, respectively.
Interactions
BAG1 has been shown to interact with:
Androgen receptor,
C-Raf,
Calcitriol receptor,
Glucocorticoid receptor,
HSPA8,
HBEGF,
PPP1R15A,
NR1B1, and
SIAH1.
References
External links
Further reading
Ageing
Oncogenes
Aging-related genes
Aging-related proteins
Co-chaperones |
https://en.wikipedia.org/wiki/Vitamin-K-epoxide%20reductase%20%28warfarin-sensitive%29 | In enzymology, a vitamin-K-epoxide reductase (warfarin-sensitive) () is an enzyme that catalyzes the chemical reaction
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
Thus, the two substrates of this enzyme are 2-methyl-3-phytyl-1,4-naphthoquinone and oxidized dithiothreitol, whereas its two products are 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone and 1,4-dithiothreitol.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH or CH2 groups of donor with a disulfide as acceptor. The systematic name of this enzyme class is 2-methyl-3-phytyl-1,4-naphthoquinone:oxidized-dithiothreitol oxidoreductase. This enzyme participates in biosynthesis of steroids. At least one compound, Warfarin is known to inhibit this enzyme.
References
EC 1.17.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Xylitol%20oxidase | In enzymology, a xylitol oxidase () is an enzyme that catalyzes the chemical reaction
xylitol + O2 xylose + H2O2
Thus, the two substrates of this enzyme are xylitol and O2, whereas its two products are xylose and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is xylitol:oxygen oxidoreductase.
References
EC 1.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dopamine%20receptor%20D1 | {{DISPLAYTITLE:Dopamine receptor D1}}
Dopamine receptor D1, also known as DRD1. It is one of the two types of D1-like receptor family receptors D1 and D5. It is a protein that in humans is encoded by the DRD1 gene.
Tissue distribution
D1 receptors are the most abundant kind of dopamine receptor in the central nervous system.
Northern blot and in situ hybridization show that the mRNA expression of DRD1 is highest in the dorsal striatum (caudate and putamen) and ventral striatum (nucleus accumbens and olfactory tubercle).
Lower levels occur in the basolateral amygdala, cerebral cortex, septum, thalamus, and hypothalamus.
Function
D1 receptors regulate the memory, learning, and the growth of neurons, also is used in the reward system and locomotor activity, mediating some behaviors and modulating dopamine receptor D2-mediated events.
They play a role in addiction by facilitating the gene expression changes that occur in the nucleus accumbens during addiction.
They are Gs/a coupled and can stimulate neurons by indirectly activating cyclic AMP-dependent protein kinase.
Production
The DRD1 gene expresses primarily in the caudate putamen in humans, and in the caudate putamen, the nucleus accumbens and the olfactory tubercle in mouse. Gene expression patterns from the Allen Brain Atlases in mouse and human can be found here.
Ligands
There are a number of ligands selective for the D1 receptors. To date, most of the known ligands are based on dihydrexidine or the prototyp |
https://en.wikipedia.org/wiki/FOXO3 | Forkhead box O3, also known as FOXO3 or FOXO3a, is a human protein encoded by the FOXO3 gene.
Function
FOXO3 belongs to the O subclass of the forkhead family of transcription factors which are characterized by a distinct fork head DNA-binding domain. There are three other FoxO family members in humans, FOXO1, FOXO4 and FOXO6. These transcription factors share the ability to be inhibited and translocated out of the nucleus on phosphorylation by proteins such as Akt/PKB in the PI3K signaling pathway (aside from FOXO6, which may be constitutively nuclear). Other post-translational modifications including acetylation and methylation are seen and can result in increased or altered FOXO3a activity.
The use of FOXO3a knockout mice has revealed a diverse range of functions in both health and disease, namely infertility, lymphoproliferation, adenoma, organ inflammation, metabolism etc.; yet despite the purported importance of FOXO transcription factors in aging, FOXO3A knockout mice do not show an obvious shortening of lifespan or accelerated aging
Apoptosis
Yu & Fellows et al. (2018) demonstrated that FOXO3a activation in vascular smooth muscle cells induces prominent apoptosis and extracellular matrix breakdown in vitro and exacerbates atherosclerosis and vascular remodelling in vivo. Also, these processes were at least partially dependent on MMP-13, as shown by siRNA knockdown and specific pharmacological inhibition. Further experiments also revealed MMP-13 as a novel, bona |
https://en.wikipedia.org/wiki/Parathyroid%20hormone%201%20receptor | Parathyroid hormone/parathyroid hormone-related peptide receptor, also known as parathyroid hormone 1 receptor (PTH1R), is a protein that in humans is encoded by the PTH1R gene. PTH1R functions as a receptor for parathyroid hormone (PTH) and for parathyroid hormone-related protein (PTHrP), also called parathyroid hormone-like hormone (PTHLH).
Function
This "classical" PTH receptor is expressed in high levels in bone and kidney and regulates calcium ion homeostasis through activation of adenylate cyclase and phospholipase C. In bone, it is expressed on the surface of osteoblasts. When the receptor is activated through PTH binding, osteoblasts express RANKL (Receptor Activator of Nuclear Factor kB Ligand), which binds to RANK (Receptor Activator of Nuclear Factor kB) on osteoclasts. This turns on osteoclasts to ultimately increase the resorption rate.
Mechanism
It is a member of the secretin family of G protein-coupled receptors. The activity of this receptor is mediated by Gs G proteins, which activate adenylyl cyclase. Besides this, they also activate the phosphatidylinositol-calcium second messenger system.
Pathology
Defects in this receptor are known to be the cause of Jansen's metaphyseal chondrodysplasia (JMC) and chondrodysplasia Blomstrand type (BOCD) as well as enchondromatosis and primary failure of tooth eruption.
Interactions
Parathyroid hormone 1 receptor has been shown to interact with Sodium-hydrogen exchange regulatory cofactor 2 and Sodium-hydrogen antip |
https://en.wikipedia.org/wiki/RBBP4 | Histone-binding protein RBBP4 (also known as RbAp48, or NURF55) is a protein that in humans is encoded by the RBBP4 gene.
Function
This gene encodes a ubiquitously expressed nuclear protein that belongs to a highly conserved subfamily of WD-repeat proteins. It is present in protein complexes involved in histone acetylation and chromatin assembly. It is part of the Mi-2/NuRD complex that has been implicated in chromatin remodeling and transcriptional repression associated with histone deacetylation. This encoded protein is also part of corepressor complexes, which is an integral component of transcriptional silencing. It is found among several cellular proteins that bind directly to retinoblastoma protein to regulate cell proliferation. This protein also seems to be involved in transcriptional repression of E2F-responsive genes.
Clinical significance
A decrease of RbAp48 in the dentate gyrus (DG) of the hippocampus in the brain is suspected to be a main cause of memory loss in normal aging. An age related decrease in RbAp48 is observed in the DG from human post-mortem tissue and also in mice. Furthermore, a gene knockin of a dominant negative form of RbAp48 of causes memory deficits in young mice similar to that observed in older mice. Finally lentiviral gene transfer to increase the expression of RbAp48 in the brain reverses memory deficits in older mice.
RBBP4 works at least in part through the PKA-CREB1-CPB pathway. Hence one possible therapeutic approach to restor |
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