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https://en.wikipedia.org/wiki/Pethidine%20intermediate%20A | Pethidine intermediate A is a 4-phenylpiperidine derivative that is a precursor to the opioid analgesic drug pethidine (meperidine). It is not known to have any analgesic activity in its own right, however other derivatives of pethidine with a 4-cyano group in place of the carboxylate ethyl ester have been found to be active, so pethidine intermediate A might also show opioid effects. It is scheduled by UN Single Convention on Narcotic Drugs. It is a Schedule II Narcotic controlled substance in the United States and has an ACSCN of 9232. The 2014 annual manufacturing quota was 6 grammes (as an end product, presumably for research use).
See also
Moramide intermediate
Methadone intermediate
Pethidine intermediate B (norpethidine)
Pethidine intermediate C (pethidinic acid)
References
Synthetic opioids
4-Phenylpiperidines
Nitriles |
https://en.wikipedia.org/wiki/Nseluka | Nseluka is a small town in northern Zambia. It is on the M1 road, which heads to Kasama in the south and Mbala/Mpulungu in the north.
Statistics
elevation –
Transport
It has a station on the TAZARA railway. It is the proposed junction for a branch railway to Mpulungu on the shores of Lake Tanganyika.
See also
Transport in Zambia
References
Populated places in Northern Province, Zambia |
https://en.wikipedia.org/wiki/NSP2%20%28rotavirus%29 | NSP2 (NS35), is a rotavirus nonstructural RNA-binding protein that accumulates in cytoplasmic inclusions (viroplasms) and is required for genome replication. NSP2 is closely associated in vivo with the viral replicase. The non-structural protein NSP5 plays a role in the structure of viroplasms mediated by its interaction with NSP2.
References
Rotaviruses
Viral nonstructural proteins |
https://en.wikipedia.org/wiki/NSP3%20%28rotavirus%29 | Rotavirus protein NSP3 (NS34) is bound to the 3' end consensus sequence of viral mRNAs in infected cells.
Four nucleotides are the minimal requirement for RNA recognition by rotavirus nonstructural protein NSP3: using short oligoribonucleotides, it was established that the minimal RNA sequence required for binding of NSP3A is GACC.
Rotavirus RNA-binding protein NSP3 interacts with eIF4GI and evicts the poly(A)-binding protein from eIF4F. And NSP3A, by taking the place of PABP on eIF4GI, is responsible for the shut-off of cellular protein synthesis.
Expression of NSP3 in mammalian cells allows the efficient translation of virus-like mRNA: NSP3 forms a link between viral mRNA and the cellular translation machinery and hence is a functional analogue of cellular poly(A)-binding protein.
Site-directed mutagenesis and isothermal titration calorimetry documented that NSP3 and PABP use analogous eIF4G recognition strategies, despite marked differences in tertiary structure.
Using the yeast two-hybrid assay, RoXan a novel cellular protein was found to bind NSP3. The interaction between NSP3 and RoXaN does not impair the interaction between NSP3 and eIF4GI, and a ternary complex made of NSP3, RoXaN, and eIF4G I can be detected in rotavirus-infected cells, implicating RoXaN in translation regulation.
References
Rotaviruses
RNA-binding proteins
Viral nonstructural proteins |
https://en.wikipedia.org/wiki/Recombinase-mediated%20cassette%20exchange | RMCE (recombinase-mediated cassette exchange) is a procedure in reverse genetics allowing the systematic, repeated modification of higher eukaryotic genomes by targeted integration, based on the features of site-specific recombination processes (SSRs). For RMCE, this is achieved by the clean exchange of a preexisting gene cassette for an analogous cassette carrying the "gene of interest" (GOI).
The genetic modification of mammalian cells is a standard procedure for the production of correctly modified proteins with pharmaceutical relevance. To be successful, the transfer and expression of the transgene has to be highly efficient and should have a largely predictable outcome. Current developments in the field of gene therapy are based on the same principles. Traditional procedures used for transfer of GOIs are not sufficiently reliable, mostly because the relevant epigenetic influences have not been sufficiently explored: transgenes integrate into chromosomes with low efficiency and at loci that provide only sub-optimal conditions for their expression. As a consequence the newly introduced information may not be realized (expressed), the gene(s) may be lost and/or re-insert and they may render the target cells in unstable state. It is exactly this point where RMCE enters the field. The procedure was introduced in 1994 and it uses the tools yeasts and bacteriophages have evolved for the efficient replication of important genetic information:
General principles
Most yeast s |
https://en.wikipedia.org/wiki/M/M/1%20queue | In queueing theory, a discipline within the mathematical theory of probability, an M/M/1 queue represents the queue length in a system having a single server, where arrivals are determined by a Poisson process and job service times have an exponential distribution. The model name is written in Kendall's notation. The model is the most elementary of queueing models and an attractive object of study as closed-form expressions can be obtained for many metrics of interest in this model. An extension of this model with more than one server is the M/M/c queue.
Model definition
An M/M/1 queue is a stochastic process whose state space is the set {0,1,2,3,...} where the value corresponds to the number of customers in the system, including any currently in service.
Arrivals occur at rate λ according to a Poisson process and move the process from state i to i + 1.
Service times have an exponential distribution with rate parameter μ in the M/M/1 queue, where 1/μ is the mean service time.
All arrival times and services times are (usually) assumed to be independent of one another.
A single server serves customers one at a time from the front of the queue, according to a first-come, first-served discipline. When the service is complete the customer leaves the queue and the number of customers in the system reduces by one.
The buffer is of infinite size, so there is no limit on the number of customers it can contain.
The model can be described as a continuous time Markov chain with |
https://en.wikipedia.org/wiki/NSP4%20%28rotavirus%29 | The rotavirus nonstructural protein NSP4 was the first viral enterotoxin discovered. It is a viroporin and induces diarrhea and causes Ca2+-dependent transepithelial secretion.
A transmembrane glycoprotein, NSP4 is organized into three main domains: a three-helical TM domain in the N-terminus (also a viroporin domain), a central cytoplasmic coiled-coil domain for multimerization, and an C-terminal flexible region. It can also be secreted out of the cell. As of 2019, only structures of the central domain, which is responsible for diarrhea, has been solved. It oligomerizes into dimeric, tetrameric, pentameric, and even higher-order forms.
References
Rotaviruses
Viral nonstructural proteins |
https://en.wikipedia.org/wiki/NSP5%20%28rotavirus%29 | NSP5 (nonstructural protein 5) encoded by genome segment 11 of group A rotaviruses. In virus-infected cells NSP5 accumulates in the viroplasms. NSP5 has been shown to be autophosphorylated.
Interaction of NSP5 with NSP2 was also demonstrated. In rotavirus-infected cells, the non-structural proteins NSP5 and NSP2 localize in complexes called viroplasms, where replication and assembly occur and they can drive the formation of viroplasm-like structures in the absence of other rotaviral proteins and rotavirus replication.
There is no atomic-resolution structure of NSP5 determined as of June 2019. However, the low resolution three-dimensional structure of the NSP2-NSP5 assembly has been observed by cryo-EM. NSP5 occupies the same site as RNA when binding to NSP2. The EM data from this 2006 study has not been published.
References
Rotaviruses
Viral nonstructural proteins |
https://en.wikipedia.org/wiki/NSP6%20%28rotavirus%29 | Putative transmembrane domain more commonly known as Non-structural Protein 6 (NSP6) is one of the two non-structural proteins that gene 11 in rotavirus encodes for alongside NSP5. NSP6 is composed of six transmembrane domains and a C terminal tail. In contrast to the other rotavirus non-structural proteins, NSP6 was found to have a high rate of turnover, being completely degraded within 2 hours of synthesis. NSP6 was found to be a sequence-independent nucleic acid binding protein, with similar affinities for ssRNA and dsRNA
It has been determined that NSP6 has three crucial functions that it conducts. As messages flow among the replication organelle and the endoplasmic reticulum (ER) NSP6 acts as a filter. In this case, NSP6 hinders the access of ER luminal proteins to the DMVs but permits the passing of lipids. Next NSP6 arranges DMV clusters, since the DMV clusters are organized by NSP6 it can reconstruct them with LD-derived Lipids. Lastly, through LD-tethering complex DFCP1-RAB18 intervenes in the contact of lipid droplets (LDs).
Since NSP6 is one of two non-structural proteins that gene 11 codes for NSP6 is found in both α and β coronaviruses and produces autophagosomes. While NSP6 is found to produce a substantial amount of autophagosomes, through the analysis of MAP1LC3B puncta it is observed that autophagosomes produced by NSP6 are much smaller in size. As indicated by the statistical analysis of WIPI2 puncta the size of NSP6-produced autophagosomes is restricted |
https://en.wikipedia.org/wiki/SHC1 | SHC-transforming protein 1 is a protein that in humans is encoded by the SHC1 gene. SHC has been found to be important in the regulation of apoptosis and drug resistance in mammalian cells.
SCOP classifies the 3D structure as belonging to the SH2 domain family.
Gene and expression
The gene SHC1 is located on chromosome 1 and encodes 3 main protein isoforms: p66SHC, p52SHC and p46SHC. These proteins differ in activity and subcellular locations, p66 is the longest and while the p52 and p46 link activated receptor tyrosine kinase to the RAS pathway. The protein SHC1 also acts as a scaffold protein which is used in cell surface receptors. The three proteins that SHC1 codes for have distinctly different molecular weights. All three SHC1 proteins share the same domain arrangement consisting of an N-terminal phosphotyrosine-binding(PTB) domain and a C-terminal Src-homology2(SH2) domain. Both of the domains for the three proteins can bind to tyrosine-phosphorylated proteins but they are different in their phosphopeptide-binding specificities. P66SHC is characterized by having an additional N-terminal CH2 domain.
Function
Overexpression of SHC proteins are associated with cancer mitogenesis, carcinogenesis and metastasis. The SHC and its adaptor proteins transmit signaling of the cell surface receptors such as EGFR, erbV-2 and insulin receptors. p52SHC and p46SHC activate the Ras-ERK pathway. p66SHC inhibits ERK1/2 activity and antagonize mitogenic and survival abilities of T- |
https://en.wikipedia.org/wiki/Caveolin%201 | Caveolin-1 is a protein that in humans is encoded by the CAV1 gene.
Function
The scaffolding protein encoded by this gene is the main component of the caveolae plasma membranes found in most cell types. The protein links integrin subunits to the tyrosine kinase FYN, an initiating step in coupling integrins to the Ras-ERK pathway and promoting cell cycle progression. The gene is a tumor suppressor gene candidate and a negative regulator of the Ras-p42/44 MAP kinase cascade. CAV1 and CAV2 are located next to each other on chromosome 7 and express colocalizing proteins that form a stable hetero-oligomeric complex. By using alternative initiation codons in the same reading frame, two isoforms (alpha and beta) are encoded by a single transcript from this gene.
Interactions
Caveolin 1 has been shown to interact with heterotrimeric G proteins,
Src tyrosine kinases (Src, Lyn) and H-Ras,
cholesterol,
TGF beta receptor 1,
endothelial NOS,
androgen receptor,
amyloid precursor protein,
gap junction protein, alpha 1,
nitric oxide synthase 2A, epidermal growth factor receptor, endothelin receptor type B, PDGFRB, PDGFRA, PTGS2, TRAF2, estrogen receptor alpha, caveolin 2, PLD2, Bruton's tyrosine kinase, and SCP2. All these interactions are through a caveolin-scaffolding domain (CSD) within caveolin-1 molecule. Molecules that interact with caveolin-1 contain caveolin-binding motifs (CBM).
See also
Caveolin
References
Further reading
Genes
Human proteins |
https://en.wikipedia.org/wiki/Nitric%20oxide%20synthase%202%20%28inducible%29 | Nitric oxide synthase, inducible is an enzyme which is encoded by the NOS2 gene in humans and mice.
Genetics
Three related pseudogenes are located within the Smith-Magenis syndrome region on chromosome 17. Alternative splicing of this gene results in two transcript variants encoding different isoforms.
Location
Nitric oxide synthase is expressed in epithelial cells of the liver, lung and bone marrow. It is inducible by a combination of lipopolysaccharide and certain cytokines.
Function
Nitric oxide is a reactive free radical mediating in neurotransmission, antimicrobial and antitumoral activities.
In mice, the function of Nos2 in immunity against a number of viruses, bacteria, fungi, and parasites has been well characterized, whereas in humans the role of NOS2 has remained elusive and controversial. Nos2 is important for protective immunity against CMV.
Caveolin 1 has been shown to interact with Nitric oxide synthase 2A. and Rac2.
Deficiency
Autosomal recessive NOS2 deficiency has been described in mice. They lack the gene encoding nitric oxide synthase 2 (Nos2) and are susceptible to murine CMV infection.
In February 2020, the same autosomal recessive, complete NOS2 deficiency was described in a human. A 51-year-old previously healthy person died after 29 months of progressive CMV infection due to respiratory failure secondary to CMV pneumonitis, CMV encephalitis, and hemophagocytic lymphohistiocytosis. Whole-exome sequencing on genomic DNA from his blood showed he h |
https://en.wikipedia.org/wiki/Endothelin%201 | Endothelin 1 (ET-1), also known as preproendothelin-1 (PPET1), is a potent vasoconstrictor peptide produced by vascular endothelial cells. The protein encoded by this gene EDN1 is proteolytically processed to release endothelin 1. Endothelin 1 is one of three isoforms of human endothelin.
Sources
Preproendothelin is precursor of the peptide ET-1. Endothelial cells convert preproendothelin to proendothelin and subsequently to mature endothelin, which the cells release.
Clinical significance
Endothelin-1 receptor antagonists (Bosentan) are used in the treatment of pulmonary hypertension. Use of these antagonists prevents pulmonary arterial constriction and thus inhibits pulmonary hypertension.
As of 2020, the role of endothelin-1 in affecting lipid metabolism and insulin resistance in obesity mechanisms was under clinical research.
References
External links
Endothelin receptor agonists |
https://en.wikipedia.org/wiki/GJB2 | Gap junction beta-2 protein (GJB2), also known as connexin 26 (Cx26) — is a protein that in humans is encoded by the GJB2 gene.
Clinical significance
Defects in this gene lead to the most common form of congenital deafness in developed countries, called DFNB1 (also known as connexin 26 deafness or GJB2-related deafness). One fairly common mutation is the deletion of one guanine from a string of six, resulting in a frameshift and termination of the protein at amino acid number 13. Having two copies of this mutation results in deafness.
Connexin 26 also plays a role in tumor suppression through mediation of the cell cycle. The abnormal expression of Cx26, correlated with several types of human cancers, may serve as a prognostic factor for cancers such as colorectal cancer, breast cancer, and bladder cancer. Furthermore, Cx26 over-expression is suggested to promote cancer development by facilitating cell migration and invasion and by stimulating the self-perpetuation ability of cancer stem cells.
Function
Gap junctions were first characterized by electron microscopy as regionally specialized structures on plasma membranes of contacting adherent cells. These structures were shown to consist of cell-to-cell channels. Proteins, called connexins, purified from fractions of enriched gap junctions from different tissues differ. The connexins are designated by their molecular mass. Another system of nomenclature divides gap junction proteins into two categories, alpha and beta, a |
https://en.wikipedia.org/wiki/C.%20M.%20Gupta | Chhitar Mal Gupta (born 1944) is an Indian molecular biologist and academic, known for researches on transbilayer phospholipid asymmetry in biological membranes., drug targeting in parasitic diseases and characterization of structure and function of Leishmania actin and actin binding proteins. He is former director of the Central Drug Research Institute, Lucknow and the Institute of Microbial Technology, Chandigarh. A Distinguished Biotechnology Fellow and Distinguished Biotechnology Research Professor of the Department of Biotechnology, Government of India, he is an elected fellow of The World Academy of Sciences, Indian Academy of Sciences, Indian National Science Academy, National Academy of Sciences, India and the National Academy of Medical Sciences. The Council of Scientific and Industrial Research, the apex agency of the Government of India for scientific research, awarded him the Shanti Swarup Bhatnagar Prize for Science and Technology, one of the highest Indian science awards, in 1985, for his contributions to biological sciences.
Education and research
Gupta graduated in medicinal chemistry from the Central Drug Research Institute, Lucknow, India with the degrees MSc and PhD. He served as the director of the Institute of Microbial Technology, Chandigarh for five years, and director of the Central Drug Research Institute (CDRI), Lucknow for over ten years.
After his superannuation, he continued to work at CDRI first as distinguished biotechnologist and then as d |
https://en.wikipedia.org/wiki/ORAI1 | Calcium release-activated calcium channel protein 1 is a calcium selective ion channel that in humans is encoded by the ORAI1 gene. Orai channels play an important role in the activation of T-lymphocytes. The loss of function mutation of Orai1 causes severe combined immunodeficiency (SCID) in humans The mammalian orai family has two additional homologs, Orai2 and Orai3. Orai proteins share no homology with any other ion channel family of any other known proteins. They have 4 transmembrane domains and form hexamers.
Structure and function
Orai channels are activated upon the depletion of internal calcium stores, which is called the "store-operated" or the "capacitative" mechanism. They are molecular constituents of the "calcium release activated calcium currents" (ICRAC). Upon activation of phospholipase C by various cell surface receptors, inositol trisphosphate is formed that releases calcium from the endoplasmic reticulum. The decreased calcium concentration in the endoplasmic reticulum is sensed by the STIM1 protein. STIM1 clusters upon the depletion of the calcium stores and forms "puncta", and relocates near the plasma membrane, where it activates Orai1 via protein-protein interaction.
In 2012, a 3.35-angstrom (Å) crystal structure of the Drosophila Orai channel, which shares 73% sequence identity with human Orai1 within its transmembrane region, was published. The structure, thought to show the closed state of the channel, revealed that a single channel is composed |
https://en.wikipedia.org/wiki/Axel%20Elveljung | Erik Axel Rickard Elveljung (born Erik Axel Rickard Johansson; 6 March 1989) is a Swedish footballer who plays as a striker for Rasbo IK. He has previously played for IF Brommapojkarna and Östers IF, as well as represented the Sweden U17 and U19 teams.
References
1989 births
Living people
Östers IF players
IF Brommapojkarna players
Swedish men's footballers
Men's association football forwards |
https://en.wikipedia.org/wiki/Nucleic%20acid%20analogue | Nucleic acid analogues are compounds which are analogous (structurally similar) to naturally occurring RNA and DNA, used in medicine and in molecular biology research.
Nucleic acids are chains of nucleotides, which are composed of three parts: a phosphate backbone, a pentose sugar, either ribose or deoxyribose, and one of four nucleobases.
An analogue may have any of these altered. Typically the analogue nucleobases confer, among other things, different base pairing and base stacking properties. Examples include universal bases, which can pair with all four canonical bases, and phosphate-sugar backbone analogues such as PNA, which affect the properties of the chain (PNA can even form a triple helix).
Nucleic acid analogues are also called Xeno Nucleic Acid and represent one of the main pillars of xenobiology, the design of new-to-nature forms of life based on alternative biochemistries.
Artificial nucleic acids include peptide nucleic acid (PNA), Morpholino and locked nucleic acid (LNA), as well as glycol nucleic acid (GNA), threose nucleic acid (TNA) and hexitol nucleic acids (HNA). Each of these is distinguished from naturally occurring DNA or RNA by changes to the backbone of the molecule.
In May 2014, researchers announced that they had successfully introduced two new artificial nucleotides into bacterial DNA, and by including individual artificial nucleotides in the culture media, were able to passage the bacteria 24 times; they did not create mRNA or proteins able to |
https://en.wikipedia.org/wiki/KiSS1-derived%20peptide%20receptor | The KiSS1-derived peptide receptor (also known as GPR54 or the Kisspeptin receptor) is a G protein-coupled receptor which binds the peptide hormone kisspeptin (metastin). Kisspeptin is encoded by the metastasis suppressor gene KISS1, which is expressed in a variety of endocrine and gonadal tissues. Activation of the kisspeptin receptor is linked to the phospholipase C and inositol trisphosphate second messenger cascades inside the cell.
Kisspeptins are neuropeptides synthesized in the hypothalamus and encoded by the KISS1 gene. The KISS1 gene encodes the G protein-coupled receptor 54 (known as KISS1R or GPR54) and plays a crucial role in regulating reproduction, pubertal maturation, and metabolic function. KISS1 neurons located in the arcuate nucleus (ARC) of the mediobasal hypothalamus (MBH) project to GnRH neurons in the median eminence, which expresses KISS1R, to stimulate LH secretions in a pulsatile manner from the anterior pituitary to initiate ovulation/ pubertal maturation. The KISS1 and KISS1R/GPR54 genes have been detected in the brain, pituitary, placenta, pancreas, liver, and small intestine.
Function
Kisspeptin is involved in the regulation of endocrine function and the onset of puberty, with activation of the kisspeptin receptor triggering release of gonadotropin-releasing hormone (GnRH), and release of kisspeptin itself being inhibited by oestradiol but enhanced by GnRH. Reductions in kisspeptin levels with age may conversely be one of the reasons behind age |
https://en.wikipedia.org/wiki/1%2C2-dihydrovomilenine%20reductase | In enzymology, a 1,2-dihydrovomilenine reductase () is an enzyme that catalyzes the chemical reaction
17-O-acetylnorajmaline + NADP 1,2-dihydrovomilenine + NADPH + H
Thus, the two substrates of this enzyme are 17-O-acetylnorajmaline and NADP, whereas its 3 products are 1,2-dihydrovomilenine, NADPH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 17-O-acetylnorajmaline:NADP+ oxidoreductase. This enzyme participates in indole and ipecac alkaloid biosynthesis.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/1%2C2-dihydroxy-6-methylcyclohexa-3%2C5-dienecarboxylate%20dehydrogenase | In enzymology, a 1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate dehydrogenase () is an enzyme that catalyzes the chemical reaction
1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate + NAD 3-methylcatechol + NADH + CO
Thus, the two substrates of this enzyme are 1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate and NAD, whereas its 3 products are 3-methylcatechol, NADH, and CO.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate:NAD+ oxidoreductase (decarboxylating). This enzyme participates in toluene and xylene degradation.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/12-oxophytodienoate%20reductase | 12-oxophytodienoate reductase (OPRs) is an enzyme of the family of Old Yellow Enzymes (OYE). OPRs are grouped into two groups: OPRI and OPRII – the second group is the focus of this article, as the function of the first group is unknown, but is the subject of current research. The OPR enzyme utilizes the cofactor flavin mononucleotide (FMN) and catalyzes the following reaction in the jasmonic acid synthesis pathway:
This reaction occurs in peroxisomes in plants. Several isozymes have been discovered, with varying substrate stereospecificity: three in Solanum lycopersicum, 13 in Oryza sativa, and five in Arabidopsis thaliana. The OPR3 isozyme is most extensively studied because it can reduce all 4 stereoisomers of the substrate, OPDA and because it has shown to be the most significant enzyme in the jasmonic acid synthesis pathway.
Structure
12-oxophytodienoate reductase structure resembles OYE enzymes and has been elucidated by x-ray crystal structures. The cDNA encodes 372 amino acids for this enzyme. It exhibits a barrel fold of eight parallel beta-strands surrounded by eight alpha-helices to create a barrel shape. Turns at the N-terminus loops of the beta-strands have been shown to contain three to four amino acid residues and the C-terminus loops range between three and 47 amino acid residues. The C-terminus loops largely make up the active site and the larger range of the amount of residues is due to the diversity in the different isozyme active sites.
OPR3, the most |
https://en.wikipedia.org/wiki/15%2C16-dihydrobiliverdin%3Aferredoxin%20oxidoreductase | 15,16-dihydrobiliverdin:ferredoxin oxidoreductase () is an enzyme that catalyzes the following chemical reaction
15,16-dihydrobiliverdin + oxidized ferredoxin biliverdin IXalpha + reduced ferredoxin
The two substrates of this enzyme are 15,16-dihydrobiliverdin and oxidized ferredoxin, whereas its two products are biliverdin IXalpha and reduced ferredoxin.
Classification
15,16-dihydrobiliverdin:ferredoxin oxidoreductase belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is 15,16-dihydrobiliverdin:ferredoxin oxidoreductase. This enzyme is also called PebA. This enzyme participates in porphyrin and chlorophyll metabolism.
References
EC 1.3.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/15-oxoprostaglandin%2013-oxidase | In enzymology, a 15-oxoprostaglandin 13-oxidase () is an enzyme that catalyzes the chemical reaction
(5Z)-(15S)-11alpha-hydroxy-9,15-dioxoprostanoate + NAD(P)+ (5Z)-(15S)-11alpha-hydroxy-9,15-dioxoprosta-13-enoate + NAD(P)H + H+
The 3 substrates of this enzyme are (5Z)-(15S)-11alpha-hydroxy-9,15-dioxoprostanoate, NAD+, and NADP+, whereas its 4 products are (5Z)-(15S)-11alpha-hydroxy-9,15-dioxoprosta-13-enoate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (5Z)-(15S)-11alpha-hydroxy-9,15-dioxoprostanoate:NAD(P)+ Delta13-oxidoreductase. Other names in common use include 15-oxo-Delta13-prostaglandin reductase, Delta13-15-ketoprostaglandin reductase, 15-ketoprostaglandin Delta13-reductase, prostaglandin Delta13-reductase, prostaglandin 13-reductase, and 15-ketoprostaglandin Delta13-reductase.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 1.3.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/1%2C6-dihydroxycyclohexa-2%2C4-diene-1-carboxylate%20dehydrogenase | In enzymology, a 1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase () is an enzyme that catalyzes the chemical reaction
(1R,6R)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD catechol + CO + NADH + H
Thus, the two substrates of this enzyme are (1R,6R)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate and NAD, whereas its 4 products are catechol, CO, NADH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (1R,6R)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate:NAD+ oxidoreductase (decarboxylating). Other names in common use include 3,5-cyclohexadiene-1,2-diol-1-carboxylate dehydrogenase, 3,5-cyclohexadiene-1,2-diol-1-carboxylic acid dehydrogenase, dihydrodihydroxybenzoate dehydrogenase, DHBDH, cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase, 2-hydro-1,2-dihydroxybenzoate dehydrogenase, cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate:NAD+, oxidoreductase, and dihydrodihydroxybenzoate dehydrogenase. This enzyme participates in benzoate degradation via hydroxylation and benzoate degradation via coa ligation.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2%2C3-dihydro-2%2C3-dihydroxybenzoate%20dehydrogenase | In enzymology, a 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase () is an enzyme that catalyzes the chemical reaction
2,3-dihydro-2,3-dihydroxybenzoate + NAD+ 2,3-dihydroxybenzoate + NADH + H+
Thus, the two substrates of this enzyme are 2,3-dihydro-2,3-dihydroxybenzoate and NAD+, whereas its 3 products are 2,3-dihydroxybenzoate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2,3-dihydro-2,3-dihydroxybenzoate:NAD+ oxidoreductase. This enzyme is also called 2,3-diDHB dehydrogenase. This enzyme participates in biosynthesis of siderophore group nonribosomal.
Structure
2,3-diDHB dehydrogenase is a tetramer protein with dimension 65x69x43 Å. It has a crystallographic 222 symmetry, which exhibited for other members of short-chain oxireductase (SCOR) family of enzymes. The length of each monomer is 248 residues and the weight of the protein is 24647 Da. Each monomer consists of 7 beta-pleated sheets and 6 alpha helices.
Although the structure of the binding protein is not clearly defined, it was proposed that the binding pocket is made out of Leu83, Met85, Arg138, Gly140, Met141, Ser176, Met181, Gln182 and Leu185. It was also speculated that Arg138 is a likely subunit that interacts with the carboxyl group of 2,3-diDHB. Since there was a strong indication of oxidation at C3 position, Ser176 and Gln182 interact with the C2-hyd |
https://en.wikipedia.org/wiki/2%2C3-dihydroxy-2%2C3-dihydro-p-cumate%20dehydrogenase | In enzymology, a 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase () is an enzyme that catalyzes the chemical reaction
cis-5,6-dihydroxy-4-isopropylcyclohexa-1,3-dienecarboxylate + NAD+ 2,3-dihydroxy-p-cumate + NADH + H+
Thus, the two substrates of this enzyme are cis-5,6-dihydroxy-4-isopropylcyclohexa-1,3-dienecarboxylate and NAD+, whereas its 3 products are 2,3-dihydroxy-p-cumate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-2,3-dihydroxy-2,3-dihydro-p-cumate:NAD+ oxidoreductase. This enzyme participates in biphenyl degradation.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2%2C4-dichlorobenzoyl-CoA%20reductase | In enzymology, a 2,4-dichlorobenzoyl-CoA reductase () is an enzyme that catalyzes the chemical reaction
4-chlorobenzoyl-CoA + NADP+ + HCl 2,4-dichlorobenzoyl-CoA + NADPH + H+
The 3 substrates of this enzyme are 4-chlorobenzoyl-CoA, NADP+, and HCl, whereas its 3 products are 2,4-dichlorobenzoyl-CoA, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4-chlorobenzoyl-CoA:NADP+ oxidoreductase (halogenating). This enzyme participates in 2,4-dichlorobenzoate degradation.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-alkenal%20reductase | In enzymology, a 2-alkenal reductase () is an enzyme that catalyzes the chemical reaction
n-alkanal + NAD(P)+ alk-2-enal + NAD(P)H + H+
The 3 substrates of this enzyme are n-alkanal, NAD+, and NADP+, whereas its 4 products are alk-2-enal, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is n-alkanal:NAD(P)+ 2-oxidoreductase. Other names in common use include NAD(P)H-dependent alkenal/one oxidoreductase, and NADPH:2-alkenal alpha,beta-hydrogenase.
Structural studies
As of late 2007, three structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 1.3.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/2-Coumarate%20reductase | In enzymology, a 2-coumarate reductase or melilotate dehydrogenase () is an enzyme that catalyzes the chemical reaction
3-(2-hydroxyphenyl)propanoate + NAD+ 2-coumarate + NADH + H+
Thus, the two substrates of this enzyme are 3-(2-hydroxyphenyl)propanoate and NAD+, whereas its 3 products are 2-coumarate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-(2-hydroxyphenyl)propanoate:NAD+ oxidoreductase. This enzyme participates in phenylalanine metabolism.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure
Hydroxycinnamic acids metabolism |
https://en.wikipedia.org/wiki/2-enoate%20reductase | In enzymology, a 2-enoate reductase () is an enzyme that catalyzes the chemical reaction
butanoate + NAD+ 2-butenoate + NADH + H+
Thus, the two substrates of this enzyme are butanoate and NAD+, whereas its 3 products are 2-butenoate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is butanoate:NAD+ Delta2-oxidoreductase. This enzyme is also called enoate reductase. This enzyme participates in phenylalanine metabolism. It has 4 cofactors: FAD, Iron, Sulfur, and Iron-sulfur.
References
EC 1.3.1
NADH-dependent enzymes
Flavoproteins
Iron enzymes
Sulfur enzymes
Iron-sulfur enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-furoyl-CoA%20dehydrogenase | In enzymology, a 2-furoyl-CoA dehydrogenase () is an enzyme that catalyzes the chemical reaction
2-furoyl-CoA + H2O + acceptor S-(5-hydroxy-2-furoyl)-CoA + reduced acceptor
The 3 substrates of this enzyme are 2-furoyl-CoA, H2O, and acceptor, whereas its two products are S-(5-hydroxy-2-furoyl)-CoA and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is 2-furoyl-CoA:acceptor 5-oxidoreductase (hydroxylating). Other names in common use include furoyl-CoA hydroxylase, 2-furoyl coenzyme A hydroxylase, 2-furoyl coenzyme A dehydrogenase, and 2-furoyl-CoA:(acceptor) 5-oxidoreductase (hydroxylating). It employs one cofactor, copper.
References
EC 1.3.99
Copper enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-hexadecenal%20reductase | In enzymology, a 2-hexadecenal reductase () is an enzyme that catalyzes the chemical reaction
hexadecanal + NADP+ 2-trans-hexadecenal + NADPH + H+
Thus, the two substrates of this enzyme are hexadecanal and NADP+, whereas its 3 products are 2-trans-hexadecenal, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is hexadecanal:NADP+ Delta2-oxidoreductase. Other names in common use include 2-alkenal reductase, and hexadecanal: NADP+ oxidoreductase.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-hydroxy-6-oxo-6-phenylhexa-2%2C4-dienoate%20reductase | In enzymology, a 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate reductase () is an enzyme that catalyzes the chemical reaction
2,6-dioxo-6-phenylhexanoate + NADP+ 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + NADPH + H+
Thus, the two substrates of this enzyme are 2,6-dioxo-6-phenylhexanoate and NADP+, whereas its 3 products are 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2,6-dioxo-6-phenylhexanoate:NADP+ Delta2-oxidoreductase. Other names in common use include 2-hydroxy-6-oxo-phenylhexa-2,4-dienoate (reduced nicotinamide, and adenine dinucleotide phosphate) reductase.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2%27-hydroxydaidzein%20reductase | In enzymology, a 2'-hydroxydaidzein reductase () is an enzyme that catalyzes the chemical reaction
2'-hydroxy-2,3-dihydrodaidzein + NADP+ 2'-hydroxydaidzein + NADPH + H+
Thus, the two substrates of this enzyme are 2'-hydroxy-2,3-dihydrodaidzein and NADP+, whereas its 3 products are 2'-hydroxydaidzein, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2'-hydroxy-2,3-dihydrodaidzein:NADP+ 2'-oxidoreductase. Other names in common use include NADPH:2'-hydroxydaidzein oxidoreductase, HDR, and 2'-hydroxydihydrodaidzein:NADP+ 2'-oxidoreductase. This enzyme participates in isoflavonoid biosynthesis.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure
Isoflavonoids metabolism |
https://en.wikipedia.org/wiki/2%27-Hydroxyisoflavone%20reductase | In enzymology, a 2'-hydroxyisoflavone reductase () is an enzyme that catalyzes the chemical reaction
vestitone + NADP+ 2'-hydroxyformononetin + NADPH + H+
Thus, the two substrates of this enzyme are vestitone and NADP+, whereas its 3 products are 2'-hydroxyformononetin, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is vestitone:NADP+ oxidoreductase. Other names in common use include NADPH:2'-hydroxyisoflavone oxidoreductase, isoflavone reductase, and 2',7-dihydroxy-4',5'-methylenedioxyisoflavone reductase.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-methylacyl-CoA%20dehydrogenase | In enzymology, a 2-methylacyl-CoA dehydrogenase () is an enzyme that catalyzes the chemical reaction
2-methylbutanoyl-CoA + acceptor 2-methylbut-2-enoyl-CoA + reduced acceptor
Thus, the two substrates of this enzyme are 2-methylbutanoyl-CoA and acceptor, whereas its two products are 2-methylbut-2-enoyl-CoA and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is 2-methylbutanoyl-CoA:acceptor oxidoreductase. Other names in common use include branched-chain acyl-CoA dehydrogenase, 2-methyl branched chain acyl-CoA dehydrogenase, and 2-methylbutanoyl-CoA:(acceptor) oxidoreductase. This enzyme participates in valine, leucine and isoleucine degradation.
References
EC 1.3.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-methyl-branched-chain-enoyl-CoA%20reductase | In enzymology, a 2-methyl-branched-chain-enoyl-CoA reductase () is an enzyme that catalyzes the chemical reaction
2-methylbutanoyl-CoA + electron transfer flavoprotein 2-methylcrotonoyl-CoA + reduced electron transfer flavoprotein + H+
Thus, the two substrates of this enzyme are 2-methylbutanoyl-CoA and an electron transfer flavoprotein, whereas its 3 products are 2-methylcrotonoyl-CoA, reduced electron transfer flavoprotein, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donors with flavin as acceptor. The systematic name of this enzyme class is 2-methyl-branched-chain-acyl-CoA:electron-transfer flavoprotein 2-oxidoreductase . This enzyme participates in the degradation of isoleucine. It employs one cofactor, FAD.
References
EC 1.3.8
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-methyleneoxindole%20reductase | In enzymology, a 3-methyleneoxindole reductase () is an enzyme that catalyzes the chemical reaction
3-methyl-1,3-dihydroindol-2-one + NADP+ 3-methylene-1,3-dihydro-2H-indol-2-one + NADPH + H+
Thus, the two substrates of this enzyme are 3-methyl-1,3-dihydroindol-2-one and NADP+, whereas its three products are 3-methylene-1,3-dihydro-2H-indol-2-one, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-methyl-1,3-dihydroindol-2-one:NADP+ oxidoreductase. This enzyme is also termed 3-methyloxindole:NADP+ oxidoreductase.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tumor%20necrosis%20factor%20receptor%201 | Tumor necrosis factor receptor 1 (TNFR1), also known as tumor necrosis factor receptor superfamily member 1A (TNFRSF1A) and CD120a, is a ubiquitous membrane receptor that binds tumor necrosis factor-alpha (TNFα).
Function
The protein encoded by this gene is a member of the tumor necrosis factor receptor superfamily, which also contains TNFRSF1B. This protein is one of the major receptors for the tumor necrosis factor-alpha. This receptor can activate the transcription factor NF-κB, mediate apoptosis, and function as a regulator of inflammation. Antiapoptotic protein BCL2-associated athanogene 4 (BAG4/SODD) and adaptor proteins TRADD and TRAF2 have been shown to interact with this receptor, and thus play regulatory roles in the signal transduction mediated by the receptor.
Clinical significance
Germline mutations of the extracellular domains of this receptor were found to be associated with the human genetic disorder called tumor necrosis factor associated periodic syndrome (TRAPS) or periodic fever syndrome. Impaired receptor clearance is thought to be a mechanism of the disease.
Mutations in the TNFRSF1A gene are associated with elevated risk of multiple sclerosis.
Serum levels of TNFRSF1A are elevated in schizophrenia and bipolar disorder, and high levels are associated with more severe psychotic symptoms.
High serum levels are also associated with cognitive impairment and dementia.
Interactions
TNFRSF1A has been shown to interact with:
BAG4,
CASP10,
FADD, |
https://en.wikipedia.org/wiki/3-oxo-5beta-steroid%204-dehydrogenase | In enzymology, a 3-oxo-5beta-steroid 4-dehydrogenase () is an enzyme that catalyzes the chemical reaction
a 3-oxo-5beta-steroid + acceptor a 3-oxo-Delta4-steroid + reduced acceptor
Thus, the two substrates of this enzyme are 3-oxo-5beta-steroid and acceptor, whereas its two products are 3-oxo-Delta4-steroid and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, to be specific, those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is 3-oxo-5beta-steroid:acceptor Delta4-oxidoreductase. This enzyme is also called 3-oxo-5beta-steroid:(acceptor) Delta4-oxidoreductase. This enzyme participates in 3 metabolic pathways: bile acid biosynthesis, c21-steroid hormone metabolism, and androgen and estrogen metabolism.
References
EC 1.3.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-oxosteroid%201-dehydrogenase | In enzymology, a 3-oxosteroid 1-dehydrogenase () is an enzyme that catalyzes the chemical reaction
a 3-oxosteroid + acceptor a 3-oxo-Delta1-steroid + reduced acceptor
Thus, the two substrates of this enzyme are 3-oxosteroid and acceptor, whereas its two products are 3-oxo-Delta1-steroid and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is 3-oxosteroid:acceptor Delta1-oxidoreductase. Other names in common use include 3-oxosteroid Delta1-dehydrogenase, Delta1-dehydrogenase, 3-ketosteroid-1-en-dehydrogenase, 3-ketosteroid-Delta1-dehydrogenase, 1-ene-dehydrogenase, 3-oxosteroid:(2,6-dichlorphenolindophenol) Delta1-oxidoreductase, 4-en-3-oxosteroid:(acceptor)-1-en-oxido-reductase, Delta1-steroid reductase, and 3-oxosteroid:(acceptor) Delta1-oxidoreductase.
References
EC 1.3.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%283S%2C4R%29-3%2C4-dihydroxycyclohexa-1%2C5-diene-1%2C4-dicarboxylate%20dehydrogenase | In enzymology, a (3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate dehydrogenase () is an enzyme that catalyzes the chemical reaction
(3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate + NAD 3,4-dihydroxybenzoate + CO + NADH
Thus, the two substrates of this enzyme are (3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate and NAD, whereas its 3 products are 3,4-dihydroxybenzoate, CO, and NADH.
This enzyme is a part of the terephthalate degradation pathway in bacteria.
Family
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate:NAD+ oxidoreductase. Another name in common use is (1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate dehydrogenase. This enzyme employs one cofactor, iron.
References
EC 1.3.1
NADH-dependent enzymes
Iron enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/4-hydroxybenzoyl-CoA%20reductase | In enzymology, a 4-hydroxybenzoyl-CoA reductase () is an enzyme found in some bacteria and archaea that catalyzes the chemical reaction
benzoyl-CoA + acceptor + H2O 4-hydroxybenzoyl-CoA + reduced acceptor
The 3 substrates of this enzyme are benzoyl-CoA, acceptor, and H2O, whereas its two products are 4-hydroxybenzoyl-CoA and reduced acceptor.
This enzyme participates in benzoate degradation via coa ligation.
Nomenclature
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is benzoyl-CoA:acceptor oxidoreductase. Other names in common use include:
4-hydroxybenzoyl-CoA reductase (dehydroxylating), and
4-hydroxybenzoyl-CoA:(acceptor) oxidoreductase.
References
Further reading
EC 1.3.7
Enzymes of known structure |
https://en.wikipedia.org/wiki/5%2C6-dihydroxy-3-methyl-2-oxo-1%2C2%2C5%2C6-tetrahydroquinoline%20dehydrogenase | In enzymology, a 5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline dehydrogenase () is an enzyme that catalyzes the chemical reaction
5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline + NAD+ 5,6-dihydroxy-3-methyl-2-oxo-1,2-dihydroquinoline + NADH + H+
Thus, the two substrates of this enzyme are 5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline and NAD+, whereas its 3 products are 5,6-dihydroxy-3-methyl-2-oxo-1,2-dihydroquinoline, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline:NAD+ oxidoreductase.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/6-hydroxynicotinate%20reductase | In enzymology, a 6-hydroxynicotinate reductase () is an enzyme that catalyzes the chemical reaction
6-oxo-1,4,5,6-tetrahydronicotinate + oxidized ferredoxin 6-hydroxynicotinate + reduced ferredoxin
Thus, the two substrates of this enzyme are 6-oxo-1,4,5,6-tetrahydronicotinate and oxidized ferredoxin, whereas its two products are 6-hydroxynicotinate and reduced ferredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is 6-oxo-1,4,5,6-tetrahydronicotinate:ferredoxin oxidoreductase. Other names in common use include 6-oxotetrahydronicotinate dehydrogenase, 6-hydroxynicotinic reductase, HNA reductase, and 1,4,5,6-tetrahydro-6-oxonicotinate:ferredoxin oxidoreductase.
References
EC 1.3.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acyl-CoA%20dehydrogenase%20%28NADP%2B%29 | In enzymology, an acyl-CoA dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
acyl-CoA + NADP+ 2,3-dehydroacyl-CoA + NADPH + H+
Thus, the two substrates of this enzyme are acyl-CoA and NADP+, whereas its 3 products are 2,3-dehydroacyl-CoA, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is acyl-CoA:NADP+ 2-oxidoreductase. Other names in common use include 2-enoyl-CoA reductase, dehydrogenase, acyl coenzyme A (nicotinamide adenine dinucleotide, phosphate), enoyl coenzyme A reductase, crotonyl coenzyme A reductase, crotonyl-CoA reductase, and acyl-CoA dehydrogenase (NADP+).
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Acyl-CoA%20oxidase | In enzymology, an acyl-CoA oxidase () is an enzyme that catalyzes the chemical reaction
acyl-CoA + O2 trans-2,3-dehydroacyl-CoA + H2O2
Thus, the two substrates of this enzyme are acyl-CoA and O2, whereas its two products are trans-2,3-dehydroacyl-CoA and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is acyl-CoA:oxygen 2-oxidoreductase. Other names in common use include fatty acyl-CoA oxidase, acyl coenzyme A oxidase, and fatty acyl-coenzyme A oxidase. This enzyme participates in 3 metabolic pathways: fatty acid metabolism, polyunsaturated fatty acid biosynthesis, and ppar signaling pathway. It employs one cofactor, FAD.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
See also
ACOX1
ACOX3
References
EC 1.3.3
Flavoproteins
Enzymes of known structure |
https://en.wikipedia.org/wiki/All-trans-retinol%2013%2C14-reductase | In enzymology, an all-trans-retinol 13,14-reductase () is an enzyme, encoded by the RETSAT gene, that catalyzes the chemical reaction
all-trans-13,14-dihydroretinol + acceptor all-trans-retinol + reduced acceptor
Thus, the two substrates of this enzyme are all-trans-13,14-dihydroretinol and acceptor, whereas its two products are all-trans-retinol and reduced acceptor. Under physiological conditions the reaction proceeds in the opposite direction catalyzing the saturation of the 13-14 double bond of all-trans-retinol.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is all-trans-13,14-dihydroretinol:acceptor 13,14-oxidoreductase. Other names in common use include retinol saturase, RetSat, (13,14)-all-trans-retinol saturase, and all-trans-retinol:all-trans-13,14-dihydroretinol saturase.
The gene has also been called PPAR-alpha-regulated and starvation-induced gene protein.
References
Further reading
EC 1.3.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Alpha-santonin%201%2C2-reductase | In enzymology, an alpha-santonin 1,2-reductase () is an enzyme that catalyzes the chemical reaction
1,2-dihydrosantonin + NAD(P)+ alpha-santonin + NAD(P)H + H+
The 3 substrates of this enzyme are 1,2-dihydrosantonin, NAD+, and NADP+, whereas its 4 products are alpha-santonin, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 1,2-dihydrosantonin:NAD(P)+ 1,2-oxidoreductase.
References
EC 1.3.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Anthocyanidin%20reductase | In enzymology, an anthocyanidin reductase () is an enzyme that catalyzes the chemical reaction
a flavan-3-ol + 2 NAD(P)+ an anthocyanidin + 2 NAD(P)H + H+
The 3 substrates of this enzyme are flavan-3-ol, NAD+, and NADP+, whereas its 4 products are anthocyanidin, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is flavan-3-ol:NAD(P)+ oxidoreductase. Other names in common use include AtANR, and MtANR. This enzyme participates in flavonoid biosynthesis.
References
EC 1.3.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure
Flavanols metabolism
Anthocyanins metabolism |
https://en.wikipedia.org/wiki/Arogenate%20dehydrogenase | In enzymology, an arogenate dehydrogenase () is an enzyme that catalyzes the chemical reaction
L-arogenate + NAD+ L-tyrosine + NADH + CO2
Thus, the two substrates of this enzyme are L-arogenate and NAD+, whereas its 3 products are L-tyrosine, NADH, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-arogenate:NAD+ oxidoreductase (decarboxylating). Other names in common use include arogenic dehydrogenase (ambiguous), cyclohexadienyl dehydrogenase, pretyrosine dehydrogenase (ambiguous), and L-arogenate:NAD+ oxidoreductase. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and novobiocin biosynthesis.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Arogenate%20dehydrogenase%20%28NAD%28P%29%2B%29 | In enzymology, an arogenate dehydrogenase [NAD(P)+] () is an enzyme that catalyzes the chemical reaction
L-arogenate + NAD(P)+ L-tyrosine + NAD(P)H + CO2
The 3 substrates of this enzyme are L-arogenate, NAD+, and NADP+, whereas its 4 products are L-tyrosine, NADH, NADPH, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-arogenate:NAD(P)+ oxidoreductase (decarboxylating). Other names in common use include arogenic dehydrogenase (ambiguous), cyclohexadienyl dehydrogenase, and pretyrosine dehydrogenase (ambiguous).
References
EC 1.3.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Arogenate%20dehydrogenase%20%28NADP%2B%29 | In enzymology, an arogenate dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
L-arogenate + NADP+ L-tyrosine + NADPH + CO2
Thus, the two substrates of this enzyme are L-arogenate and NADP+, whereas its 3 products are L-tyrosine, NADPH, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-arogenate:NADP+ oxidoreductase (decarboxylating). Other names in common use include arogenic dehydrogenase (ambiguous), pretyrosine dehydrogenase (ambiguous), TyrAAT1, TyrAAT2, and TyrAa.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Benzoyl-CoA%20reductase | In enzymology, a benzoyl-CoA reductase () is an enzyme that catalyzes the chemical reaction
benzoyl-CoA + reduced acceptor + 2 ATP + 2 H2O cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + 2 ADP + 2 phosphate
The 4 substrates of this enzyme are benzoyl-CoA, reduced acceptor, ATP, and H2O, whereas its 4 products are cyclohexa-1,5-diene-1-carbonyl-CoA, acceptor, ADP, and phosphate.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is cyclohexa-1,5-diene-1-carbonyl-CoA:acceptor oxidoreductase (aromatizing, ATP-forming). This enzyme is also called benzoyl-CoA reductase (dearomatizing). This enzyme participates in benzoate degradation via CoA ligation. It has two cofactors: manganese, and magnesium.
References
EC 1.3.7
Manganese enzymes
Magnesium enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Beta-nitroacrylate%20reductase | In enzymology, a beta-nitroacrylate reductase () is an enzyme that catalyzes the chemical reaction
3-nitropropanoate + NADP+ 3-nitroacrylate + NADPH + H+
Thus, the two substrates of this enzyme are 3-nitropropanoate and NADP+, whereas its 3 products are 3-nitroacrylate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-nitropropanoate:NADP+ oxidoreductase.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Bilirubin%20oxidase | In enzymology, a bilirubin oxidase, BOD or BOx, () is an enzyme encoded by a gene in various organisms that catalyzes the chemical reaction
2 bilirubin + O2 2 biliverdin + 2 H2O
This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is bilirubin:oxygen oxidoreductase. This enzyme is also called bilirubin oxidase M-1. This enzyme participates in porphyrin and chlorophyll metabolism. It is widely studied as a catalyst for oxygen reduction.
Two structures of bilirubin oxidase from the ascomycete Myrothecium verrucaria have been deposited in the Protein Data Bank (accession codes and ).
The active site consists of four copper centers, reminiscent of laccase. These centers are classified as type I (cys, met, his, his), type II (3his), and two type III (2his).
Further reading
References
EC 1.3.3
Copper enzymes |
https://en.wikipedia.org/wiki/Biochanin-A%20reductase | In enzymology, a biochanin-A reductase () is an enzyme that catalyzes the chemical reaction
dihydrobiochanin A + NADP+ biochanin A + NADPH + H+
Thus, the two substrates of this enzyme are dihydrobiochanin A and NADP+, whereas its 3 products are biochanin A, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is dihydrobiochanin-A:NADP+ Delta2-oxidoreductase. This enzyme participates in isoflavonoid biosynthesis.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure
Isoflavonoids metabolism |
https://en.wikipedia.org/wiki/Cholestenone%205alpha-reductase | In enzymology, a cholestenone 5alpha-reductase () is an enzyme that catalyzes the chemical reaction
5alpha-cholestan-3-one + NADP+ cholest-4-en-3-one + NADPH + H+
Thus, the two substrates of this enzyme are 5alpha-cholestan-3-one and NADP+, whereas its 3 products are cholest-4-en-3-one, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-oxo-5alpha-steroid:NADP+ Delta4-oxidoreductase. Other names in common use include testosterone Delta4-5alpha-reductase, steroid 5alpha-reductase, 3-oxosteroid Delta4-dehydrogenase, 5alpha-reductase, steroid 5alpha-hydrogenase, 3-oxosteroid 5alpha-reductase, testosterone Delta4-hydrogenase, 4-ene-3-oxosteroid 5alpha-reductase, reduced nicotinamide adenine dinucleotide, phosphate:Delta4-3-ketosteroid 5alpha-oxidoreductase, 4-ene-5alpha-reductase, Delta4-3-ketosteroid 5alpha-oxidoreductase, cholest-4-en-3-one 5alpha-reductase, and testosterone 5alpha-reductase.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cis-1%2C2-dihydro-1%2C2-dihydroxynaphthalene%20dehydrogenase | In enzymology, a cis-1,2-dihydro-1,2-dihydroxynaphthalene dehydrogenase () is an enzyme that catalyzes the chemical reaction
cis-1,2-dihydronaphthalene-1,2-diol + NAD+ naphthalene-1,2-diol + NADH + H+
Thus, the two substrates of this enzyme are cis-1,2-dihydronaphthalene-1,2-diol and NAD+, whereas its 3 products are naphthalene-1,2-diol, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-1,2-dihydronaphthalene-1,2-diol:NAD+ 1,2-oxidoreductase. Other names in common use include (+)-cis-naphthalene dihydrodiol dehydrogenase, naphthalene dihydrodiol dehydrogenase, and cis-dihydrodiol naphthalene dehydrogenase. This enzyme participates in 1- and 2-methylnaphthalene degradation and naphthalene and anthracene degradation.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cis-1%2C2-dihydrobenzene-1%2C2-diol%20dehydrogenase | In enzymology, a cis-1,2-dihydrobenzene-1,2-diol dehydrogenase () is an enzyme that catalyzes the chemical reaction
cis-1,2-dihydrobenzene-1,2-diol + NAD+ catechol + NADH + H+
Thus, the two substrates of this enzyme are cis-1,2-dihydrobenzene-1,2-diol and NAD+, whereas its 3 products are catechol, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-1,2-dihydrobenzene-1,2-diol:NAD+ oxidoreductase. Other names in common use include cis-benzene glycol dehydrogenase, cis-1,2-dihydrocyclohexa-3,5-diene (nicotinamide adenine, and dinucleotide) oxidoreductase. This enzyme participates in 4 metabolic pathways: gamma-hexachlorocyclohexane degradation, toluene and xylene degradation, naphthalene and anthracene degradation, and styrene degradation.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cis-1%2C2-dihydroxy-4-methylcyclohexa-3%2C5-diene-1-carboxylate%20dehydrogenase | In enzymology, a cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate dehydrogenase () is an enzyme that catalyzes the chemical reaction
cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate + NAD(P)+ 4-methylcatechol + NAD(P)H + CO2
The 3 substrates of this enzyme are cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate, NAD+, and NADP+, whereas its 4 products are 4-methylcatechol, NADH, NADPH, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate:NAD(P)+ oxidoreductase (decarboxylating). This enzyme participates in toluene and xylene degradation.
References
EC 1.3.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cis-2%2C3-dihydrobiphenyl-2%2C3-diol%20dehydrogenase | In enzymology, a cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase () is an enzyme that catalyzes the chemical reaction
cis-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+ biphenyl-2,3-diol + NADH + H+
Thus, the two substrates of this enzyme are cis-3-phenylcyclohexa-3,5-diene-1,2-diol and NAD+, whereas its 3 products are biphenyl-2,3-diol, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-3-phenylcyclohexa-3,5-diene-1,2-diol:NAD+ oxidoreductase. This enzyme is also called 2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase. This enzyme participates in biphenyl degradation.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cis-2-enoyl-CoA%20reductase%20%28NADPH%29 | In enzymology, a cis-2-enoyl-CoA reductase (NADPH) () is an enzyme that catalyzes the chemical reaction
acyl-CoA + NADP+ cis-2,3-dehydroacyl-CoA + NADPH + H+
Thus, the two substrates of this enzyme are acyl-CoA and NADP+, whereas its 3 products are cis-2,3-dehydroacyl-CoA, NADPH, and H+.
Nomenclature
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is acyl-CoA:NADP+ cis-2-oxidoreductase. Other names in common use include NADPH-dependent cis-enoyl-CoA reductase, reductase, cis-2-enoyl coenzyme A, cis-2-enoyl-coenzyme A reductase, and cis-2-enoyl-CoA reductase (NADPH).
References
Further reading
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cis-3%2C4-dihydrophenanthrene-3%2C4-diol%20dehydrogenase | In enzymology, a cis-3,4-dihydrophenanthrene-3,4-diol dehydrogenase () is an enzyme that catalyzes the chemical reaction
(+)-cis-3,4-dihydrophenanthrene-3,4-diol + NAD+ phenanthrene-3,4-diol + NADH + H+
Thus, the two substrates of this enzyme are (+)-cis-3,4-dihydrophenanthrene-3,4-diol and NAD+, whereas its 3 products are phenanthrene-3,4-diol, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (+)-cis-3,4-dihydrophenanthrene-3,4-diol:NAD+ 3,4-oxidoreductase. This enzyme participates in naphthalene and anthracene degradation.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cis-dihydroethylcatechol%20dehydrogenase | In enzymology, a cis-dihydroethylcatechol dehydrogenase () is an enzyme that catalyzes the chemical reaction
cis-1,2-dihydro-3-ethylcatechol + NAD+ 3-ethylcatechol + NADH + H+
Thus, the two substrates of this enzyme are cis-1,2-dihydro-3-ethylcatechol and NAD+, whereas its 3 products are 3-ethylcatechol, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-1,2-dihydro-3-ethylcatechol:NAD+ oxidoreductase. This enzyme participates in ethylbenzene degradation.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Coproporphyrinogen%20dehydrogenase | In enzymology, a coproporphyrinogen dehydrogenase () is an enzyme that catalyzes the chemical reaction
coproporphyrinogen III + 2 S-adenosyl-L-methionine protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
Thus, the two substrates of this enzyme are coproporphyrinogen III and S-adenosyl-L-methionine, whereas its 4 products are protoporphyrinogen IX, CO2, L-methionine, and 5'-deoxyadenosine.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is coproporphyrinogen-III:S-adenosyl-L-methionine oxidoreductase (decarboxylating). Other names in common use include oxygen-independent coproporphyrinogen-III oxidase, HemF, HemN, radical SAM enzyme, and coproporphyrinogen III oxidase. This enzyme participates in porphyrin and chlorophyll metabolism. HemN is the Oxygen-independent oxidase produced in E. coli. HemF is the oxygen-dependent oxidase within E. coli. Importantly, only HemN utilizes S-adenosyl Methionine (SAM). Human variants of Coproporphyrinogen oxidase are cofactor-independent.
References
EC 1.3.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cortisone%20alpha-reductase | In enzymology, a cortisone alpha-reductase () is an enzyme that catalyzes the chemical reaction
4,5alpha-dihydrocortisone + NADP+ cortisone + NADPH + H+
Thus, the two substrates of this enzyme are 4,5alpha-dihydrocortisone and NADP+, whereas its 3 products are cortisone, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4,5alpha-dihydrocortisone:NADP+ Delta4-oxidoreductase. Other names in common use include cortisone Delta4-5alpha-reductase, microsomal steroid reductase (5alpha), Delta4-3-ketosteroid reductase (5alpha), Delta4-3-oxosteroid-5alpha-reductase, NADPH:Delta4-3-oxosteroid-5alpha-oxidoreductase, and Delta4-5alpha-reductase.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cucurbitacin%20Delta23-reductase | In enzymology, a cucurbitacin Delta23-reductase () is an enzyme that catalyzes the chemical reaction
23,24-dihydrocucurbitacin + NAD(P)+ cucurbitacin + NAD(P)H + H+
The 3 substrates of this enzyme are 23,24-dihydrocucurbitacin, NAD+, and NADP+, whereas its 4 products are cucurbitacin, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 23,24-dihydrocucurbitacin:NAD(P)+ Delta23-oxidoreductase. This enzyme is also called NAD(P)H: cucurbitacin B Delta23-oxidoreductase. It employs one cofactor, manganese.
References
EC 1.3.1
NADPH-dependent enzymes
NADH-dependent enzymes
Manganese enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cyclohexanone%20dehydrogenase | In enzymology, a cyclohexanone dehydrogenase () is an enzyme that catalyzes a chemical reaction
cyclohexanone + acceptor cyclohex-2-enone + reduced acceptor
Thus, the two substrates of this enzyme are cyclohexanone and acceptor, whereas its two products are cyclohex-2-enone and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is cyclohexanone:acceptor 2-oxidoreductase. This enzyme is also called cyclohexanone:(acceptor) 2-oxidoreductase.
References
EC 1.3.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Delta14-sterol%20reductase | In enzymology, a Delta14-sterol reductase () is an enzyme that catalyzes the chemical reaction
4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP+ 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + NADPH + H+
Thus, the two substrates of this enzyme are 4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol and NADP+, whereas its 3 products are 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol:NADP+ Delta14-oxidoreductase. This enzyme participates in biosynthesis of steroids.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Delta24%28241%29-sterol%20reductase | In enzymology, a Delta24(241)-sterol reductase () is an enzyme that catalyzes the chemical reaction
ergosterol + NADP+ ergosta-5,7,22,24(241)-tetraen-3beta-ol + NADPH + H+
Thus, the two substrates of this enzyme are ergosterol and NADP+, whereas its 3 products are ergosta-5,7,22,24(241)-tetraen-3beta-ol, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is ergosterol:NADP+ Delta24(241)-oxidoreductase. Other names in common use include sterol Delta24(28)-methylene reductase, and sterol Delta24(28)-reductase. This enzyme participates in biosynthesis of steroids.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Delta24-sterol%20reductase | In enzymology, a Delta24-sterol reductase () is an enzyme that catalyzes the chemical reaction
5alpha-cholest-7-en-3beta-ol + NADP+ 5alpha-cholesta-7,24-dien-3beta-ol + NADPH + H+
Thus, the two substrates of this enzyme are 5alpha-cholest-7-en-3beta-ol and NADP+, whereas its 3 products are 5alpha-cholesta-7,24-dien-3beta-ol, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is sterol:NADP+ Delta24-oxidoreductase. This enzyme is also called lanosterol Delta24-reductase. This enzyme participates in biosynthesis of steroids.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dibenzothiophene%20dihydrodiol%20dehydrogenase | In enzymology, a dibenzothiophene dihydrodiol dehydrogenase () is an enzyme that catalyzes the chemical reaction
cis-1,2-dihydroxy-1,2-dihydrodibenzothiophene + NAD+ 1,2-dihydroxydibenzothiophene + NADH + H+
Thus, the two substrates of this enzyme are cis-1,2-dihydroxy-1,2-dihydrodibenzothiophene and NAD+, whereas its 3 products are 1,2-dihydroxydibenzothiophene, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-1,2-dihydroxy-1,2-dihydrodibenzothiophene:NAD+ oxidoreductase.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dihydropyrimidine%20dehydrogenase%20%28NADP%2B%29 | In enzymology, a dihydropyrimidine dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
5,6-dihydrouracil + NADP+ uracil + NADPH + H+
Thus, the two substrates of this enzyme are 5,6-dihydrouracil and NADP+, whereas its 3 products are uracil, NADPH, and H+.
In humans the enzyme is encoded by the DPYD gene. It is the initial and rate-limiting step in pyrimidine catabolism. It catalyzes the reduction of uracil and thymine. It is also involved in the degradation of the chemotherapeutic drugs 5-fluorouracil and tegafur. It also participates in beta-alanine metabolism and pantothenate and coa biosynthesis.
Terminology
The systematic name of this enzyme class is 5,6-dihydrouracil:NADP+ 5-oxidoreductase. Other names in common use include:
dihydrothymine dehydrogenase
dihydrouracil dehydrogenase (NADP+)
4,5-dihydrothymine: oxidoreductase
DPD
DHPDH
dehydrogenase, dihydrouracil (nicotinamide adenine dinucleotide, phosphate)
DHU dehydrogenase
hydropyrimidine dehydrogenase
dihydropyrimidine dehydrogenase (NADP+)
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
Function
The protein is a pyrimidine catabolic enzyme and the initial and rate-limiting factor in the pathway of uracil and thymidine catabolism. Genetic deficiency of this enzyme results in an error in pyrimidine metabolism associated with thymine-uraciluria and an increased risk of toxicity in cancer patients receivin |
https://en.wikipedia.org/wiki/Dihydrouracil%20dehydrogenase%20%28NAD%2B%29 | In enzymology, a dihydrouracil dehydrogenase (NAD+) () is an enzyme that catalyzes the chemical reaction
5,6-dihydrouracil + NAD+ uracil + NADH + H+
Thus, the two substrates of this enzyme are 5,6-dihydrouracil and NAD+, whereas its 3 products are uracil, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 5,6-dihydrouracil:NAD+ oxidoreductase. Other names in common use include dehydrogenase, dihydrouracil, dihydropyrimidine dehydrogenase, dihydrothymine dehydrogenase, pyrimidine reductase, thymine reductase, uracil reductase, and dihydrouracil dehydrogenase (NAD+). This enzyme participates in 3 metabolic pathways: pyrimidine metabolism, beta-alanine metabolism, and pantothenate and coa biosynthesis.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dihydrouracil%20oxidase | In enzymology, a dihydrouracil oxidase () is an enzyme that catalyzes the chemical reaction
5,6-dihydrouracil + O2 uracil + H2O2
Thus, the two substrates of this enzyme are 5,6-dihydrouracil and O2, whereas its two products are uracil and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is 5,6-dihydrouracil:oxygen oxidoreductase. It employs one cofactor, FMN.
References
EC 1.3.3
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Divinyl%20chlorophyllide%20a%208-vinyl-reductase | In enzymology, divinyl chlorophyllide a 8-vinyl-reductase () is an enzyme that catalyzes the chemical reaction
3,8-divinylprotochlorophyllide + NADPH + H+ protochlorophyllide + NADP+
The three substrates of this enzyme are 3,8-divinylprotochlorophyllide, NADPH, and H+; its two products are protochlorophyllide and NADP+. This enzyme can also convert alternative substrates, for example 3,8-divinyl chlorophyllide a and in all cases reduces a single specific vinyl group to an ethyl group.
This enzyme belongs to the family of oxidoreductases. The systematic name of this enzyme class is chlorophyllide-a :NADP+ oxidoreductase. Other names in common use include 3,8-divinyl protochlorophyllide a 8-vinyl-reductase, [4-vinyl]chlorophyllide a reductase, and 4VCR. This enzyme is part of the biosynthetic pathway to chlorophylls.
See also
Biosynthesis of chlorophylls
References
</ref>
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Enoyl-%28acyl-carrier-protein%29%20reductase%20%28NADPH%2C%20A-specific%29 | In enzymology, an enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) () is an enzyme that catalyzes the chemical reaction
acyl-[acyl-carrier-protein] + NADP+ trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADPH + H+
Thus, the two substrates of this enzyme are [[acyl-[acyl-carrier-protein]]] and NADP+, whereas its 3 products are [[trans-2,3-dehydroacyl-[acyl-carrier-protein]]], NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, to be specific, those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is acyl-[acyl-carrier-protein]:NADP+ oxidoreductase (A-specific). Other names in common use include acyl-ACP dehydrogenase, enoyl-[acyl carrier protein] (reduced nicotinamide adenine, dinucleotide phosphate) reductase, NADPH 2-enoyl Co A reductase, enoyl-ACp reductase, and enoyl-[acyl-carrier-protein] reductase (NADPH2, A-specific).
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Enoyl-%28acyl-carrier-protein%29%20reductase%20%28NADPH%2C%20B-specific%29 | In enzymology, an enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) () is an enzyme that catalyzes the chemical reaction
acyl-[acyl-carrier-protein] + NADP+ trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADPH + H+
Thus, the two substrates of this enzyme are [[acyl-[acyl-carrier-protein]]] and NADP+, whereas its 3 products are [[trans-2,3-dehydroacyl-[acyl-carrier-protein]]], NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, to be specific, those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is acyl-[acyl-carrier-protein]:NADP+ oxidoreductase (B-specific). Other names in common use include acyl-ACP dehydrogenase, reductase, enoyl-[acyl carrier protein] (reduced nicotinamide, adenine dinucleotide phosphate), NADPH 2-enoyl Co A reductase, enoyl acyl-carrier-protein reductase, enoyl-ACP reductase, and enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific). This enzyme participates in fatty acid biosynthesis.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Fumarate%20reductase%20%28NADH%29 | In enzymology, a fumarate reductase (NADH) () is an enzyme that catalyzes the chemical reaction
succinate + NAD+ fumarate + NADH + H+
Thus, the two substrates of this enzyme are succinate and NAD+, whereas its three products are fumarate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is succinate:NAD+ oxidoreductase. Other names in common use include NADH-fumarate reductase, NADH-dependent fumarate reductase, and fumarate reductase (NADH).
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Geissoschizine%20dehydrogenase | In enzymology, a geissoschizine dehydrogenase () is an enzyme that catalyzes the chemical reaction
geissoschizine + NADP+ 4,21-didehydrogeissoschizine + NADPH
Thus, the two substrates of this enzyme are geissoschizine and NADP+, whereas its two products are 4,21-didehydrogeissoschizine and NADPH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is geissoschizine:NADP+ 4,21-oxidoreductase. This enzyme participates in indole and ipecac alkaloid biosynthesis.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Isoquinoline%201-oxidoreductase | In enzymology, an isoquinoline 1-oxidoreductase () is an enzyme that catalyzes the chemical reaction
isoquinoline + acceptor + H2O isoquinolin-1(2H)-one + reduced acceptor
The 3 substrates of this enzyme are isoquinoline, acceptor, and H2O, whereas its two products are isoquinolin-1(2H)-one and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is isoquinoline:acceptor 1-oxidoreductase (hydroxylating).
References
EC 1.3.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Isovaleryl-CoA%20dehydrogenase | In enzymology, an isovaleryl-CoA dehydrogenase () is an enzyme that catalyzes the chemical reaction
3-methylbutanoyl-CoA + acceptor 3-methylbut-2-enoyl-CoA + reduced acceptor
Thus, the two substrates of this enzyme are 3-methylbutanoyl-CoA and acceptor, whereas its two products are 3-methylbut-2-enoyl-CoA and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is 3-methylbutanoyl-CoA:acceptor oxidoreductase. Other names in common use include isovaleryl-coenzyme A dehydrogenase, isovaleroyl-coenzyme A dehydrogenase, and 3-methylbutanoyl-CoA:(acceptor) oxidoreductase. This enzyme participates in valine, leucine and isoleucine degradation. It employs one cofactor, FAD.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code . It was created by a group containing K.A.Tiffany, D.L.Roberts, M.Wang, R.Paschke, A.-W.A.Mohsen, J.Vockley, and J.J.P.Kim. The structure was released on May 20, 1998.
Leucine metabolism
References
EC 1.3.8
Flavoproteins
Enzymes of known structure
Mitochondrial proteins |
https://en.wikipedia.org/wiki/Kynurenate-7%2C8-dihydrodiol%20dehydrogenase | In enzymology, a kynurenate-7,8-dihydrodiol dehydrogenase () is an enzyme that catalyzes the chemical reaction
7,8-dihydro-7,8-dihydroxykynurenate + NAD+ 7,8-dihydroxykynurenate + NADH + H+
Thus, the two substrates of this enzyme are 7,8-dihydro-7,8-dihydroxykynurenate and NAD+, whereas its 3 products are 7,8-dihydroxykynurenate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 7,8-dihydro-7,8-dihydroxykynurenate:NAD+ oxidoreductase. Other names in common use include 7,8-dihydro-7,8-dihydroxykynurenate dehydrogenase, and 7,8-dihydroxykynurenic acid 7,8-diol dehydrogenase. This enzyme participates in tryptophan metabolism.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/L-galactonolactone%20oxidase | In enzymology, a L-galactonolactone oxidase () is an enzyme that catalyzes the chemical reaction
L-galactono-1,4-lactone + O2 L-ascorbate + H2O2
Thus, the two substrates of this enzyme are L-galactono-1,4-lactone and O2, whereas its two products are L-ascorbic acid and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donors with oxygen as acceptor. The systematic name of this enzyme class is L-galactono-1,4-lactone:oxygen 3-oxidoreductase. This enzyme is also called L-galactono-1,4-lactone oxidase. This enzyme participates in ascorbic acid and aldaric acid metabolism. It employs one cofactor, FAD.
References
EC 1.3.3
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Maleylacetate%20reductase | In enzymology, a maleylacetate reductase () is an enzyme that catalyzes the chemical reaction
3-oxoadipate + NAD(P)+ 2-maleylacetate + NAD(P)H + H+
The 3 substrates of this enzyme are 3-oxoadipate, NAD+, and NADP+, whereas its 4 products are 2-maleylacetate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-oxoadipate:NAD(P)+ oxidoreductase. This enzyme is also called maleolylacetate reductase. This enzyme participates in 3 metabolic pathways: gamma-hexachlorocyclohexane degradation, benzoate degradation via hydroxylation, and 1,4-dichlorobenzene degradation.
References
EC 1.3.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Meso-tartrate%20dehydrogenase | In enzymology, a meso-tartrate dehydrogenase () is an enzyme that catalyzes the chemical reaction
meso-tartrate + NAD+ dihydroxyfumarate + NADH + H+
Thus, the two substrates of this enzyme are meso-tartaric acid and NAD+, whereas its 3 products are dihydroxyfumarate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is meso-tartrate:NAD+ oxidoreductase. This enzyme participates in glyoxylic acid and dicarboxylic acid metabolism.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Orotate%20reductase%20%28NADH%29 | In enzymology, an orotate reductase (NADH) () is an enzyme that catalyzes the chemical reaction
(S)-dihydroorotate + NAD+ orotate + NADH + H+
Thus, the two substrates of this enzyme are (S)-dihydroorotate and NAD+, whereas its 3 products are orotate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-dihydroorotate:NAD+ oxidoreductase. This enzyme is also called orotate reductase (NADH). This enzyme participates in pyrimidine metabolism. It has 2 cofactors: FAD, and FMN.
References
EC 1.3.1
NADH-dependent enzymes
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Orotate%20reductase%20%28NADPH%29 | In enzymology, an orotate reductase (NADPH) () is an enzyme that catalyzes the chemical reaction
(S)-dihydroorotate + NADP+ orotate + NADPH + H+
Thus, the two substrates of this enzyme are (S)-dihydroorotate and NADP+, whereas its 3 products are orotate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-dihydroorotate:NADP+ oxidoreductase. Other names in common use include orotate reductase, dihydroorotate dehydrogenase, dihydro-orotic dehydrogenase, L-5,6-dihydro-orotate:NAD+ oxidoreductase, and orotate reductase (NADPH). It has one cofactor, FAD.
References
EC 1.3.1
NADPH-dependent enzymes
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phloroglucinol%20reductase | In enzymology, a phloroglucinol reductase () is an enzyme that catalyzes the chemical reaction
dihydrophloroglucinol + NADP+ phloroglucinol + NADPH + H+
Thus, the two substrates of this enzyme are dihydrophloroglucinol and NADP+, whereas its 3 products are phloroglucinol, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is dihydrophloroglucinol:NADP+ oxidoreductase. This enzyme participates in benzoate degradation via coa ligation.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphatidylcholine%20desaturase | In enzymology, a phosphatidylcholine desaturase (, previously EC 1.3.1.35) is an enzyme that catalyzes the chemical reaction
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + NAD+ 1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + NADH + H+
Thus, the two substrates of this enzyme are 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine and NAD+, whereas its 3 products are 1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine:NAD+ Delta12-oxidoreductase. Other names in common use include oleate desaturase, linoleate synthase, oleoyl-CoA desaturase, and oleoylphosphatidylcholine desaturase.
References
EC 1.14.19
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phthalate%204%2C5-cis-dihydrodiol%20dehydrogenase | In enzymology, a phthalate 4,5-cis-dihydrodiol dehydrogenase () is an enzyme that catalyzes the chemical reaction
cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,2-dicarboxylate + NAD+ 4,5-dihydroxyphthalate + NADH + H+
Thus, the two substrates of this enzyme are cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,2-dicarboxylate and NAD+, whereas its 3 products are 4,5-dihydroxyphthalate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,2-dicarboxylate:NAD+ oxidoreductase. This enzyme participates in 2,4-dichlorobenzoate degradation.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phycocyanobilin%3Aferredoxin%20oxidoreductase | In enzymology, a phycocyanobilin:ferredoxin oxidoreductase (PcyA, ) is an enzyme that catalyzes the chemical reaction
(3Z)-phycocyanobilin + oxidized ferredoxin biliverdin IXalpha + reduced ferredoxin
Thus, the two substrates of this enzyme are (3Z)-phycocyanobilin and oxidized ferredoxin, whereas its two products are biliverdin IXalpha and reduced ferredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is (3Z)-phycocyanobilin:ferredoxin oxidoreductase. This enzyme participates in porphyrin and chlorophyll metabolism.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 1.3.7
Enzymes of known structure |
https://en.wikipedia.org/wiki/Phycoerythrobilin%3Aferredoxin%20oxidoreductase | In enzymology, a phycoerythrobilin:ferredoxin oxidoreductase () is an enzyme that catalyzes the chemical reaction
(3Z)-phycoerythrobilin + oxidized ferredoxin 15,16-dihydrobiliverdin + reduced ferredoxin
Thus, the two substrates of this enzyme are (3Z)-phycoerythrobilin and oxidized ferredoxin, whereas its two products are 15,16-dihydrobiliverdin and reduced ferredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is (3Z)-phycoerythrobilin:ferredoxin oxidoreductase. This enzyme is also called PebB. This enzyme participates in porphyrin and chlorophyll metabolism.
References
EC 1.3.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phytochromobilin%3Aferredoxin%20oxidoreductase | In enzymology, a phytochromobilin:ferredoxin oxidoreductase () is an enzyme that catalyzes the chemical reaction
(3Z)-phytochromobilin + oxidized ferredoxin biliverdin IXalpha + reduced ferredoxin
Thus, the two substrates of this enzyme are (3Z)-phytochromobilin and oxidized ferredoxin, whereas its two products are biliverdin IXalpha and reduced ferredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is (3Z)-phytochromobilin:ferredoxin oxidoreductase. Other names in common use include HY2, PPhiB synthase, and phytochromobilin synthase. This enzyme participates in porphyrin and chlorophyll metabolism.
References
EC 1.3.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pimeloyl-CoA%20dehydrogenase | In enzymology, a pimeloyl-CoA dehydrogenase () is an enzyme that catalyzes the chemical reaction
pimeloyl-CoA + NAD+ 6-carboxyhex-2-enoyl-CoA + NADH + H+
Thus, the two substrates of this enzyme are pimeloyl-CoA and NAD+, whereas its 3 products are 6-carboxyhex-2-enoyl-CoA, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is pimeloyl-CoA:NAD+ oxidoreductase. This enzyme participates in benzoate degradation via coa ligation.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Precorrin-2%20dehydrogenase | In enzymology, a precorrin-2 dehydrogenase () is an enzyme that catalyzes the chemical reaction
precorrin-2 + NAD+ sirohydrochlorin + NADH + H+
The two substrates of this enzyme are precorrin-2 and NAD+; its three products are sirohydrochlorin, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is precorrin-2:NAD+ oxidoreductase. Other names in common use include Met8p, SirC, and CysG. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in anaerobic bacteria and to Cofactor F430.
See also
Cobalamin biosynthesis
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Precorrin-6A%20reductase | In enzymology, a precorrin-6A reductase () is an enzyme that catalyzes the chemical reaction
precorrin-6A + NADPH + H+ precorrin-6B + NADP+
The three substrates of this enzyme are precorrin 6A, NADPH and a proton; its two products are precorrin 6B and NADP+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH=CH group of an acceptor with NAD or NADPH as donor. The systematic name of this enzyme class is precorrin-6B:NADP+ oxidoreductase. Other names in common use include precorrin-6X reductase, precorrin-6Y:NADP+ oxidoreductase and CobK. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in aerobic bacteria.
See also
Cobalamin biosynthesis
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Prephenate%20dehydrogenase | Prephenate dehydrogenase is an enzyme found in the shikimate pathway, and helps catalyze the reaction from prephenate to tyrosine.
Nomenclature
Gene: (Saccharomyces Cerevisiae) TYR1
Shikimate pathway: Arogenate/Prephenate (ADH/PDH). Although in the shikimate pathway arogenate and prephenate dehydrogenase catalyze different reactions, they can at times be used interchangeably.
TyrA (tyrosine A: within the tyrosine pathway)
Prephenate dehydrogenase
Prephenate (Nicotinamide adenine dinucleotide phosphate) dehydrogenase
Prephenate dehydrogenase (NADP)
NADP+ oxidoreductase
Homology
This enzyme so far has been found in sixteen different organisms; twelve different kinds of bacteria (mostly cyanobacteria) and four different kinds of plants (mostly different kinds of beans).
Bacteria organisms (examples): Acenitobacter calcoaceticus, Fischerella sp., Flavobacterium so., Comamonas testosteroni, and nostoc sp.
Plant organisms: phaseolus coccineus, phaseolus vulgaris, vicia faba, vigna radiata
Function
Present in the shikimate pathway, in the pathway to synthesize tyrosine (a non-essential amino acid in both plants and animals). It catalyzes the oxidative decarboxylation reaction of prephenate to 4-hydroxyphenylpyruvate.
Reaction
In enzymology, a prephenate dehydrogenase () is an enzyme that catalyzes the chemical reaction
prephenate + NAD+ 4-hydroxyphenylpyruvate + CO2 + NADH
Thus, the two substrates of this enzyme are prephenate and NAD+, whereas its 3 products are |
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