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https://en.wikipedia.org/wiki/TRAF1 | TNF receptor-associated factor 1 is a protein that in humans is encoded by the TRAF1 gene.
Function
The protein encoded by this gene is a member of the TNF receptor (TNFR) associated factor (TRAF) protein family. TRAF proteins associate with, and mediate the signal transduction from various receptors of the TNFR superfamily. This protein and TRAF2 form a heterodimeric complex, which is required for TNF-alpha-mediated activation of MAPK8/JNK and NF-kappaB. The protein complex formed by this protein and TRAF2 also interacts with IAP, and thus mediates the anti-apoptotic signals from TNF receptors. The expression of this protein can be induced by Epstein-Barr virus (EBV). EBV infection membrane protein 1 (LMP1) is found to interact with this and other TRAF proteins; this interaction is thought to link LMP1-mediated B lymphocyte transformation to the signal transduction from TNFR family receptors. TRAF1 also functions as a negative regulator of inflammation by interfering with the linear ubiquitination of NEMO downstream of TLR signaling. This explains why TRAF1 polymorphisms cause an increased risk for rheumatic diseases.
Interactions
TRAF1 has been shown to interact with:
BIRC2,
Baculoviral IAP repeat-containing protein 3,
CFLAR,
Caspase 8,
HIVEP3,
RANK
TNFAIP3,
TRAF interacting protein, and
TRAF2.
RNF31.
RBCK1.
SHARPIN.
References
Further reading |
https://en.wikipedia.org/wiki/HDAC4 | Histone deacetylase 4, also known as HDAC4, is a protein that in humans is encoded by the HDAC4 gene.
Function
Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromosome structure and affects transcription factor access to DNA. The protein encoded by this gene belongs to class II of the histone deacetylase/acuc/apha family. It possesses histone deacetylase activity and represses transcription when tethered to a promoter. This protein does not bind DNA directly but through transcription factors MEF2C and MEF2D. It seems to interact in a multiprotein complex with RbAp48 and HDAC3. Furthermore, HDAC4 is required for TGFbeta1-induced myofibroblastic differentiation.
Clinical significance
Studies have shown that HDAC4 regulates bone and muscle development. Harvard University researchers also concluded that it promotes healthy vision: Reduced levels of the protein led to the death of the rod photoreceptors and bipolar cells in the retinas of mice.
Interactions
HDAC4 has been shown to interact with:
BCL6,
BTG2,
CBX5,
GATA1,
HDAC3,
MAPK1,
MAPK3,
MEF2C,
Myocyte-specific enhancer factor 2A,
Nuclear receptor co-repressor 1,
Nuclear receptor co-repressor 2,
Testicular receptor 2,
YWHAB,
YWHAE, and
Zinc finger and BTB domain-containing protein 16.
See also
Histone deacetylase
References
Further reading
External links
EC 3.5.1 |
https://en.wikipedia.org/wiki/2%2C5-dioxovalerate%20dehydrogenase | In enzymology, a 2,5-dioxovalerate dehydrogenase () is an enzyme that catalyzes the chemical reaction
2,5-dioxopentanoate + NADP+ + H2O 2-oxoglutarate + NADPH + 2 H+
The 3 substrates of this enzyme are 2,5-dioxopentanoate, NADP+, and H2O, whereas its 3 products are 2-oxoglutarate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2,5-dioxopentanoate:NADP+ 5-oxidoreductase. Other names in common use include 2-oxoglutarate semialdehyde dehydrogenase, and alpha-ketoglutaric semialdehyde dehydrogenase. This enzyme participates in ascorbate and aldarate metabolism.
References
EC 1.2.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Apolipoprotein%20A-II | Apolipoprotein A-II is a protein that in humans is encoded by the APOA2 gene. It is the second most abundant protein of the high density lipoprotein particles. The protein is found in plasma as a monomer, homodimer, or heterodimer with apolipoprotein D. ApoA-II regulates many steps in HDL metabolism, and its role in coronary heart disease is unclear. Remarkably, defects in this gene may result in apolipoprotein A-II deficiency or hypercholesterolemia.
Interactions
ApoA-II has been shown to interact with phospholipid transfer protein.
Interactive pathway map
References
External links
Further reading
Apolipoproteins |
https://en.wikipedia.org/wiki/2-oxoaldehyde%20dehydrogenase%20%28NAD%2B%29 | In enzymology, a 2-oxoaldehyde dehydrogenase (NAD+) () is an enzyme that catalyzes the chemical reaction
a 2-oxoaldehyde + NAD+ + H2O a 2-oxo acid + NADH + H+
The 3 substrates of this enzyme are 2-oxoaldehyde, NAD+, and H2O, whereas its 3 products are 2-oxo acid, NADH, and H+.
This enzyme participates in pyruvate metabolism.
Nomenclature
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-oxoaldehyde:NAD+ 2-oxidoreductase.
Other names in common use include:
alpha-ketoaldehyde dehydrogenase
methylglyoxal dehydrogenase
NAD+-linked alpha-ketoaldehyde dehydrogenase
2-ketoaldehyde dehydrogenase
NAD+-dependent alpha-ketoaldehyde dehydrogenase
2-oxoaldehyde dehydrogenase (NAD+)
See also
2-oxoaldehyde dehydrogenase (NADP+)
References
EC 1.2.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/BARD1 | BRCA1-associated RING domain protein 1 is a protein that in humans is encoded by the BARD1 gene. The human BARD1 protein is 777 amino acids long and contains a RING finger domain (residues 46-90), four ankyrin repeats (residues 420-555), and two tandem BRCT domains (residues 568-777).
Function
Most, if not all, BRCA1 heterodimerizes with BARD1 in vivo. BARD1 and BRCA1 form a heterodimer via their N-terminal RING finger domains. The BARD1-BRCA1 interaction is observed in vivo and in vitro and is essential for BRCA1 stability. BARD1 shares homology with the two most conserved regions of BRCA1: the N-terminal RING motif and the C-terminal BRCT domain. The RING motif is a cysteine-rich sequence found in a variety of proteins that regulate cell growth, including the products of tumor suppressor genes and dominant protooncogenes, and developmentally important genes such as the polycomb group of genes. The BARD1 protein also contains three tandem ankyrin repeats.
The BARD1/BRCA1 interaction is disrupted by tumorigenic amino acid substitutions in BRCA1, implying that the formation of a stable complex between these proteins may be an essential aspect of BRCA1 tumor suppression. BARD1 may be the target of oncogenic mutations in breast or ovarian cancer. Mutations in the BARD1 protein that affect its structure appear in many breast, ovarian, and uterine cancers, suggesting the mutations disable BARD1's tumor suppressor function. Three missense mutations, each affecting BARD1's BRCT |
https://en.wikipedia.org/wiki/2-oxoaldehyde%20dehydrogenase%20%28NADP%2B%29 | In enzymology, a 2-oxoaldehyde dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
a 2-oxoaldehyde + NADP+ + H2O a 2-oxo acid + NADPH + H+
The 3 substrates of this enzyme are 2-oxoaldehyde, NADP+, and H2O, whereas its 3 products are 2-oxo acid, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-oxoaldehyde:NADP+ 2-oxidoreductase. Other names in common use include alpha-ketoaldehyde dehydrogenase, methylglyoxal dehydrogenase, NADP+-linked alpha-ketoaldehyde dehydrogenase, 2-ketoaldehyde dehydrogenase, NADP+-dependent alpha-ketoaldehyde dehydrogenase, and 2-oxoaldehyde dehydrogenase (NADP+). This enzyme participates in pyruvate metabolism.
References
EC 1.2.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-oxobutyrate%20synthase | In enzymology, a 2-oxobutyrate synthase () is an enzyme that catalyzes the chemical reaction
2-oxobutanoate + CoA + oxidized ferredoxin propanoyl-CoA + CO2 + reduced ferredoxin
The 3 substrates of this enzyme are 2-oxobutanoate, CoA, and oxidized ferredoxin, whereas its 3 products are propanoyl-CoA, CO2, and reduced ferredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is 2-oxobutanoate:ferredoxin 2-oxidoreductase (CoA-propanoylating). Other names in common use include alpha-ketobutyrate-ferredoxin oxidoreductase, 2-ketobutyrate synthase, alpha-ketobutyrate synthase, 2-oxobutyrate-ferredoxin oxidoreductase, and 2-oxobutanoate:ferredoxin 2-oxidoreductase (CoA-propionylating). This enzyme participates in propanoate metabolism.
References
EC 1.2.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cholecystokinin%20B%20receptor | The cholecystokinin B receptor also known as CCKBR or CCK2 is a protein that in humans is encoded by the CCKBR gene.
This gene encodes a G protein-coupled receptor for gastrin and cholecystokinin (CCK), regulatory peptides of the brain and gastrointestinal tract. This protein is a type B gastrin receptor, which has a high affinity for both sulfated and nonsulfated CCK analogs and is found principally in the central nervous system and the gastrointestinal tract. A misspliced transcript variant including an intron has been observed in cells from colorectal and pancreatic tumors.
CNS effects
CCK receptors significantly influence neurotransmission in the brain, regulating anxiety, feeding, and locomotion. CCK-B expression may correlate parallel to anxiety and depression phenotypes in humans. CCK-B receptors possess a complex regulation of dopamine activity in the brain. CCK-B activation appears to possess a general inhibitory action on dopamine activity in the brain, opposing the dopamine-enhancing effects of CCK-A. However, the effects of CCK-B on dopamine activity vary depending on location. CCK-B antagonism enhances dopamine release in rat striatum. Activation enhances GABA release in rat anterior nucleus accumbens. CCK-B receptors modulate dopamine release, and influence the development of tolerance to opioids. CCK-B activation decreases amphetamine-induced DA release, and contributes to individual variability in response to amphetamine.
In rats, CCK-B antagonism prevents |
https://en.wikipedia.org/wiki/2-oxoglutarate%20synthase | In enzymology, a 2-oxoglutarate synthase () is an enzyme that catalyzes the chemical reaction
2-oxoglutarate + CoA + 2 oxidized ferredoxin succinyl-CoA + CO2 + 2 reduced ferredoxin
The 3 substrates of this enzyme are 2-oxoglutarate, CoA, and oxidized ferredoxin, whereas its 3 products are succinyl-CoA, CO2, and reduced ferredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is 2-oxoglutarate:ferredoxin oxidoreductase (decarboxylating). Other names in common use include 2-ketoglutarate ferredoxin oxidoreductase, 2-oxoglutarate:ferredoxin oxidoreductase, KGOR, 2-oxoglutarate ferredoxin oxidoreductase, and 2-oxoglutarate:ferredoxin 2-oxidoreductase (CoA-succinylating). This enzyme participates in the Citric acid cycle. Some forms catalyze the reverse reaction within the Reverse Krebs cycle, as a means of carbon fixation.
References
EC 1.2.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-oxoisovalerate%20dehydrogenase%20%28acylating%29 | In enzymology, a 2-oxoisovalerate dehydrogenase (acylating) () is an enzyme that catalyzes the chemical reaction
3-methyl-2-oxobutanoate + CoA + NAD+ 2-methylpropanoyl-CoA + CO2 + NADH
The 3 substrates of this enzyme are 3-methyl-2-oxobutanoate, CoA, and NAD+, whereas its 3 products are 2-methylpropanoyl-CoA, CO2, and NADH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-methyl-2-oxobutanoate:NAD+ 2-oxidoreductase (CoA-methyl-propanoylating). Other names in common use include 2-oxoisovalerate dehydrogenase, and alpha-ketoisovalerate dehydrogenase. This enzyme participates in valine, leucine and isoleucine degradation.
References
EC 1.2.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/DCTN1 | Dynactin subunit 1 is a protein that in humans is encoded by the DCTN1 gene.
Function
This gene encodes the largest subunit of dynactin, a macromolecular complex consisting of 23 subunits (11 individual proteins ranging in size from 22 to 150 kD). Dynactin binds to cytoplasmic dynein, dynein cargo adaptors, and microtubules. It is involved in a diverse array of cellular functions, including ER-to-Golgi transport, the centripetal movement of lysosomes and endosomes, spindle formation, chromosome movement, nuclear positioning, and axonogenesis.
This subunit is commonly referred to p150-glued. It is present in two copies per dynactin complex and forms an ≈75 nm long flexible arm that extends from the main body of dynactin. The p150-glued arm contains binding sites for microtubules, the microtubule plus tip binding protein EB1, and the N-terminus of the dynein intermediate chain.
Alternative splicing of this gene results in at least 2 functionally distinct isoforms: a ubiquitously expressed one and a brain-specific one. Based on its cytogenetic location, this gene is considered as a candidate gene for limb-girdle muscular dystrophy.
Interactions
DCTN1 has been shown to interact with:
BBS4,
Dystonin,
Grb2, and
RAB6A.
References
Further reading
External links
GeneReviews/NIH/NCBI/UW entry on Perry syndrome |
https://en.wikipedia.org/wiki/3alpha%2C7alpha%2C12alpha-trihydroxycholestan-26-al%2026-oxidoreductase | In enzymology, a 3alpha,7alpha,12alpha-trihydroxycholestan-26-al 26-oxidoreductase is an enzyme that catalyzes the chemical reaction:
(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al + NAD+ + H2O (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate + NADH + 2 H+
The 3 substrates of this enzyme are (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al, NAD+, and H2O, whereas its 2 products are (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate, NADH, and H+. This enzyme participates in bile acid biosynthesis.
Nomenclature
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al:NAD+ 26-oxidoreductase. Other names in common use include:
cholestanetriol-26-al 26-dehydrogenase,
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al, dehydrogenase,
trihydroxydeoxycoprostanal dehydrogenase,
THAL-NAD oxidoreductase,
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al:NAD+, and
26-oxidoreductase.
References
EC 1.2.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-methyl-2-oxobutanoate%20dehydrogenase | In enzymology, a 3-methyl-2-oxobutanoate dehydrogenase () is an enzyme that catalyzes the chemical reaction
3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
The 3 substrates of this enzyme are 3-methyl-2-oxobutanoate, dihydrolipoyllysine-residue (2-methylpropanoyl)transferase, and lipoyllysine, whereas its 3 products are dihydrolipoyllysine-residue (2-methylpropanoyl)transferase, S-(2-methylpropanoyl)dihydrolipoyllysine, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a disulfide as acceptor.
This enzyme participates in valine, leucine and isoleucine degradation. It employs one cofactor, thiamin diphosphate. It is the E1 subunit of a catalytic complex.
Structural studies
As of late 2007, twenty-nine structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , , , , , , , , , , , , , and .
References
EC 1.2.4
Thiamine enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/3-methyl-2-oxobutanoate%20dehydrogenase%20%28ferredoxin%29 | In enzymology, a 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) () is an enzyme that catalyzes the chemical reaction
3-methyl-2-oxobutanoate + CoA + oxidized ferredoxin S-(2-methylpropanoyl)-CoA + CO2 + reduced ferredoxin
The 3 substrates of this enzyme are 3-methyl-2-oxobutanoate, CoA, and oxidized ferredoxin, whereas its 3 products are S-(2-methylpropanoyl)-CoA, CO2, and reduced ferredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is '''. Other names in common use include 2-ketoisovalerate ferredoxin reductase, 3-methyl-2-oxobutanoate synthase (ferredoxin), VOR, branched-chain ketoacid ferredoxin reductase, branched-chain oxo acid ferredoxin reductase, keto-valine-ferredoxin oxidoreductase, ketoisovalerate ferredoxin reductase, and 2-oxoisovalerate ferredoxin reductase'''.
References
EC 1.2.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/MT-ND2 | MT-ND2 is a gene of the mitochondrial genome coding for the NADH dehydrogenase 2 (ND2) protein. The ND2 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. Variants of human MT-ND2 are associated with mitochondrial encephalomyopathy, lactic acidosis, and stroke-like episodes (MELAS), Leigh's syndrome (LS), Leber's hereditary optic neuropathy (LHON) and increases in adult BMI.
Structure
MT-ND2 is located in mitochondrial DNA from base pair 4,470 to 5,511. The MT-ND2 gene produces a 39 kDa protein composed of 347 amino acids. MT-ND2 is one of seven mitochondrial genes encoding subunits of the enzyme NADH dehydrogenase (ubiquinone), together with MT-ND1, MT-ND3, MT-ND4, 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. The MT-ND2 product 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-ND2 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 transfer to u |
https://en.wikipedia.org/wiki/4-formylbenzenesulfonate%20dehydrogenase | In enzymology, a 4-formylbenzenesulfonate dehydrogenase () is an enzyme that catalyzes the chemical reaction
4-formylbenzenesulfonate + NAD+ + H2O 4-sulfobenzoate + NADH + 2 H+
The 3 substrates of this enzyme are 4-formylbenzenesulfonate, NAD+, and H2O, whereas its 3 products are 4-sulfobenzoate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4-formylbenzenesulfonate:NAD+ oxidoreductase. This enzyme participates in 2,4-dichlorobenzoate degradation.
References
EC 1.2.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/PLD2 | Phospholipase D2 is an enzyme that in humans is encoded by the PLD2 gene.
Function
Phosphatidylcholine (PC)-specific phospholipases D (PLDs) catalyze the hydrolysis of PC to produce phosphatidic acid and choline. Activation of PC-specific PLDs occurs as a consequence of agonist stimulation of both tyrosine kinase and G protein-coupled receptors. PC-specific PLDs have been proposed to function in regulated secretion, cytoskeletal reorganization, transcriptional regulation, and cell cycle control.[supplied by OMIM]
Mechanism of activation
PLD2 is activated by substrate presentation. The enzyme is palmitoylated, which drives PLD2 to lipid rafts. PC substrate is polyunsaturated and resides in the membrane separately from lipid rafts near phosphatidylinositol 4,5-bisphosphate (PIP2). When PIP2 levels increase, PLD2 trafficks to PIP2 where it encounters its substrate PC. Scaffolding proteins that interact with PLD2 likely changes its preference of lipid rafts vs PIP2.
Interactions
PLD2 has been shown to interact with:
ARF1,
Aldolase A,
Amphiphysin,
BIN1,
Caveolin 1,
Glyceraldehyde 3-phosphate dehydrogenase,
PLCG1,
PRKCD,
Src, and
Wiskott-Aldrich syndrome protein.
Inhibitors
N-(2-(1-(3-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]decan-8-yl)ethyl)-2-naphthamide: 75-fold selective versus PLD1, IC50 = 20 nM.
References
Further reading
EC 3.1.4 |
https://en.wikipedia.org/wiki/4-hydroxybenzaldehyde%20dehydrogenase | In enzymology, a 4-hydroxybenzaldehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction
4-hydroxybenzaldehyde + NAD+ + H2O 4-hydroxybenzoate + NADH + 2 H+
The 3 substrates of this enzyme are 4-hydroxybenzaldehyde, NAD+, and H2O, whereas its 3 products are 4-hydroxybenzoate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-hydroxybenzaldehyde:NAD+ oxidoreductase. This enzyme is also called p-hydroxybenzaldehyde dehydrogenase. This enzyme participates in toluene and xylene degradation in bacteria. It is also found in carrots (Daucus carota).
References
EC 1.2.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/4-hydroxymuconic-semialdehyde%20dehydrogenase | In enzymology, a 4-hydroxymuconic-semialdehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction
4-hydroxymuconic semialdehyde + NAD+ + H2O maleylacetate + NADH + 2 H+
The 3 substrates of this enzyme are 4-hydroxymuconic semialdehyde, NAD+, and H2O, whereas its 3 products are maleylacetate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4-hydroxymuconic-semialdehyde:NAD+ oxidoreductase. This enzyme participates in gamma-hexachlorocyclohexane degradation.
References
EC 1.2.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/4-hydroxyphenylacetaldehyde%20dehydrogenase | In enzymology, a 4-hydroxyphenylacetaldehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction
4-hydroxyphenylacetaldehyde + NAD+ + H2O 4-hydroxyphenylacetate + NADH + 2 H+
The 3 substrates of this enzyme are 4-hydroxyphenylacetaldehyde, NAD+, and H2O, whereas its 3 products are 4-hydroxyphenylacetate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4-hydroxyphenylacetaldehyde:NAD+ oxidoreductase. This enzyme is also called 4-HPAL dehydrogenase. This enzyme participates in tyrosine metabolism.
References
EC 1.2.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/4-hydroxyphenylpyruvate%20oxidase | In enzymology, a 4-hydroxyphenylpyruvate oxidase () is an enzyme that catalyzes the chemical reaction
4-hydroxyphenylpyruvate + 1/2 O2 4-hydroxyphenylacetate + CO2
Thus, the two substrates of this enzyme are 4-hydroxyphenylpyruvate and O2, whereas its two products are 4-hydroxyphenylacetate and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is 4-hydroxyphenylpyruvate:oxygen oxidoreductase (decarboxylating). This enzyme participates in tyrosine metabolism.
References
EC 1.2.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/4-trimethylammoniobutyraldehyde%20dehydrogenase | In enzymology, a 4-trimethylammoniobutyraldehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction
4-trimethylammoniobutanal + NAD+ + H2O 4-trimethylammoniobutanoate + NADH + 2 H+
The 3 substrates of this enzyme are 4-trimethylammoniobutanal, NAD+, and H2O, whereas its 3 products are 4-trimethylammoniobutanoate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4-trimethylammoniobutanal:NAD+ 1-oxidoreductase. Other names in common use include 4-trimethylaminobutyraldehyde dehydrogenase, and 4-N-trimethylaminobutyraldehyde dehydrogenase. This enzyme participates in lysine degradation and carnitine biosynthesis.
See also
Carnitine biosynthesis
γ-Butyrobetaine hydroxylase
Nε-Trimethyllysine hydroxylase
References
EC 1.2.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/5-carboxymethyl-2-hydroxymuconic-semialdehyde%20dehydrogenase | In enzymology, a 5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+ 5-carboxymethyl-2-hydroxymuconate + NADH + 2 H+
The 3 substrates of this enzyme are 5-carboxymethyl-2-hydroxymuconate semialdehyde, H2O, and NAD+, whereas its 3 products are 5-carboxymethyl-2-hydroxymuconate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 5-carboxymethyl-2-hydroxymuconic-semialdehyde:NAD+ oxidoreductase. This enzyme is also called carboxymethylhydroxymuconic semialdehyde dehydrogenase. This enzyme participates in tyrosine metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.2.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/6-oxohexanoate%20dehydrogenase | In enzymology, a 6-oxohexanoate dehydrogenase () is an enzyme that catalyzes the chemical reaction
6-oxohexanoate + NADP+ + H2O adipate + NADPH + 2 H+
The 3 substrates of this enzyme are 6-oxohexanoate, NADP+, and H2O, whereas its 3 products are adipate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 6-oxohexanoate:NADP+ oxidoreductase. This enzyme participates in caprolactam degradation.
References
EC 1.2.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/UCP3 | Mitochondrial uncoupling protein 3 is a protein that in humans is encoded by the UCP3 gene. The gene is located in chromosome (11q13.4) with an exon count of 7 (HGNC et al., 2016) and is expressed on the inner mitochondrial membrane. Uncoupling proteins transfer anions from the inner mitochondrial membrane to the outer mitochondrial membrane, thereby separating (or uncoupling) oxidative phosphorylation from synthesis of ATP, and dissipating energy stored in the mitochondrial membrane potential as heat. Uncoupling proteins also reduce generation of reactive oxygen species.
Function
Mitochondrial uncoupling protein 3 (UCP3) is a members of the larger family of mitochondrial anion carrier proteins (MACP). UCPs facilitate the transfer of anions from the inner to the outer mitochondrial membrane and transfer of protons from the outer to the inner mitochondrial membrane, reducing the mitochondrial membrane potential in mammalian cells. The exact mechanisms of how UCPs transfer H+/OH− are not known. In addition to UCP1, UCP3 is an important mediator of thermogenesis.
Protein expression
Uncoupling proteins are transporters in mitochondrial membrane which deplete the proton gradient. UCP1 is highly expressed in brown adipocytes, UCP2 is variably expressed in many different tissues, and UCP3 is expressed primarily in skeletal muscle. At amino acid level human UCP3 is 71% equivalent to UCP2. UCP3 i
Associated SNPs
UCP3 were confirmed containing four single nucleotide polymorphism |
https://en.wikipedia.org/wiki/Abscisic-aldehyde%20oxidase | In enzymology, an abscisic-aldehyde oxidase () is an enzyme that catalyzes the chemical reaction
abscisic aldehyde + H2O + O2 abscisate + H2O2
The 3 substrates of this enzyme are abscisic aldehyde, H2O, and O2, whereas its two products are abscisate and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is abscisic-aldehyde:oxygen oxidoreductase. Other names in common use include abscisic aldehyde oxidase, AAO3, AOd, and AOdelta. This enzyme participates in carotenoid biosynthesis.
References
EC 1.2.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aldehyde%20dehydrogenase%20%28FAD-independent%29 | In enzymology, an aldehyde dehydrogenase (FAD-independent) () is an enzyme that catalyzes the chemical reaction
an aldehyde + H2O + acceptor a carboxylate + reduced acceptor
The 3 substrates of this enzyme are aldehyde, H2O, and acceptor, whereas its two products are carboxylate and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with other acceptors. The systematic name of this enzyme class is aldehyde:acceptor oxidoreductase (FAD-independent). Other names in common use include aldehyde oxidase, aldehyde oxidoreductase, Mop, and AORDd.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.2.99
Enzymes of known structure |
https://en.wikipedia.org/wiki/Aldehyde%20dehydrogenase%20%28NAD%2B%29 | In enzymology, an aldehyde dehydrogenase (NAD+) () is an enzyme that catalyzes the chemical reaction
an aldehyde + NAD+ + H2O an acid + NADH + H+
The 3 substrates of this enzyme are aldehyde, NAD+, and H2O, whereas its 3 products are acid, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is aldehyde:NAD+ oxidoreductase. Other names in common use include CoA-independent aldehyde dehydrogenase, m-methylbenzaldehyde dehydrogenase, NAD-aldehyde dehydrogenase, NAD-dependent 4-hydroxynonenal dehydrogenase, NAD-dependent aldehyde dehydrogenase, NAD-linked aldehyde dehydrogenase, propionaldehyde dehydrogenase, and aldehyde dehydrogenase (NAD). This enzyme participates in 17 metabolic pathways: glycolysis / gluconeogenesis, ascorbate and aldarate metabolism, fatty acid metabolism, bile acid biosynthesis, urea cycle and metabolism of amino groups, valine, leucine and isoleucine degradation, lysine degradation, histidine metabolism, tryptophan metabolism, beta-alanine metabolism, glycerolipid metabolism, pyruvate metabolism, 1,2-dichloroethane degradation, propanoate metabolism, 3-chloroacrylic acid degradation, butanoate metabolism, and limonene and pinene degradation.
References
External links
EC 1.2.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Aldehyde%20dehydrogenase%20%28NAD%28P%29%2B%29 | In enzymology, an aldehyde dehydrogenase [NAD(P)+] () is an enzyme that catalyzes the chemical reaction
an aldehyde + NAD(P)+ + H2O an acid + NAD(P)H + H+
The 4 substrates of this enzyme are aldehyde, NAD+, NADP+, and H2O, whereas its 4 products are acid, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is aldehyde:NAD(P)+ oxidoreductase. Other names in common use include aldehyde dehydrogenase [NAD(P)+], and ALDH. This enzyme participates in 5 metabolic pathways: glycolysis / gluconeogenesis, histidine metabolism, tyrosine metabolism, phenylalanine metabolism, and metabolism of xenobiotics by cytochrome p450.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 203-221.
EC 1.2.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/NCF1C | Putative neutrophil cytosol factor 1C is a protein that in humans is encoded by the NCF1C gene. It relates to a type of white blood cell called a neutrophil. The Neutrophil Cytosolic Factor 1C (NCF1C) gene is responsible for encoding the 47 kDA cytosolic subunit of NADPH oxidase. The NCF1C gene is located near two pseudogenes and when the NCF1C gene recombines with them, the NCF1C gene will inactivate and can lead to chronic granulomatous disease.
References
Further reading
Human proteins |
https://en.wikipedia.org/wiki/Aldehyde%20dehydrogenase%20%28NADP%2B%29 | In enzymology, an aldehyde dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
an aldehyde + NADP+ + H2O an acid + NADPH + H+
The 3 substrates of this enzyme are aldehyde, NADP+, and H2O, whereas its 3 products are acid, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is aldehyde:NADP+ oxidoreductase. Other names in common use include NADP+-acetaldehyde dehydrogenase, NADP+-dependent aldehyde dehydrogenase, and aldehyde dehydrogenase (NADP+). This enzyme participates in caprolactam degradation.
References
Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 203-221.
EC 1.2.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aldehyde%20dehydrogenase%20%28pyrroloquinoline-quinone%29 | In enzymology, an aldehyde dehydrogenase (pyrroloquinoline-quinone) () is an enzyme that catalyzes the chemical reaction
an aldehyde + acceptor + H2O a carboxylate + reduced acceptor
The 3 substrates of this enzyme are aldehyde, acceptor, and H2O, whereas its two products are carboxylate and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with other acceptors. The systematic name of this enzyme class is aldehyde:(pyrroloquinoline-quinone) oxidoreductase. This enzyme is also called aldehyde dehydrogenase (acceptor). This enzyme participates in 4 metabolic pathways: fatty acid metabolism, pyruvate metabolism, propanoate metabolism, and butanoate metabolism. It employs one cofactor, PQQ.
References
EC 1.2.99
Pyrroloquinoline quinone enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aminobutyraldehyde%20dehydrogenase | In enzymology, an aminobutyraldehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction
4-aminobutanal + NAD+ + H2O 4-aminobutanoate + NADH + 2 H+
The 3 substrates of this enzyme are 4-aminobutanal, NAD+, and H2O, whereas its 3 products are 4-aminobutanoate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4-aminobutanal:NAD+ 1-oxidoreductase. Other names in common use include gamma-guanidinobutyraldehyde dehydrogenase (ambiguous), ABAL dehydrogenase, 4-aminobutyraldehyde dehydrogenase, 4-aminobutanal dehydrogenase, gamma-aminobutyraldehyde dehydrogenase, 1-pyrroline dehydrogenase, ABALDH, and YdcW. This enzyme participates in the urea cycle and the metabolism of amino groups and beta-alanine.
References
EC 1.2.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aminomuconate-semialdehyde%20dehydrogenase | In enzymology, an aminomuconate-semialdehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction
2-aminomuconate 6-semialdehyde + NAD+ + H2O 2-aminomuconate + NADH + 2 H+
The 3 substrates of this enzyme are 2-aminomuconate 6-semialdehyde, NAD+, and H2O, whereas its 3 products are 2-aminomuconate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in 3 metabolic pathways: benzoic acid degradation via hydroxylation, tryptophan metabolism, and the degradation pathway for toluene and xylene.
Nomenclature
The systematic name of this enzyme class is 2-aminomuconate-6-semialdehyde:NAD+ 6-oxidoreductase. Other names in common use include 2-aminomuconate semialdehyde dehydrogenase, 2-hydroxymuconic acid semialdehyde dehydrogenase, 2-hydroxymuconate semialdehyde dehydrogenase, alpha-aminomuconic epsilon-semialdehyde dehydrogenase, alpha-hydroxymuconic epsilon-semialdehyde dehydrogenase, and 2-hydroxymuconic semialdehyde dehydrogenase.
References
Further reading
EC 1.2.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aryl-aldehyde%20dehydrogenase | In enzymology, an aryl-aldehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction
an aromatic aldehyde + NAD+ + H2O an aromatic acid + NADH + H+
The 3 substrates of this enzyme are aromatic aldehyde, NAD+, and H2O, whereas its 3 products are aromatic acid, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is aryl-aldehyde:NAD+ oxidoreductase. This enzyme participates in tyrosine metabolism and biphenyl degradation.
References
EC 1.2.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aryl-aldehyde%20dehydrogenase%20%28NADP%2B%29 | In enzymology, an aryl-aldehyde dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
an aromatic aldehyde + NADP+ + AMP + diphosphate + H2O an aromatic acid + NADPH + H+ + ATP
The 5 substrates of this enzyme are aromatic aldehyde, NADP+, AMP, diphosphate, and H2O, whereas its 4 products are aromatic acid, NADPH, H+, and ATP.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is aryl-aldehyde:NADP+ oxidoreductase (ATP-forming). Other names in common use include aromatic acid reductase, and aryl-aldehyde dehydrogenase (NADP+).
References
EC 1.2.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aryl-aldehyde%20oxidase | In enzymology, an aryl-aldehyde oxidase () is an enzyme that catalyzes the chemical reaction
an aromatic aldehyde + O2 + H2O an aromatic carboxylic acid + H2O2
The 3 substrates of this enzyme are aromatic aldehyde, O2, and H2O, whereas its two products are aromatic carboxylic acid and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is aryl-aldehyde:oxygen oxidoreductase.
References
EC 1.2.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aspartate-semialdehyde%20dehydrogenase | In enzymology, an aspartate-semialdehyde dehydrogenase () is an enzyme that is very important in the biosynthesis of amino acids in prokaryotes, fungi, and some higher plants. It forms an early branch point in the metabolic pathway forming lysine, methionine, leucine and isoleucine from aspartate. This pathway also produces diaminopimelate which plays an essential role in bacterial cell wall formation. There is particular interest in ASADH as disabling this enzyme proves fatal to the organism giving rise to the possibility of a new class of antibiotics, fungicides, and herbicides aimed at inhibiting it.
The enzyme catalyzes the reversible chemical reaction
L-aspartate 4-semialdehyde + phosphate + NADP+ L-4-aspartyl phosphate + NADPH + H+
The 3 substrates of this enzyme are L-aspartate 4-semialdehyde, phosphate, and NADP+, whereas its 3 products are L-4-aspartyl phosphate, NADPH, and H+.
However, under physiological conditions the reaction runs in the opposite direction.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of a donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-aspartate-4-semialdehyde:NADP+ oxidoreductase (phosphorylating). Other names in common use include aspartate semialdehyde dehydrogenase, aspartic semialdehyde dehydrogenase, L-aspartate-beta-semialdehyde:NADP+ oxidoreductase, (phosphorylating), aspartic beta-semialdehyde dehydrogenase, and ASA dehydrogenase. Th |
https://en.wikipedia.org/wiki/ALOX15 | ALOX15 (also termed arachidonate 15-lipoxygenase, 15-lipoxygenase-1, 15-LO-1, 15-LOX-1) is, like other lipoxygenases, a seminal enzyme in the metabolism of polyunsaturated fatty acids to a wide range of physiologically and pathologically important products.
▼ Gene Function
Kelavkar and Badr (1999) stated that the ALOX15 gene product is implicated in antiinflammation, membrane remodeling, and cancer development/metastasis. Kelavkar and Badr (1999) described experiments yielding data that supported the hypothesis that loss of the TP53 gene, or gain-of-function activities resulting from the expression of its mutant forms, regulates ALOX15 promoter activity in human and in mouse, albeit in directionally opposite manners. These studies defined a direct link between ALOX15 gene activity and an established tumor-suppressor gene located in close chromosomal proximity. Kelavkar and Badr (1999) referred to this as evidence that 15-lipoxygenase is a mutator gene.
▼ Mapping
By PCR analysis of a human-hamster somatic hybrid DNA panel, Funk et al. (1992) demonstrated that genes for 12-lipoxygenase and 15-lipoxygenase are located on human chromosome 17, whereas the most unrelated lipoxygenase (5-lipoxygenase) was mapped to chromosome 10.
Kelavkar and Badr (1999) stated that the ALOX15 gene maps to 17p13.3 in close proximity to the tumor-suppressor gene TP53 (191170). In humans, it is encoded by the ALOX15 gene located on chromosome 17p13.3. This 11 kilobase pair gene consists of 14 exon |
https://en.wikipedia.org/wiki/Benzaldehyde%20dehydrogenase%20%28NAD%2B%29 | In enzymology, a benzaldehyde dehydrogenase (NAD+) () is an enzyme that catalyzes the chemical reaction
benzaldehyde + NAD+ + H2O benzoate + NADH + 2 H+
The 3 substrates of this enzyme are benzaldehyde, NAD+, and H2O, whereas its 3 products are benzoate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is benzaldehyde:NAD+ oxidoreductase. Other names in common use include benzaldehyde (NAD+) dehydrogenase, and benzaldehyde dehydrogenase (NAD+). This enzyme participates in benzoate degradation via hydroxylation and toluene and xylene degradation.
References
EC 1.2.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Benzaldehyde%20dehydrogenase%20%28NADP%2B%29 | In enzymology, a benzaldehyde dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
benzaldehyde + NADP+ + H2O benzoate + NADPH + 2 H+
The 3 substrates of this enzyme are benzaldehyde, NADP+, and H2O, whereas its 3 products are benzoate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is benzaldehyde:NADP+ oxidoreductase. Other names in common use include NADP+-linked benzaldehyde dehydrogenase, and benzaldehyde dehydrogenase (NADP+). This enzyme participates in benzoate degradation via hydroxylation and toluene and xylene degradation.
References
EC 1.2.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/BIN1 | Myc box-dependent-interacting protein 1, also known as Bridging Integrator-1 and Amphiphysin-2 is a protein that in humans is encoded by the BIN1 gene.
This gene encodes several isoforms of a nucleocytoplasmic adaptor protein, one of which was initially identified as a MYC-interacting protein with features of a tumor suppressor.
Isoforms that are expressed in the central nervous system may be involved in synaptic vesicle endocytosis and may interact with dynanim, synaptojanin, endophilin, and clathrin.
Isoforms that are expressed in muscle and ubiquitously expressed isoforms localize to the cytoplasm and nucleus and activate a caspase-independent apoptotic process.
Studies in mouse suggest that this gene plays an important role in cardiac muscle development. Alternate splicing of the gene results in ten transcript variants encoding different isoforms. Aberrant splice variants expressed in tumor cell lines have also been described.
Clinical significance
In humans, mutations in BIN1 have been associated with skeletal myopathies including centronuclear myopathy causing muscle weakness and myotonic dystrophy causing progressive muscle wasting, myotonia, cataracts, and heart conduction defects. An association has also been found between BIN1 mutations and Alzheimer's disease. Knockdown of BIN1 produces a cardiomyopathy phenotype in zebrafish, and in sheep BIN1 may be responsible for the loss of T-tubules seen in heart failure.
Interactions
BIN1 has been shown to interact w |
https://en.wikipedia.org/wiki/Betaine-aldehyde%20dehydrogenase | In enzymology, a betaine-aldehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction
betaine aldehyde + NAD+ + H2O betaine + NADH + 2 H+
The 3 substrates of this enzyme are betaine aldehyde, NAD+, and H2O, whereas its 3 products are betaine, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is betaine-aldehyde:NAD+ oxidoreductase. Other names in common use include betaine aldehyde oxidase, BADH, betaine aldehyde dehydrogenase, and BetB. This enzyme participates in glycine, serine and threonine metabolism.
Structural studies
, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 1.2.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/APOA4 | Apolipoprotein A-IV (also known as apoA-IV, apoAIV, or apoA4) is plasma protein that is the product of the human gene APOA4.
Gene
APOA4 resides on chromosome 11 in close linkage to APOA1 and APOC3. APOA4 contains 3 exons separated by two introns, and is polymorphic, although most of the reported sequence polymorphisms occur in exon 3. The best validated and studied non-synonymous SNPs are a glutamine → histidine substitution at codon 360 and a threonine → serine substitution at codon 347; a sequence polymorphism has also been identified in the 3'UTR of the third exon. Intra-species comparative gene sequence analysis suggests that the APOA4 gene arose from APOA1 by gene duplication approximately 270 MYA.
Function
The primary translation product of the APOA4 gene is a 396-residue preprotein, which undergoes proteolytic processing to yield apo A-IV, a 376-residue mature O-linked glycoprotein. In most mammals, including humans, apo A-IV synthesis is confined to the intestine; however in mice and rats hepatic synthesis also occurs. Apo A-IV is secreted into circulation on the surface of newly synthesized chylomicron particles. Intestinal fat absorption dramatically increases the synthesis and secretion of apo A-IV. Although its primary function in human lipid metabolism has not been established, apo A-IV has been found to:
activate lecithin-cholesterol acyltransferase and cholesterylester transfer protein in vitro;
play a role in the regulation of appetite and satiety in r |
https://en.wikipedia.org/wiki/Butanal%20dehydrogenase | In enzymology, a butanal dehydrogenase () is an enzyme that catalyzes the chemical reaction
butanal + CoA + NAD(P)+ butanoyl-CoA + NAD(P)H + H+
The 4 substrates of this enzyme are butanal, CoA, NAD+, and NADP+, whereas its 4 products are butanoyl-CoA, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is butanal:NAD(P)+ oxidoreductase (CoA-acylating). This enzyme participates in butanoate metabolism.
References
EC 1.2.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Carbon%20monoxide%20dehydrogenase | In enzymology, carbon monoxide dehydrogenase (CODH) () is an enzyme that catalyzes the chemical reaction
CO + H2O + A CO2 + AH2
The chemical process catalyzed by carbon monoxide dehydrogenase is similar to the water-gas shift reaction.
The 3 substrates of this enzyme are CO, H2O, and A, whereas its two products are CO2 and AH2.
A variety of electron donors/receivers (Shown as "A" and "AH2" in the reaction equation above) are observed in micro-organisms which utilize CODH. Several examples of electron transfer cofactors has been proposed, including Ferredoxin, NADP+/NADPH and flavoprotein complexes like flavin adenine dinucleotide (FAD) as well as hydrogenases. CODHs support the metabolisms of diverse prokaryotes, including methanogens, aerobic carboxidotrophs, acetogens, sulfate-reducers, and hydrogenogenic bacteria. The bidirectional reaction catalyzed by CODH plays a role in the carbon cycle allowing organisms to both make use of CO as a source of energy and utilize CO2 as a source of carbon. CODH can form a monofunctional enzyme, as is the case in Rhodospirillum rubrum, or can form a cluster with acetyl-CoA synthase as has been shown in M.thermoacetica. When acting in concert, either as structurally independent enzymes or in a bifunctional CODH/ACS unit, the two catalytic sites are key to carbon fixation in the reductive acetyl-CoA pathway Microbial organisms (Both aerobic and anaerobic) encode and synthesize CODH for the purpose of carbon fixation (CO oxidation and |
https://en.wikipedia.org/wiki/Carbon-monoxide%20dehydrogenase%20%28cytochrome%20b-561%29 | In enzymology, a carbon-monoxide dehydrogenase (cytochrome b-561) () is an enzyme that catalyzes the chemical reaction
CO + H2O + 2 ferricytochrome b-561 CO2 + 2 H+ + 2 ferrocytochrome b-561
The 3 substrates of this enzyme are CO, H2O, and ferricytochrome b-561, whereas its 3 products are CO2, H+, and ferrocytochrome b-561.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is carbon monoxide,water:cytochrome b-561 oxidoreductase. Other names in common use include carbon monoxide oxidase, carbon monoxide oxygenase (cytochrome b-561), carbon monoxide:methylene blue oxidoreductase, CO dehydrogenase, and carbon-monoxide dehydrogenase.
References
EC 1.2.2
Enzymes of unknown structure
Carbon monoxide |
https://en.wikipedia.org/wiki/Carbon-monoxide%20dehydrogenase%20%28ferredoxin%29 | In enzymology, a carbon-monoxide dehydrogenase (ferredoxin) () is an enzyme that catalyzes the chemical reaction
CO + H2O + oxidized ferredoxin CO2 + reduced ferredoxin
The 3 substrates of this enzyme are CO, H2O, and oxidized ferredoxin, whereas its two products are CO2 and reduced ferredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is carbon-monoxide,water:ferredoxin oxidoreductase.
References
EC 1.2.7
Enzymes of unknown structure
Carbon monoxide |
https://en.wikipedia.org/wiki/Carboxylate%20reductase | In enzymology, a carboxylate reductase () is an enzyme that catalyzes the chemical reaction
an aldehyde + acceptor + H2O a carboxylate + reduced acceptor
The 3 substrates of this enzyme are aldehyde, acceptor, and H2O, whereas its two products are carboxylate and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with other acceptors. The systematic name of this enzyme class is aldehyde:acceptor oxidoreductase. This enzyme is also called aldehyde:(acceptor) oxidoreductase. This enzyme participates in pyruvate metabolism. It employs one cofactor, tungsten.
References
EC 1.2.99
Tungsten enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cinnamoyl-CoA%20reductase | Cinnamoyl-CoA reductase (), systematically named cinnamaldehyde:NADP+ oxidoreductase (CoA-cinnamoylating) but commonly referred to by the acronym CCR, is an enzyme that catalyzes the reduction of a substituted cinnamoyl-CoA to its corresponding cinnamaldehyde, utilizing NADPH and H+ and releasing free CoA and NADP+ in the process. Common biologically relevant cinnamoyl-CoA substrates for CCR include p-coumaroyl-CoA and feruloyl-CoA, which are converted into p-coumaraldehyde and coniferaldehyde, respectively, though most CCRs show activity toward a variety of other substituted cinnamoyl-CoA's as well. Catalyzing the first committed step in monolignol biosynthesis, this enzyme plays a critical role in lignin formation, a process important in plants both for structural development and defense response.
Structure
The first confirmed CCR was isolated from soybean (Glycine max) in 1976. However, crystal structures have so far been reported for just three CCR homologs: Petunia x hybrida CCR1, Medicago truncatula CCR2, and Sorghum bicolor CCR1. While the enzyme crystallizes as an asymmetric dimer, it is thought to exist as a monomer in the cytoplasm, with each individual protein having a bilobal structure consisting of two domains surrounding a large, empty inner cleft for substrate binding. Typical CCRs have a molecular weight of around 36-38 kDa.
The domain containing the enzyme's N-terminus consists of several alpha helices and six beta strands that, in addition to a seventh st |
https://en.wikipedia.org/wiki/Ephrin%20B2 | Ephrin-B2 is a protein that in humans is encoded by the EFNB2 gene.
Function
This gene encodes a member of the ephrin (EPH) family. The ephrins and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and have been implicated in mediating developmental events, especially in the nervous system and in erythropoiesis. Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. This gene encodes an EFNB class ephrin which binds to the EPHB4 and EPHA3 receptors.
Cancer
EFNB2 gene has been observed progressively downregulated in Human papillomavirus-positive neoplastic keratinocytes derived from uterine cervical preneoplastic lesions at different levels of malignancy. For this reason, EFNB2 is likely to be associated with tumorigenesis and may be a potential prognostic marker for uterine cervical preneoplastic lesions progression.
Interactions
EFNB2 has been shown to interact with EPHA3 and EPHB1 in optic chiasm development.
EFNB2 has also been shown to serve as a receptor for Hendra Virus and Nipah Virus, mediating entry into the cell during infection.
References
Further reading |
https://en.wikipedia.org/wiki/Coniferyl-aldehyde%20dehydrogenase | In enzymology, a coniferyl-aldehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction
coniferyl aldehyde + H2O + NAD(P)+ ferulate + NAD(P)H + 2 H+
The 4 substrates of this enzyme are coniferyl aldehyde, H2O, NAD+, and NADP+, whereas its 4 products are ferulate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is coniferyl aldehyde:NAD(P)+ oxidoreductase.
References
EC 1.2.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Fluoroacetaldehyde%20dehydrogenase | In enzymology, a fluoroacetaldehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction
fluoroacetaldehyde + NAD+ + H2O fluoroacetate + NADH + 2 H+
The 3 substrates of this enzyme are fluoroacetaldehyde, NAD+, and H2O, whereas its 3 products are fluoroacetate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is fluoroacetaldehyde:NAD+ oxidoreductase.
References
EC 1.2.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Formaldehyde%20dehydrogenase | In enzymology, a formaldehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction
formaldehyde + NAD+ + H2O formate + NADH + H+
The 3 substrates of this enzyme are formaldehyde, NAD+, and H2O, whereas its 3 products are formate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is formaldehyde:NAD+ oxidoreductase. Other names in common use include NAD+-linked formaldehyde dehydrogenase, s-nitrosoglutathione reductase (GSNO reductase) and NAD+-dependent formaldehyde dehydrogenase. This enzyme participates in methane metabolism.
Ubiquitous function
S-nitrosoglutathione reductase (GSNOR) is a class III alcohol dehydrogenase (ADH) encoded by the ADH5 gene in humans. It is a primordial ADH that is ubiquitously expressed in plant and animals alike. GSNOR reduces S-nitrosoglutathione (GSNO) to the unstable intermediate, S-hydroxylaminoglutathione, which then rearranges to form glutathione sulfinamide, or in the presence of GSH, forms oxidized glutathione (GSSG) and hydroxyl amine. Through this catabolic process, GSNOR regulates the cellular concentrations of GSNO and plays a central role in regulating the levels of endogenous S-nitrosothiols and controlling protein S-nitrosylation-based signaling. As an example of S-nitrosylation-based signaling, Barglow et al. showed that GSNO selectively S-nitrosylates |
https://en.wikipedia.org/wiki/Formaldehyde%20dismutase | In enzymology, a formaldehyde dismutase () is an enzyme that catalyzes the chemical reaction
2 formaldehyde formate + methanol
Hence, this enzyme has one substrate, formaldehyde, and two products, formate and methanol.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with other acceptors. The systematic name of this enzyme class is formaldehyde:formaldehyde oxidoreductase. Other names in common use include aldehyde dismutase, and cannizzanase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.2.99
Enzymes of known structure |
https://en.wikipedia.org/wiki/Formate%20dehydrogenase%20%28cytochrome%29 | In enzymology, a formate dehydrogenase (cytochrome) () is an enzyme that catalyzes the chemical reaction
formate + 2 ferricytochrome b1 CO2 + 2 ferrocytochrome b1 + 2 H+
Thus, the two substrates of this enzyme are formate and ferricytochrome b1, whereas its 3 products are CO2, ferrocytochrome b1, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is formate:ferricytochrome-b1 oxidoreductase. Other names in common use include formate dehydrogenase, and formate:cytochrome b1 oxidoreductase. This enzyme participates in glyoxylate and dicarboxylate metabolism.
References
EC 1.2.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/5-HT2C%20receptor | {{DISPLAYTITLE:5-HT2C receptor}}
The 5-HT2C receptor is a subtype of 5-HT receptor that binds the endogenous neurotransmitter serotonin (5-hydroxytryptamine, 5-HT). It is a G protein-coupled receptor (GPCR) that is coupled to Gq/G11 and mediates excitatory neurotransmission. HTR2C denotes the human gene encoding for the receptor, that in humans is located at the X chromosome. As males have one copy of the gene and in females one of the two copies of the gene is repressed, polymorphisms at this receptor can affect the two sexes to differing extent.
Structure
At the cell surface the receptor exists as a homodimer. The crystal structure has been known since 2018.
Distribution
5-HT2C receptors are located mainly in the choroid plexus, and in rats is also found in many other brain regions in high concentrations, including parts of the hippocampus, anterior olfactory nucleus, substantia nigra, several brainstem nuclei, amygdala, subthalamic nucleus and lateral habenula. 5-HT2C receptors are also found on epithelial cells lining the ventricles.
Function
The 5-HT2C receptor is one of the many binding sites for serotonin. Activation of this receptor by serotonin inhibits dopamine and norepinephrine release in certain areas of the brain.
5-HT2C receptors are claimed to significantly regulate mood, anxiety, feeding, and reproductive behavior. 5-HT2C receptors regulate dopamine release in the striatum, prefrontal cortex, nucleus accumbens, hippocampus, hypothalamus, and amygdala |
https://en.wikipedia.org/wiki/Formate%20dehydrogenase%20%28cytochrome-c-553%29 | In enzymology, a formate dehydrogenase (cytochrome-c-553) () is an enzyme that catalyzes the chemical reaction
formate + ferricytochrome c-553 CO2 + ferrocytochrome c-553
Thus, the two substrates of this enzyme are formate and ferricytochrome c-553, whereas its two products are CO2 and ferrocytochrome c-553.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is formate:ferricytochrome-c-553 oxidoreductase.
References
EC 1.2.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/CYR61 | Cysteine-rich angiogenic inducer 61 (CYR61) or CCN family member 1 (CCN1), is a matricellular protein that in humans is encoded by the CYR61 gene.
CYR61 is a secreted, extracellular matrix (ECM)-associated signaling protein of the CCN family (CCN intercellular signaling protein). CYR61 is capable of regulating a broad range of cellular activities, including cell adhesion, migration, proliferation, differentiation, apoptosis, and senescence through interaction with cell surface integrin receptors and heparan sulfate proteoglycans. During embryonic development, CYR61 is critical for cardiac septal morphogenesis, blood vessel formation in placenta, and vascular integrity. In adulthood CYR61 plays important roles in inflammation and tissue repair, and is associated with diseases related to chronic inflammation, including rheumatoid arthritis, atherosclerosis, diabetes-related nephropathy and retinopathy, and many different forms of cancers.
CCN protein family
CYR61 was first identified as a protein encoded by a serum-inducible gene in mouse fibroblasts. Other highly conserved homologs were later identified to comprise the CCN protein family (CCN intercellular signaling protein). The CCN acronym is derived from the first three members of the family identified, namely CYR61 (CCN1), CTGF (connective tissue growth factor, or CCN2), and NOV (nephroblastoma overexpressed, or CCN3). These proteins, together with WISP1 (CCN4), WISP2 (CCN5), and WISP3 (CCN6) comprise the six members |
https://en.wikipedia.org/wiki/Formate%20dehydrogenase%20%28NADP%2B%29 | In enzymology, a formate dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
formate + NADP+ CO2 + NADPH
Thus, the two substrates of this enzyme are formate and NADP+, whereas its two products are CO2 and NADPH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is formate:NADP+ oxidoreductase. Other names in common use include NADP+-dependent formate dehydrogenase, and formate dehydrogenase (NADP+). This enzyme participates in methane metabolism. It has 3 cofactors: iron, Tungsten, and Selenium.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.17.1
NADPH-dependent enzymes
Iron enzymes
Tungsten enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/MT-ND4L | MT-ND4L is a gene of the mitochondrial genome coding for the NADH-ubiquinone oxidoreductase chain 4L (ND4L) protein. The ND4L 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. Variants of human MT-ND4L are associated with increased BMI in adults and Leber's Hereditary Optic Neuropathy (LHON).
Structure
The MT-ND4L gene is located in human mitochondrial DNA from base pair 10,469 to 10,765. The MT-ND4L gene produces an 11 kDa protein composed of 98 amino acids. MT-ND4L 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-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-ND4L 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-ND4L gene is the 7-nucleotide gene overlap of its last three codons (5'-CAA TGC TAA-3' coding for Gln, Cys and Stop) with the first three codons of the MT-ND4 gene (5'-ATG CTA AAA-3' coding for amino acids Met-Leu-Lys). With respect to the MT-ND4L reading |
https://en.wikipedia.org/wiki/Gamma-guanidinobutyraldehyde%20dehydrogenase | In enzymology, a gamma-guanidinobutyraldehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction
4-guanidinobutanal + NAD+ + H2O 4-guanidinobutanoate + NADH + 2 H+
The 3 substrates of this enzyme are 4-guanidinobutanal, NAD+, and H2O, whereas its 3 products are 4-guanidinobutanoate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4-guanidinobutanal:NAD+ 1-oxidoreductase. Other names in common use include alpha-guanidinobutyraldehyde dehydrogenase, 4-guanidinobutyraldehyde dehydrogenase, and GBAL dehydrogenase. This enzyme participates in urea cycle and metabolism of amino groups.
References
EC 1.2.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glutamate-5-semialdehyde%20dehydrogenase | In enzymology, a glutamate-5-semialdehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction
L-glutamate 5-semialdehyde + phosphate + NADP+ L-glutamyl 5-phosphate + NADPH + H+
The 3 substrates of this enzyme are L-glutamate 5-semialdehyde, phosphate, and NADP+, whereas its 3 products are L-glutamyl 5-phosphate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-glutamate-5-semialdehyde:NADP+ 5-oxidoreductase (phosphorylating). Other names in common use include beta-glutamylphosphate reductase, gamma-glutamyl phosphate reductase, beta-glutamylphosphate reductase, glutamate semialdehyde dehydrogenase, and glutamate-gamma-semialdehyde dehydrogenase. This enzyme participates in urea cycle and metabolism of amino groups.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 1.2.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glutamyl-tRNA%20reductase | A glutamyl-tRNA reductase () is an enzyme that catalyzes the chemical reaction
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu L-glutamyl-tRNAGlu + NADPH + H+
The 3 substrates of this enzyme are L-glutamate 1-semialdehyde, NADP+, and tRNA(Glu), whereas its 3 products are L-glutamyl-tRNA(Glu), NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, to be specific, those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-glutamate-semialdehyde: NADP+ oxidoreductase (L-glutamyl-tRNAGlu-forming). This enzyme participates in porphyrin and chlorophyll metabolism.
References
EC 1.2.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glutarate-semialdehyde%20dehydrogenase | In enzymology, a glutarate-semialdehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction
glutarate semialdehyde + NAD+ + H2O glutarate + NADH + 2 H+
The 3 substrates of this enzyme are glutarate semialdehyde, NAD+, and H2O, whereas its 3 products are glutarate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is glutarate-semialdehyde:NAD+ oxidoreductase. This enzyme is also called glutarate semialdehyde dehydrogenase. This enzyme participates in lysine degradation.
References
EC 1.2.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glyceraldehyde-3-phosphate%20dehydrogenase%20%28ferredoxin%29 | In enzymology, a glyceraldehyde-3-phosphate dehydrogenase (ferredoxin) () is an enzyme that catalyzes the chemical reaction
D-glyceraldehyde-3-phosphate + H2O + 2 oxidized ferredoxin 3-phospho-D-glycerate + 2 H+ + 2 reduced ferredoxin
The 3 substrates of this enzyme are D-glyceraldehyde-3-phosphate, H2O, and oxidized ferredoxin, whereas its 3 products are 3-phospho-D-glycerate, H+, and reduced ferredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is D-glyceraldehyde-3-phosphate:ferredoxin oxidoreductase. Other names in common use include GAPOR, glyceraldehyde-3-phosphate Fd oxidoreductase, and glyceraldehyde-3-phosphate ferredoxin reductase.
References
EC 1.2.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Syndecan-2 | Syndecan-2 is a protein that in humans is encoded by the SDC2 gene.
Function
The protein encoded by this gene is a transmembrane (type I) heparan sulfate proteoglycan and is a member of the syndecan proteoglycan family. The syndecans mediate cell binding, cell signaling, and cytoskeletal organization and syndecan receptors are required for internalization of the HIV-1 tat protein. The syndecan-2 protein functions as an integral membrane protein and participates in cell proliferation, cell migration and cell-matrix interactions via its receptor for extracellular matrix proteins. Altered syndecan-2 expression has been detected in several different tumor types.
Interactions
SDC2 has been shown to interact with:
CASK,
Laminin, alpha 3, and
EZR
References
Further reading |
https://en.wikipedia.org/wiki/Glyceraldehyde-3-phosphate%20dehydrogenase%20%28NAD%28P%29%2B%29 | In enzymology, a glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) () is an enzyme that catalyzes the chemical reaction
D-glyceraldehyde 3-phosphate + phosphate + NAD(P)+ 3-phospho-D-glyceroyl phosphate + NAD(P)H + H+
The 4 substrates of this enzyme are D-glyceraldehyde 3-phosphate, phosphate, NAD+, and NADP+, whereas its 4 products are 3-phospho-D-glyceroyl phosphate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-glyceraldehyde 3-phosphate:NAD(P)+ oxidoreductase (phosphorylating). Other names in common use include (phosphorylating), triosephosphate dehydrogenase (NAD(P)), and glyceraldehyde-3-phosphate dehydrogenase (NAD(P)) (phosphorylating).
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
P. Mathis (Ed.), Photosynthesis: From Light to Biosphere, vol. 1, Kluwer Academic Publishers, 1995, p. 959-962.
EC 1.2.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glyceraldehyde-3-phosphate%20dehydrogenase%20%28NADP%2B%29%20%28phosphorylating%29 | In enzymology, a glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) () is an enzyme that catalyzes the chemical reaction
D-glyceraldehyde 3-phosphate + phosphate + NADP+ 3-phospho-D-glyceroyl phosphate + NADPH + H+
The 3 substrates of this enzyme are D-glyceraldehyde 3-phosphate, phosphate, and NADP+, whereas its 3 products are 3-phospho-D-glyceroyl phosphate, NADPH, and H+.
Function
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in the Calvin cycle which is an autotrophic carbon fixation pathway.
Nomenclature
The systematic name of this enzyme class is D-glyceraldehyde-3-phosphate:NADP+ oxidoreductase (phosphorylating). Other names in common use include:
dehydrogenase, glyceraldehyde phosphate (nicotinamide adenine dinucleotide phosphate) (phosphorylating)
GAPDH
glyceraldehyde phosphate dehydrogenase (nicotinamide adenine dinucleotide phosphate) (phosphorylating)
glyceraldehyde-3-phosphate dehydrogenase (NADP) (phosphorylating)
NADP-dependent glyceraldehyde phosphate dehydrogenase
NADP-glyceraldehyde phosphate dehydrogenase
NADP-glyceraldehyde-3-phosphate dehydrogenase
NADP-triose phosphate dehydrogenase
triosephosphate dehydrogenase (NADP)
References
Further reading
EC 1.2.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glyceraldehyde-3-phosphate%20dehydrogenase%20%28phosphorylating%29 | In enzymology, a glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) () is an enzyme that catalyzes the chemical reaction
D-glyceraldehyde 3-phosphate + phosphate + NAD+ 3-phospho-D-glyceroyl phosphate + NADH + H+
The 3 substrates of this enzyme are D-glyceraldehyde 3-phosphate, phosphate, and NAD+, whereas its 3 products are 3-phospho-D-glyceroyl phosphate, NADH, and H+. This enzyme participates in glycolysis / gluconeogenesis.
Nomenclature
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating). Other names in common use include triosephosphate dehydrogenase, dehydrogenase, glyceraldehyde phosphate, phosphoglyceraldehyde dehydrogenase, 3-phosphoglyceraldehyde dehydrogenase, NAD+-dependent glyceraldehyde phosphate dehydrogenase, glyceraldehyde phosphate dehydrogenase (NAD+), glyceraldehyde-3-phosphate dehydrogenase (NAD+), NADH-glyceraldehyde phosphate dehydrogenase, and glyceraldehyde-3-P-dehydrogenase.
References
Further reading
EC 1.2.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Somatostatin%20receptor%202 | Somatostatin receptor type 2 is a protein that in humans is encoded by the SSTR2 gene.
The SSTR2 gene is located on chromosome 17 on the long arm in position 25.1 in humans. It is also found in most other vertebrates.
The somatostatin receptor 2 (SSTR2), which belongs to the G-protein coupled receptor family, is a protein which is most highly expressed in the pancreas (both alpha- and beta-cells), but also in other tissues such as the cerebrum and kidney and in lower amount in the jejunum, colon and liver. In the pancreas, after binding to somatostatin, it inhibits the secretion of peptide hormones from pancreatic islets. During development, it stimulates neuronal migration and axon outgrowth.
The somatostatin receptor 2 is expressed in most tumors. Patients with neuroendocrine tumors that over-express the somatostatin receptor 2 have an improved prognosis. The over expression of SSTR2 in tumors can be exploited to selectively deliver radio-peptides to tumors to either detect or destroy them. Somatostatin receptor 2 also has the ability to stimulate apoptosis in many cells including cancer cells. The somatostatin receptor 2 is also being looked at as a possible target in cancer treatment for its ability to inhibit tumor growth.
Function
The gene for somatostatin receptor 2, SSTR2 for short, is responsible for making a receptor for the signalling peptide, somatostatin (SST). Production occurs in the central nervous system, especially the hypothalamus, as well as the dige |
https://en.wikipedia.org/wiki/Glycolaldehyde%20dehydrogenase | In enzymology, a glycolaldehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction
glycolaldehyde + NAD+ + H2O glycolate + NADH + H+
The 3 substrates of this enzyme are glycolaldehyde, NAD+, and H2O, whereas its 3 products are glycolate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is glycolaldehyde:NAD+ oxidoreductase. This enzyme is also called glycol aldehyde dehydrogenase. This enzyme participates in glyoxylate and dicarboxylate metabolism.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 1.2.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glyoxylate%20dehydrogenase%20%28acylating%29 | In enzymology, a glyoxylate dehydrogenase (acylating) () is an enzyme that catalyzes the chemical reaction
glyoxylate + CoA + NADP+ oxalyl-CoA + NADPH + H+
The 3 substrates of this enzyme are glyoxylate, CoA, and NADP+, whereas its 3 products are oxalyl-CoA, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is glyoxylate:NADP+ oxidoreductase (CoA-oxalylating). This enzyme participates in glyoxylate and dicarboxylate metabolism.
References
EC 1.2.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glyoxylate%20oxidase | In enzymology, a glyoxylate oxidase () is an enzyme that catalyzes the chemical reaction
glyoxylate + H2O + O2 oxalate + H2O2
The 3 substrates of this enzyme are glyoxylate, H2O, and O2, whereas its two products are oxalate and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is glyoxylate:oxygen oxidoreductase. This enzyme participates in glyoxylate and dicarboxylate metabolism.
References
EC 1.2.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Hexadecanal%20dehydrogenase%20%28acylating%29 | In enzymology, a hexadecanal dehydrogenase (acylating) () is an enzyme that catalyzes the chemical reaction
hexadecanal + CoA + NAD+ hexadecanoyl-CoA + NADH + H+
The 3 substrates of this enzyme are hexadecanal, CoA, and NAD+, whereas its 3 products are hexadecanoyl-CoA, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is hexadecanal:NAD+ oxidoreductase (CoA-acylating). This enzyme is also called fatty acyl-CoA reductase.
References
EC 1.2.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Indole-3-acetaldehyde%20oxidase | In enzymology, an indole-3-acetaldehyde oxidase () is an enzyme that catalyzes the chemical reaction
(indol-3-yl)acetaldehyde + H2O + O2 (indol-3-yl)acetate + H2O2
The 3 substrates of this enzyme are (indol-3-yl)acetaldehyde, H2O, and O2, whereas its two products are (indol-3-yl)acetate and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is (indol-3-yl)acetaldehyde:oxygen oxidoreductase. Other names in common use include indoleacetaldehyde oxidase, IAAld oxidase, AO1, and indole-3-acetaldehyde:oxygen oxidoreductase. This enzyme participates in tryptophan metabolism. It has 3 cofactors: FAD, Heme, and Molybdenum.
References
EC 1.2.3
Flavoproteins
Heme enzymes
Molybdenum enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Indolepyruvate%20ferredoxin%20oxidoreductase | In enzymology, an indolepyruvate ferredoxin oxidoreductase () is an enzyme that catalyzes the chemical reaction
(indol-3-yl)pyruvate + CoA + oxidized ferredoxin S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin
The 3 substrates of this enzyme are (indol-3-yl)pyruvate, CoA, and oxidized ferredoxin, whereas its 3 products are S-2-(indol-3-yl)acetyl-CoA, CO2, and reduced ferredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is 3-(indol-3-yl)pyruvate:ferredoxin oxidoreductase (decarboxylating, CoA-indole-acetylating). Other names in common use include 3-(indol-3-yl)pyruvate synthase (ferredoxin), and IOR.
References
EC 1.2.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Lactaldehyde%20dehydrogenase | In enzymology, a lactaldehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction
(S)-lactaldehyde + NAD+ + H2O (S)-lactate + NADH + 2 H+
The 3 substrates of this enzyme are (S)-lactaldehyde, NAD+, and H2O, whereas its 3 products are (S)-lactate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-lactaldehyde:NAD+ oxidoreductase. Other names in common use include L-lactaldehyde:NAD+ oxidoreductase, and nicotinamide adenine dinucleotide (NAD+)-linked dehydrogenase. This enzyme participates in pyruvate metabolism.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 1.2.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/L-aminoadipate-semialdehyde%20dehydrogenase | In enzymology, a L-aminoadipate-semialdehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction
L-2-aminoadipate 6-semialdehyde + NAD(P)+ + H2O L-2-aminoadipate + NAD(P)H + H+
The 4 substrates of this enzyme are L-2-aminoadipate 6-semialdehyde, NAD+, NADP+, and H2O, whereas its 4 products are L-2-aminoadipate, NADH, NADPH, and H+.
This enzyme participates in lysine biosynthesis and biodegradation.
Nomenclature
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-2-aminoadipate-6-semialdehyde:NAD(P)+ 6-oxidoreductase. Other names in common use include:
aminoadipate semialdehyde dehydrogenase,
2-aminoadipate semialdehyde dehydrogenase,
alpha-aminoadipate-semialdehyde dehydrogenase,
alpha-aminoadipate reductase,
2-aminoadipic semialdehyde dehydrogenase,
L-alpha-aminoadipate delta-semialdehyde oxidoreductase,
L-alpha-aminoadipate delta-semialdehyde:NAD+ oxidoreductase,
L-alpha-aminoadipate delta-semialdehyde:nicotinamide adenine,
and dinucleotide oxidoreductase.
References
EC 1.2.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Long-chain-fatty-acyl-CoA%20reductase | In enzymology, a long-chain-fatty-acyl-CoA reductase () is an enzyme that catalyzes the chemical reaction
a long-chain aldehyde + CoA + NADP+ a long-chain acyl-CoA + NADPH + H+
The 3 substrates of this enzyme are long-chain aldehyde, CoA, and NADP+, whereas its 3 products are long-chain acyl-CoA, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is long-chain-aldehyde:NADP+ oxidoreductase (acyl-CoA-forming). Other names in common use include acyl-CoA reductase, and acyl coenzyme A reductase.
References
EC 1.2.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Malonate-semialdehyde%20dehydrogenase | In enzymology, a malonate-semialdehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction
3-oxopropanoate + NAD(P)+ + H2O malonate + NAD(P)H + 2 H+
The 4 substrates of this enzyme are 3-oxopropanoate, NAD+, NADP+, and H2O, whereas its 4 products are malonate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-oxopropanoate:NAD(P)+ oxidoreductase. This enzyme participates in beta-alanine metabolism.
References
EC 1.2.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Malonate-semialdehyde%20dehydrogenase%20%28acetylating%29 | In enzymology, a malonate-semialdehyde dehydrogenase (acetylating) () is an enzyme that catalyzes the chemical reaction
3-oxopropanoate + CoA + NAD(P)+ acetyl-CoA + CO2 + NAD(P)H
The 4 substrates of this enzyme are 3-oxopropanoate, CoA, NAD+, and NADP+, whereas its 4 products are acetyl-CoA, CO2, NADH, and NADPH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-oxopropanoate:NAD(P)+ oxidoreductase (decarboxylating, CoA-acetylating). This enzyme is also called malonic semialdehyde oxidative decarboxylase. This enzyme participates in 4 metabolic pathways: inositol metabolism, alanine and aspartate metabolism, beta-alanine metabolism, and propanoate metabolism.
References
Further reading
EC 1.2.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Methylmalonate-semialdehyde%20dehydrogenase%20%28acylating%29 | In enzymology, a methylmalonate-semialdehyde dehydrogenase (acylating) () is an enzyme that catalyzes the chemical reaction
2-methyl-3-oxopropanoate + CoA + H2O + NAD+ propanoyl-CoA + HCO3- + NADH
The 4 substrates of this enzyme are 2-methyl-3-oxopropanoate, CoA, H2O, and NAD+, whereas its 3 products are propanoyl-CoA, HCO3-, and NADH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-methyl-3-oxopropanoate:NAD+ 3-oxidoreductase (CoA-propanoylating). Other names in common use include MSDH, and MMSA dehydrogenase. This enzyme participates in 3 metabolic pathways: inositol metabolism, valine, leucine and isoleucine degradation, and propanoate metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.2.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Mycothiol-dependent%20formaldehyde%20dehydrogenase | In enzymology, a mycothiol-dependent formaldehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction
formaldehyde + mycothiol + NAD+ S-formylmycothiol + NADH + 2 H+
The 3 substrates of this enzyme are formaldehyde, mycothiol, and NAD+, whereas its 3 products are S-formylmycothiol, NADH, and H+. This enzyme catalyses the following chemical reaction
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is formaldehyde:NAD+ oxidoreductase (mycothiol-formylating). This enzyme is also called NAD/factor-dependent formaldehyde dehydrogenase or S-(hydroxymethyl)mycothiol dehydrogenase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-acetyl-gamma-glutamyl-phosphate%20reductase | In enzymology, a N-acetyl-gamma-glutamyl-phosphate reductase () is an enzyme that catalyzes the chemical reaction
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate N-acetyl-L-glutamyl 5-phosphate + NADPH + H+
The 3 substrates of this enzyme are N-acetyl-L-glutamate 5-semialdehyde, NADP+, and phosphate, whereas its 3 products are N-acetyl-L-glutamyl 5-phosphate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is N-acetyl-L-glutamate-5-semialdehyde:NADP+ 5-oxidoreductase (phosphorylating). Other names in common use include reductase, acetyl-gamma-glutamyl phosphate, N-acetylglutamate 5-semialdehyde dehydrogenase, N-acetylglutamic gamma-semialdehyde dehydrogenase, N-acetyl-L-glutamate gamma-semialdehyde:NADP+ oxidoreductase, and (phosphorylating). This enzyme participates in urea cycle and metabolism of amino groups.
Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , and .
References
EC 1.2.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Oxalate%20oxidase | In enzymology, an oxalate oxidase () is an oxalate degrading enzyme that catalyzes the chemical reaction:
oxalate + O2 + 2 H+ 2 CO2 + H2O2
The 3 substrates of this enzyme are oxalate, O2, and H+, whereas its two products are CO2 and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is oxalate:oxygen oxidoreductase. Other names in common use include aero-oxalo dehydrogenase, and oxalic acid oxidase. This enzyme participates in glyoxylate and dicarboxylate metabolism. It uses Manganese as a cofactor.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 1.2.3
Flavoproteins
Manganese enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Oxoglutarate%20dehydrogenase%20%28NADP%2B%29 | In enzymology, an oxoglutarate dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
2-oxoglutarate + CoA + NADP+ succinyl-CoA + CO2 + NADPH
The 3 substrates of this enzyme are 2-oxoglutarate, CoA, and NADP+, whereas its 3 products are succinyl-CoA, CO2, and NADPH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-oxoglutarate:NADP+ 2-oxidoreductase (CoA-succinylating). This enzyme is also called oxoglutarate dehydrogenase (NADP+).
References
EC 1.2.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phenylacetaldehyde%20dehydrogenase | In enzymology, a phenylacetaldehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction
phenylacetaldehyde + NAD+ + H2O phenylacetate + NADH + 2 H+
The 3 substrates of this enzyme are phenylacetaldehyde, NAD+, and H2O, whereas its 3 products are phenylacetate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is phenylacetaldehyde:NAD+ oxidoreductase. This enzyme participates in phenylalanine metabolism and styrene degradation.
References
EC 1.2.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phenylglyoxylate%20dehydrogenase%20%28acylating%29 | In enzymology, a phenylglyoxylate dehydrogenase (acylating; ) is an enzyme that catalyzes the chemical reaction
phenylglyoxylate + NAD+ + CoA-SH benzoyl-S-CoA + CO2 + NADH
The three substrates of this enzyme are phenylglyoxylate, NAD+, and CoA-SH, whereas its 3 products are benzoyl-S-CoA, CO2, and NADH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is phenylglyoxylate:NAD+ oxidoreductase. It has 3 cofactors: FAD, Thiamin diphosphate, and Iron-sulfur.
References
EC 1.2.1
NADH-dependent enzymes
Flavoproteins
Thiamin diphosphate enzymes
Iron-sulfur enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pyridoxal%20oxidase | In enzymology, a pyridoxal oxidase () is an enzyme that catalyzes the chemical reaction
pyridoxal + H2O + O2 4-pyridoxate + (?)
The 3 substrates of this enzyme are pyridoxal, H2O, and O2, whereas its product is 4-pyridoxate.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is pyridoxal:oxygen 4-oxidoreductase. This enzyme participates in vitamin B6 metabolism. It employs one cofactor, molybdenum.
References
EC 1.2.3
Molybdenum enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pyruvate%20dehydrogenase%20%28cytochrome%29 | In enzymology, a pyruvate dehydrogenase (cytochrome) () is an enzyme that catalyzes the chemical reaction
pyruvate + ferricytochrome b1 + H2O acetate + CO2 + ferrocytochrome b1
The 3 substrates of this enzyme are pyruvate, ferricytochrome b1, and H2O, whereas its 3 products are acetate, CO2, and ferrocytochrome b1.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is pyruvate:ferricytochrome-b1 oxidoreductase. Other names in common use include pyruvate dehydrogenase, pyruvic dehydrogenase, pyruvic (cytochrome b1) dehydrogenase, pyruvate:ubiquinone-8-oxidoreductase, and pyruvate oxidase (ambiguous). This enzyme participates in pyruvate metabolism. It has 2 cofactors: FAD, and Thiamin diphosphate.
References
EC 1.2.2
Flavoproteins
Thiamin diphosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pyruvate%20oxidase | In enzymology, a pyruvate oxidase () is an enzyme that catalyzes the chemical reaction
pyruvate + phosphate + O2 acetyl phosphate + CO2 + H2O2
The 3 substrates of this enzyme are pyruvate, phosphate, and O2, whereas its 3 products are acetyl phosphate, CO2, and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is pyruvate:oxygen 2-oxidoreductase (phosphorylating). Other names in common use include pyruvic oxidase, and phosphate-dependent pyruvate oxidase. This enzyme participates in pyruvate metabolism. It has 2 cofactors: FAD, and Thiamin diphosphate.
Structural studies
As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , and .
References
EC 1.2.3
Flavoproteins
Thiamin diphosphate enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Pyruvate%20oxidase%20%28CoA-acetylating%29 | In enzymology, a pyruvate oxidase (CoA-acetylating) () is an enzyme that catalyzes the chemical reaction
pyruvate + CoA + O2 acetyl-CoA + CO2 + H2O2
The 3 substrates of this enzyme are pyruvate, CoA, and O2, whereas its 3 products are acetyl-CoA, CO2, and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is pyruvate:oxygen 2-oxidoreductase (CoA-acetylating). This enzyme participates in pyruvate metabolism. It employs one cofactor, FAD.
References
EC 1.2.3
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pyruvate%20synthase | In enzymology, a pyruvate synthase () is an enzyme that catalyzes the interconversion of pyruvate and acetyl-CoA. It is also called pyruvate:ferredoxin oxidoreductase (PFOR).
The relevant equilibrium catalysed by PFOR is:
pyruvate + CoA + oxidized ferredoxin acetyl-CoA + CO2 + reduced ferredoxin
The 3 substrates of this enzyme are pyruvate, CoA, and oxidized ferredoxin, whereas its 3 products are acetyl-CoA, CO2, and reduced ferredoxin.
Function
This enzyme participates in 4 metabolic pathways: pyruvate metabolism, propanoate metabolism, butanoate metabolism, and reductive carboxylate cycle ( fixation).
Its major role is the extraction of reducing equivalents by the decarboxylation. In aerobic organisms, this conversion is catalysed by pyruvate dehydrogenase, also uses thiamine pyrophosphate (TPP) but relies on lipoate as the electron acceptor. Unlike the aerobic enzyme complex PFOR transfers reducing equivalents to flavins or iron-sulflur clusters. This process links glycolysis to the Wood–Ljungdahl pathway.
Nomenclature
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is pyruvate:ferredoxin 2-oxidoreductase (CoA-acetylating). Other names in common use include:
pyruvate oxidoreductase,
pyruvate synthetase,
pyruvate:ferredoxin oxidoreductase,
pyruvic-ferredoxin oxidoreductase.
Structure
PFOR adopts a dime |
https://en.wikipedia.org/wiki/%28R%29-dehydropantoate%20dehydrogenase | In enzymology, a (R)-dehydropantoate dehydrogenase () is an enzyme that catalyzes the chemical reaction
(R)-4-dehydropantoate + NAD + HO (R)-3,3-dimethylmalate + NADH + 2 H
The 3 substrates of this enzyme are (R)-4-dehydropantoate, NAD, and HO, whereas its 3 products are (R)-3,3-dimethylmalate, NADH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-4-dehydropantoate:NAD+ 4-oxidoreductase. Other names in common use include D-aldopantoate dehydrogenase, D-2-hydroxy-3,3-dimethyl-3-formylpropionate:diphosphopyridine, and nucleotide (DPN+) oxidoreductase. This enzyme participates in pantothenate and coa biosynthesis.
References
EC 1.2.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Retinal%20dehydrogenase | In enzymology, a retinal dehydrogenase, also known as retinaldehyde dehydrogenase (RALDH), catalyzes the chemical reaction converting retinal to retinoic acid. This enzyme belongs to the family of oxidoreductases, specifically the class acting on aldehyde or oxo- donor groups with NAD+ or NADP+ as acceptor groups, the systematic name being retinal:NAD+ oxidoreductase. This enzyme participates in retinol metabolism. The general scheme for the reaction catalyzed by this enzyme is:
retinal + NAD+ + H2O retinoic acid + NADH + H+
Structure
Retinal dehydrogenase is a tetramer of identical units, consisting of a dimer of dimers. Retinal dehydrogenase monomers are composed of three domains: a nucleotide-binding domain, a tetramerization domain, and a catalytic domain. The dimer can be pictured as an "X" with the dimers forming upper and lower halves that cross over each other. Interestingly, the nucleotide-binding domain of retinal dehydrogenase contains 5 instead of the usual 6 β-strands in the Rossman fold. This appears to be conserved across many aldehyde dehydrogenases. The tetramerization domains lie equatorially along the "X" and the nucleotide binding regions appear on the tips of the "X". Nearby the tetramerization domain lies a 12 Å deep tunnel that gives the substrate access to the key catalytic regions. Residues near the C-terminal end of the catalytic domain have been found to impart specificity in other aldehyde dehydrogenases. Common to many aldehyde dehydrogenases |
https://en.wikipedia.org/wiki/Retinal%20oxidase | In enzymology, a retinal oxidase () is an enzyme that catalyzes the chemical reaction
retinal + O2 + H2O retinoic acid + H2O2
The 3 substrates of this enzyme are retinal, O2, and H2O, whereas its two products are retinoic acid and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is retinal:oxygen oxidoreductase. This enzyme is also called retinene oxidase. This enzyme participates in retinol metabolism.
References
EC 1.2.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Succinate-semialdehyde%20dehydrogenase%20%28NAD%28P%29%2B%29 | In enzymology, a succinate-semialdehyde dehydrogenase [NAD(P)+] () is an enzyme that catalyzes the chemical reaction
succinate semialdehyde + NAD(P)+ + H2O succinate + NAD(P)H + 2 H+
The 4 substrates of this enzyme are succinate semialdehyde, NAD+, NADP+, and H2O, whereas its 4 products are succinate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is succinate-semialdehyde:NAD(P)+ oxidoreductase. Other names in common use include succinate semialdehyde dehydrogenase (nicotinamide adenine, dinucleotide (phosphate)), and succinate-semialdehyde dehydrogenase [NAD(P)+]. This enzyme participates in 3 metabolic pathways: glutamate metabolism, tyrosine metabolism, and butanoate metabolism.
References
Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 203-221.
EC 1.2.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Vanillin%20dehydrogenase | In enzymology, a vanillin dehydrogenase () is an enzyme that catalyzes the chemical reaction
+ NAD+ + H2O + NADH + H+
The 3 substrates of this enzyme are vanillin, NAD+, and H2O, whereas its 3 products are vanillate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is vanillin:NAD+ oxidoreductase. This enzyme participates in 2,4-dichlorobenzoate degradation.
References
EC 1.2.1
NADH-dependent enzymes
Enzymes of unknown structure |
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