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https://en.wikipedia.org/wiki/Phosphogluconate%20dehydrogenase%20%28decarboxylating%29 | In enzymology, a phosphogluconate dehydrogenase (decarboxylating) () is an enzyme that catalyzes the chemical reaction
6-phospho-D-gluconate + NADP+ D-ribulose 5-phosphate + CO2 + NADPH
Thus, the two substrates of this enzyme are 6-phospho-D-gluconate and NADP+, whereas its 3 products are D-ribulose 5-phosphate, CO2, and NADPH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 6-phospho-D-gluconate:NADP+ 2-oxidoreductase (decarboxylating). Other names in common use include phosphogluconic acid dehydrogenase, 6-phosphogluconic dehydrogenase, 6-phosphogluconic carboxylase, 6-phosphogluconate dehydrogenase (decarboxylating), and 6-phospho-D-gluconate dehydrogenase. This enzyme participates in pentose phosphate pathway. It employs one cofactor, manganese.
Enzyme Structure
The general structure, as well as several critical residues, on 6-phosphogluconate dehydrogenase appear to be well conserved over various species. The enzyme is a dimer, with each subunit containing three domains. The N-terminal coenzyme binding domain contains a Rossmann fold with additional α/β units. The second domain consists of a number of alpha helical structures, and the C-terminal domain consists of a short tail. The tails of the two subunits interact with each other to form a mobile lid on the enzyme's active site.
As of late 2007, 11 structures have been solved fo |
https://en.wikipedia.org/wiki/Prostaglandin-E2%209-reductase | {{DISPLAYTITLE:Prostaglandin-E2 9-reductase}}
In enzymology, a prostaglandin-E2 9-reductase () is an enzyme that catalyzes the chemical reaction
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+ (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate + NADPH + H+
Thus, the two substrates of this enzyme are (5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate and NADP+, whereas its 3 products are (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate:NADP+ 9-oxidoreductase. Other names in common use include PGE2-9-OR, reductase, 15-hydroxy-9-oxoprostaglandin, 9-keto-prostaglandin E2 reductase, 9-ketoprostaglandin reductase, PGE-9-ketoreductase, PGE2 9-oxoreductase, PGE2 reductase-9-ketoreductase, prostaglandin 9-ketoreductase, prostaglandin E 9-ketoreductase, and prostaglandin E2 reductase-9-oxoreductase. This enzyme participates in arachidonic acid metabolism.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Pterocarpin%20synthase | In enzymology, a pterocarpin synthase () is an enzyme that catalyzes the chemical reaction
medicarpin + NADP+ + H2O vestitone + NADPH + H+
The 3 substrates of this enzyme are medicarpin, NADP+, and H2O, whereas its 3 products are vestitone, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is medicarpin:NADP+ 2'-oxidoreductase. This enzyme is also called pterocarpan synthase. This enzyme participates in isoflavonoid biosynthesis.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure
Isoflavonoids metabolism |
https://en.wikipedia.org/wiki/Pyridoxal%204-dehydrogenase | In enzymology, a pyridoxal 4-dehydrogenase () is an enzyme that catalyzes the chemical reaction
pyridoxal + NAD+ 4-pyridoxolactone + NADH + H+
Thus, the two substrates of this enzyme are pyridoxal and NAD+, whereas its 3 products are 4-pyridoxolactone, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is pyridoxal:NAD+ 4-oxidoreductase. This enzyme is also called pyridoxal dehydrogenase. This enzyme participates in vitamin B6 metabolism.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Pyridoxine%204-dehydrogenase | In enzymology, a pyridoxine 4-dehydrogenase () is an enzyme that catalyzes the chemical reaction
pyridoxine + NADP+ pyridoxal + NADPH + H+
Thus, the two substrates of this enzyme are pyridoxine and NADP+, whereas its 3 products are pyridoxal, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is pyridoxine:NADP+ 4-oxidoreductase. Other names in common use include pyridoxin dehydrogenase, pyridoxol dehydrogenase, and pyridoxine dehydrogenase. This enzyme participates in vitamin B6 metabolism.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Quinate%20dehydrogenase | In enzymology, a quinate dehydrogenase () is an enzyme that catalyzes the chemical reaction
L-quinate + NAD+ 3-dehydroquinate + NADH + H+
Thus, the two substrates of this enzyme are L-quinate and NAD+, whereas its 3 products are 3-dehydroquinate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-quinate:NAD+ 3-oxidoreductase. Other names in common use include quinic dehydrogenase, quinate:NAD oxidoreductase, quinate 5-dehydrogenase, and quinate:NAD+ 5-oxidoreductase. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Retinol%20dehydrogenase | In enzymology, a retinol dehydrogenase (RDH) () is an enzyme that catalyzes the chemical reaction
retinol + NAD+ retinal + NADH + H+
Sometimes, in addition to or along with NAD+, NADP+ can act as a preferred cofactor in the reaction as well. The substrate of the enzyme can be all-trans- or -cis- retinol. There are at least over 20 different isolated enzymes with RDH activity to date. Thus, the two substrates of this enzyme are retinol and NAD+, whereas its 3 products are retinal, NADH (or NADPH in the case where NADP+ is a cofactor), and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is retinol:NAD+ oxidoreductase. Other names in common use include retinol (vitamin A1) dehydrogenase, MDR, microsomal retinol dehydrogenase, all-trans retinol dehydrogenase, retinal reductase, and retinene reductase. This enzyme participates in retinol metabolism. Occasionally, the literature refers to retinol dehydrogenase as an enzyme that oxidizes retinol in general, such as class IV alcohol dehydrogenase (ADH4), which reportedly is the most efficient retinol oxidation in the human alcohol dehydrogenase (ADH) family.
Structure
As one of the most important RDH, 11-cis-retinol dehydrogenase catalyzes the 11-cis retinaldehyde (the most common visual pigments in higher animals) formation. The enzyme is mainly expressed in the retinal pigment epithelium (R |
https://en.wikipedia.org/wiki/Ribitol%202-dehydrogenase | In enzymology, a ribitol 2-dehydrogenase () is an enzyme that catalyzes the chemical reaction
ribitol + NAD+ D-ribulose + NADH + H+
Thus, the two substrates of this enzyme are ribitol and NAD+, whereas its 3 products are D-ribulose, NADH, and H+.
This enzyme participates in pentose and glucuronate interconversions.
Nomenclature
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is ribitol:NAD+ 2-oxidoreductase. Other names in common use include adonitol dehydrogenase, ribitol dehydrogenase A (wild type), ribitol dehydrogenase B (mutant enzyme with different properties), and ribitol dehydrogenase D (mutant enzyme with different properties).
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ribitol-5-phosphate%202-dehydrogenase | In enzymology, a ribitol-5-phosphate 2-dehydrogenase () is an enzyme that catalyzes the chemical reaction
D-ribitol 5-phosphate + NAD(P)+ D-ribulose 5-phosphate + NAD(P)H + H+
The 3 substrates of this enzyme are D-ribitol 5-phosphate, NAD+, and NADP+, whereas its 4 products are D-ribulose 5-phosphate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-ribitol-5-phosphate:NAD(P)+ 2-oxidoreductase. This enzyme is also called dehydrogenase, ribitol 5-phosphate. This enzyme participates in pentose and glucuronate interconversions.
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Testosterone%2017b-dehydrogenase%20%28NADP%2B%29 | Testosterone 17beta-dehydrogenase (NADP+) (, 17-ketoreductase, NADP-dependent testosterone-17beta-oxidoreductase, testosterone 17beta-dehydrogenase (NADP)) is an enzyme with systematic name 17beta-hydroxysteroid:NADP+ 17-oxidoreductase. This enzyme catalyses the following chemical reaction
testosterone + NADP+ androstenedione + NADPH + H+
Also oxidizes 3-hydroxyhexobarbital to 3-oxohexobarbital.
References
External links
EC 1.1.1
Steroid hormone biosynthesis |
https://en.wikipedia.org/wiki/Ribose%201-dehydrogenase%20%28NADP%2B%29 | {{DISPLAYTITLE:Ribose 1-dehydrogenase (NADP+)}}
In enzymology, a ribose 1-dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
D-ribose + NADP+ + H2O D-ribonate + NADPH + H+
The three substrates of this enzyme are D-ribose, NADP+, and H2O, whereas its 3 products are D-ribonate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-ribose:NADP+ 1-oxidoreductase. Other names in common use include D-ribose dehydrogenase (NADP+), NADP+-pentose-dehydrogenase, and ribose 1-dehydrogenase (NADP+).
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Salutaridine%20reductase%20%28NADPH%29 | In enzymology, a salutaridine reductase (NADPH) () is an enzyme that catalyzes the chemical reaction
salutaridinol + NADP+ salutaridine + NADPH + H+
Thus, the two substrates of this enzyme are salutaridinol and NADP+, whereas its 3 products are salutaridine, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is salutaridinol:NADP+ 7-oxidoreductase. This enzyme participates in alkaloid biosynthesis i.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sepiapterin%20reductase | Sepiapterin reductase is an enzyme that in humans is encoded by the SPR gene.
Function
Sepiapterin reductase (7,8-dihydrobiopterin:NADP+ oxidoreductase; EC 1.1.1.153) catalyzes the NADPH-dependent reduction of various carbonyl substances, including derivatives of pteridines, and belongs to a group of enzymes called aldo-keto reductases. SPR plays an important role in the biosynthesis of tetrahydrobiopterin.
Reaction
Sepiapterin reductase (SPR) catalyzes the chemical reaction
L-erythro-7,8-dihydrobiopterin + NADP+ sepiapterin + NADPH + H+
Thus, the two substrates of this enzyme are L-erythro-7,8-dihydrobiopterin and NADP+, whereas its three products are sepiapterin, NADPH, and a single hydrogen ion (H+).
This enzyme belongs to the family of oxidoreductases, to be specific, those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 7,8-dihydrobiopterin:NADP+ oxidoreductase. This enzyme participates in folate biosynthesis.
Clinical significance
Mutations of the SPR gene may cause sepiapterin reductase deficiency, a rare disease. The clinical phenotype can include progressive psychomotor retardation, altered tone, seizures, choreoathetosis, temperature instability, hypersalivation, microcephaly, and irritability. Patients with sepiapterin reductase deficiency also manifest dystonia with diurnal variation, oculogyric crises, tremor, hypersomnolence, oculomotor apraxia, and weakness. Response to treatment is var |
https://en.wikipedia.org/wiki/S-%28hydroxymethyl%29glutathione%20dehydrogenase | In enzymology, a S-(hydroxymethyl)glutathione dehydrogenase () is an enzyme that catalyzes the chemical reaction
S-(hydroxymethyl)glutathione + NAD(P)+ S-formylglutathione + NAD(P)H + H+
The 3 substrates of this enzyme are S-(hydroxymethyl)glutathione, NAD+, and NADP+, whereas its 4 products are S-formylglutathione, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is S-(hydroxymethyl)glutathione:NAD+ oxidoreductase. Other names in common use include NAD-linked formaldehyde dehydrogenase (incorrect), formaldehyde dehydrogenase (incorrect), formic dehydrogenase (incorrect), class III alcohol dehydrogenase, ADH3, &chi, -ADH, FDH (incorrect), formaldehyde dehydrogenase (glutathione) (incorrect), GS-FDH (incorrect), glutathione-dependent formaldehyde dehydrogenase (incorrect), NAD-dependent formaldehyde dehydrogenase, GD-FALDH, and NAD- and glutathione-dependent formaldehyde dehydrogenase. This enzyme participates in methane metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Sorbose%205-dehydrogenase%20%28NADP%2B%29 | {{DISPLAYTITLE:Sorbose 5-dehydrogenase (NADP+)}}
In enzymology, a sorbose 5-dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
L-sorbose + NADP+ 5-dehydro-D-fructose + NADPH + H+
Thus, the two substrates of this enzyme are L-sorbose and NADP+, whereas its 3 products are 5-dehydro-D-fructose, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-sorbose:NADP+ 5-oxidoreductase. Other names in common use include 5-ketofructose reductase, 5-keto-D-fructose reductase, sorbose (nicotinamide adenine dinucleotide phosphate) dehydrogenase, reduced nicotinamide adenine dinucleotide phosphate-linked, reductase, and sorbose 5-dehydrogenase (NADP+).
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sorbose%20reductase | In enzymology, a sorbose reductase () is an enzyme that catalyzes the chemical reaction
D-glucitol + NADP+ L-sorbose + NADPH + H+
Thus, the two substrates of this enzyme are D-glucitol and NADP+, whereas its 3 products are L-sorbose, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-glucitol:NADP+ oxidoreductase. This enzyme is also called Sou1p.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sterol-4alpha-carboxylate%203-dehydrogenase%20%28decarboxylating%29 | In enzymology, a sterol-4alpha-carboxylate 3-dehydrogenase (decarboxylating) () is an enzyme that catalyzes the chemical reaction
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carboxylate + NAD(P)+ 4alpha-methyl-5alpha-cholest-7-en-3-one + CO2 + NAD(P)H
The 3 substrates of this enzyme are 3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carboxylate, NAD+, and NADP+, whereas its 4 products are 4alpha-methyl-5alpha-cholest-7-en-3-one, CO2, NADH, and NADPH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carboxylate:NAD(P)+ 3-oxidoreductase (decarboxylating). Other names in common use include 3beta-hydroxy-4beta-methylcholestenecarboxylate 3-dehydrogenase, (decarboxylating), 3beta-hydroxy-4beta-methylcholestenoate dehydrogenase, 3beta-hydroxy-4beta-methylcholestenoate dehydrogenase, and sterol 4alpha-carboxylic decarboxylase. This enzyme participates in biosynthesis of steroids.
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sulcatone%20reductase | In enzymology, a sulcatone reductase () is an enzyme that catalyzes the chemical reaction
sulcatol + NAD+ sulcatone + NADH + H+
Thus, the two substrates of this enzyme are sulcatol and NAD+, whereas its 3 products are sulcatone, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is sulcatol:NAD+ oxidoreductase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tagaturonate%20reductase | Tagaturonate reductase () is an enzyme that catalyzes the chemical reaction
D-altronate + NAD+ D-tagaturonate + NADH + H+
Thus, the two substrates of this enzyme are D-altronate and NAD+, whereas its 3 products are D-tagaturonate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-altronate:NAD+ 3-oxidoreductase. Other names in common use include altronic oxidoreductase, altronate oxidoreductase, TagUAR, altronate dehydrogenase, and D-tagaturonate reductase. This enzyme participates in pentose and glucuronate interconversions.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tartrate%20dehydrogenase | In enzymology, a tartrate dehydrogenase () is an enzyme that catalyzes the chemical reaction
tartrate + NAD+ oxaloglycolate + NADH + H+
Thus, the two substrates of this enzyme are tartrate and NAD+, whereas its 3 products are oxaloglycolate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is tartrate:NAD+ oxidoreductase. This enzyme is also called mesotartrate dehydrogenase. This enzyme participates in glyoxylate and dicarboxylate metabolism. It employs one cofactor, manganese.
References
EC 1.1.1
NADH-dependent enzymes
Manganese enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Testosterone%2017beta-dehydrogenase | In enzymology, a testosterone 17beta-dehydrogenase is an enzyme that catalyzes the chemical reaction between testosterone and androst-4-ene-3,17-dione. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor.
The systematic name of this enzyme class is 17beta-hydroxysteroid:NAD+ 17-oxidoreductase. Other names in common use include 17-ketoreductase and 17beta-HSD. This enzyme participates in androgen and estrogen metabolism.
Variants
There are two variants of the enzyme, one that uses NAD+ as a substrate, and one that uses NADP+ as acceptor.
NAD+
This variant of testosterone 17beta-dehydrogenase () catalyzes the reaction
testosterone + NAD+ androst-4-ene-3,17-dione + NADH + H+
Thus, the two substrates of this enzyme are testosterone and NAD+, whereas its 3 products are androst-4-ene-3,17-dione, NADH, and H+.
NADP+
This variant of testosterone 17beta-dehydrogenase () catalyzes the reaction
testosterone + NADP+ androst-4-ene-3,17-dione + NADPH + H+
Thus, the two substrates of this enzyme are testosterone and NADP+, whereas its 3 products are androst-4-ene-3,17-dione, NADPH, and H+.
References
External links
Testodren - Testosterone Booster
EC 1.1.1
Testosterone
NADH-dependent enzymes
NADPH-dependent enzymes
Enzymes of known structure
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tetrahydroxynaphthalene%20reductase | In enzymology, a tetrahydroxynaphthalene reductase () is an enzyme that catalyzes the chemical reaction
scytalone + NADP+ 1,3,6,8-tetrahydroxynaphthalene + NADPH + H+
Thus, the two substrates of this enzyme are scytalone and NADP+, whereas its 3 products are 1,3,6,8-tetrahydroxynaphthalene, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is scytalone:NADP+ Delta5-oxidoreductase.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Tropinone%20reductase%20I | In enzymology, a tropinone reductase I () is an enzyme that catalyzes the chemical reaction
tropine + NADP+ tropinone + NADPH + H+
Thus, the two substrates of this enzyme are tropine and NADP+, whereas its 3 products are tropinone, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is tropine:NADP+ 3alpha-oxidoreductase. Other names in common use include tropine dehydrogenase, tropinone reductase (ambiguous), and TR-I. This enzyme participates in alkaloid biosynthesis ii.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Tropinone%20reductase%20II | In enzymology, a tropinone reductase II () is an enzyme that catalyzes the chemical reaction
pseudotropine + NADP+ tropinone + NADPH + H+
Thus, the two substrates of this enzyme are pseudotropine and NADP+, whereas its 3 products are tropinone, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is pseudotropine:NADP+ 3-oxidoreductase. Other names in common use include tropinone (psi-tropine-forming) reductase, pseudotropine forming tropinone reductase, tropinone reductase (ambiguous), and TR-II. This enzyme participates in alkaloid biosynthesis ii.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/UDP-glucose%206-dehydrogenase | UDP-glucose 6-dehydrogenase is a cytosolic enzyme that in humans is encoded by the UGDH gene.
The protein encoded by this gene converts UDP-glucose to UDP-glucuronate and thereby participates in the biosynthesis of glycosaminoglycans such as hyaluronan, chondroitin sulfate, and heparan sulfate. These glycosylated compounds are common components of the extracellular matrix and likely play roles in signal transduction, cell migration, and cancer growth and metastasis. The expression of this gene is up-regulated by transforming growth factor beta and down-regulated by hypoxia.
This enzyme participates in 4 metabolic pathways: pentose and glucuronate interconversions, ascorbate and aldarate metabolism, starch and sucrose metabolism, and nucleotide sugars metabolism.
Loss of UGDH has recently been implicated in epileptic encephalopathy in humans
Nomenclature
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is UDP-glucose:NAD+ 6-oxidoreductase.
Other names in common use include:
UDP-glucose dehydrogenase,
uridine diphosphoglucose dehydrogenase,
UDPG dehydrogenase,
UDPG:NAD oxidoreductase,
UDP-alpha-D-glucose:NAD oxidoreductase,
UDP-glucose:NAD+ oxidoreductase,
uridine diphosphate glucose dehydrogenase,
UDP-D-glucose dehydrogenase, and
uridine diphosphate D-glucose dehydrogenase.
Biochemistry
In enzymology, a UDP-glucose 6-dehy |
https://en.wikipedia.org/wiki/UDP-N-acetylglucosamine%206-dehydrogenase | In enzymology, an UDP-N-acetylglucosamine 6-dehydrogenase () is an enzyme that catalyzes the chemical reaction
UDP-N-acetyl-D-glucosamine + 2 NAD+ + H2O UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + 2 NADH + 2 H+
The 3 substrates of this enzyme are UDP-N-acetyl-D-glucosamine, NAD+, and H2O, whereas its 3 products are UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is UDP-N-acetyl-D-glucosamine:NAD+ 6-oxidoreductase. Other names in common use include uridine diphosphoacetylglucosamine dehydrogenase, UDP-acetylglucosamine dehydrogenase, UDP-2-acetamido-2-deoxy-D-glucose:NAD oxidoreductase, and UDP-GlcNAc dehydrogenase. This enzyme participates in aminosugars metabolism.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/UDP-N-acetylmuramate%20dehydrogenase | In enzymology, an UDP-N-acetylmuramate dehydrogenase () is an enzyme that catalyzes the chemical reaction
UDP-N-acetyl-alpha-D-muramate + NADP+ UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine + NADPH + H+
Thus, the two substrates of this enzyme are UDP-N-acetyl-alpha-D-muramate and NADP+, whereas its 3 products are UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine, 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 UDP-N-acetyl-alpha-D-muramate:NADP+ oxidoreductase. Other names in common use include MurB reductase, UDP-N-acetylenolpyruvoylglucosamine reductase, UDP-N-acetylglucosamine-enoylpyruvate reductase, UDP-GlcNAc-enoylpyruvate reductase, uridine diphosphoacetylpyruvoylglucosamine reductase, uridine diphospho-N-acetylglucosamine-enolpyruvate reductase, uridine-5'-diphospho-N-acetyl-2-amino-2-deoxy-3-O-lactylglucose:NADP-oxidoreductase. This enzyme participates in aminosugars metabolism. It employs one cofactor, FAD.
Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , and .
References
EC 1.3.1
NADPH-dependent enzymes
Flavoproteins
Enzymes of known structure |
https://en.wikipedia.org/wiki/RMI%20Corporation | RMI Corporation, formerly Raza Microelectronics, Inc., was a privately held fabless semiconductor company headquartered in Cupertino, California, which specialized in designing system-on-a-chip processors for computer networking (known as network processors) and consumer media applications.
History
Saiyed Atiq Raza founded NexGen, which was acquired by AMD in 1995. Raza was AMD's president and chief operating officer in the late 1990s after the NexGen acquisition.
He left AMD in 1999 and founded Raza Microelectronics, Inc. in 2002.
In 2003, SandCraft Inc folded, and Raza acquired the rights to its intellectual property.
Behrooz Abdi became president and CEO in November 2007, and Raza Microelectronics changed its name to RMI Corporation in December 2007.
In January 2008 Raza settled with the US Securities and Exchange Commission over an allegation of insider trading during 2006.
RMI was not affiliated with Foundries Holdings, LLC, formerly known as Raza Foundries, Inc.
Most of RMI's revenue came from its multi-core processor product line, which had major customers from China including Huawei, ZTE, and H3C. The China business of RMI was built from scratch by its co-founder Sunny Siu. In 2008, RMI merged with NetLogic Microsystems, which was acquired by Broadcom in 2012.
Product lines
RMI had four product lines: three developed internally and one acquired.
The XLR (introduced circa 2005) was a multicore, multithreaded CPU used for network processing. XLR integrated circ |
https://en.wikipedia.org/wiki/Ureidoglycolate%20dehydrogenase | In enzymology, an ureidoglycolate dehydrogenase () is an enzyme that catalyzes the chemical reaction
(S)-ureidoglycolate + NAD(P)+ oxalurate + NAD(P)H + H+
The 3 substrates of this enzyme are (S)-ureidoglycolate, NAD+, and NADP+, whereas its 4 products are oxalurate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-ureidoglycolate:NAD(P)+ oxidoreductase. This enzyme participates in purine metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Uronate%20dehydrogenase | In enzymology, an uronate dehydrogenase () is an enzyme that catalyzes the chemical reaction
D-galacturonate + NAD+ + H2O + NADH + H+
The 3 substrates of this enzyme are D-galacturonate, NAD+, and H2O, whereas its 3 products are (the lactone of D-galactarate), NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is uronate:NAD+ 1-oxidoreductase. Other names in common use include uronate: NAD-oxidoreductase, and uronic acid dehydrogenase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/12alpha-hydroxysteroid%20dehydrogenase | In enzymology, a 12alpha-hydroxysteroid dehydrogenase () is an enzyme that catalyzes the chemical reaction
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + NADP+ 3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate + NADPH + H+
Thus, the two substrates of this enzyme are 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate and NADP+, whereas its 3 products are 3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 12alpha-hydroxysteroid:NADP+ 12-oxidoreductase. Other names in common use include 12alpha-hydroxy steroid dehydrogenase, 12alpha-hydroxy steroid dehydrogenase, NAD+-dependent 12alpha-hydroxysteroid dehydrogenase, and NADP+-12alpha-hydroxysteroid dehydrogenase. This enzyme is involved in a metabolic pathway that degrades bile acids into cholesterol.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/12beta-hydroxysteroid%20dehydrogenase | In enzymology, a 12beta-hydroxysteroid dehydrogenase () is an enzyme that catalyzes the chemical reaction
3alpha,7alpha,12beta-trihydroxy-5beta-cholanate + NADP+ 3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate + NADPH + H+
Thus, the two substrates of this enzyme are 3alpha,7alpha,12beta-trihydroxy-5beta-cholanate and NADP+, whereas its 3 products are 3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 12beta-hydroxysteroid:NADP+ 12-oxidoreductase. Other names in common use include 12beta-hydroxy steroid (nicotinamide adenine dinucleotide phosphate), and dehydrogenase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/1%2C3-propanediol%20dehydrogenase | In enzymology, a 1,3-propanediol dehydrogenase () is an enzyme that catalyzes the chemical reaction
propane-1,3-diol + NAD+ 3-hydroxypropanal + NADH + H+
Thus, the two substrates of this enzyme are propane-1,3-diol and NAD+, whereas its 3 products are 3-hydroxypropanal, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is propane-1,3-diol:NAD+ 1-oxidoreductase. Other names in common use include 3-hydroxypropionaldehyde reductase, 1,3-PD:NAD+ oxidoreductase, 1,3-propanediol:NAD+ oxidoreductase, and 1,3-propanediol dehydrogenase. This enzyme participates in ether lipid metabolism as a step in glycerolipid biosynthesis.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/1%2C5-anhydro-D-fructose%20reductase | In enzymology, a 1,5-anhydro-D-fructose reductase () is an enzyme that catalyzes the chemical reaction
1,5-anhydro-D-glucitol + NADP 1,5-anhydro-D-fructose + NADPH + H
Thus, the two substrates of this enzyme are 1,5-anhydro-D-glucitol and NADP, whereas its 3 products are 1,5-anhydro-D-fructose, NADPH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is 1,5-anhydro-D-glucitol:NADP oxidoreductase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/1%2C5-anhydro-D-fructose%20reductase%20%281%2C5-anhydro-D-mannitol-forming%29 | In enzymology, a 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming) () is an enzyme that catalyzes the chemical reaction
1,5-anhydro-D-mannitol + NADP 1,5-anhydro-D-fructose + NADPH + H
Thus, the two substrates of this enzyme are 1,5-anhydro-D-mannitol and NADP, whereas its 3 products are 1,5-anhydro-D-fructose, NADPH, and H.
This enzyme belongs to the common family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is 1,5-anhydro-D-mannitol:NADP oxidoreductase. Other names in common use include 1,5-anhydro-D-fructose reductase (ambiguous), and AFR.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/15-hydroxyicosatetraenoate%20dehydrogenase | In enzymology, a 15-hydroxyicosatetraenoate dehydrogenase () is an enzyme that catalyzes the chemical reaction
(15S)-15-hydroxy-5,8,11-cis-13-trans-icosatetraenoate + NAD(P)+ 15-oxo-5,8,11-cis-13-trans-icosatetraenoate + NAD(P)H + H+
The 3 substrates of this enzyme are 15-Hydroxyicosatetraenoic acid (i.e. 15(S)-15-hydroxy-5,8,11-cis-13-trans-icosatetraenoate), NAD+, and NADP+, whereas its 4 products are 15-oxo-5,8,11-cis-13-trans-icosatetraenoate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (15S)-15-hydroxy-5,8,11-cis-13-trans-icosatetraenoate:NAD(P)+ 15-oxidoreductase. This enzyme is also called 15-hydroxyeicosatetraenoate dehydrogenase. This enzyme participates in arachidonic acid metabolism.
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/15-hydroxyprostaglandin-D%20dehydrogenase%20%28NADP%2B%29 | {{DISPLAYTITLE:15-hydroxyprostaglandin-D dehydrogenase (NADP+)}}
In enzymology, a 15-hydroxyprostaglandin-D dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADP+ (5Z,13E)-9alpha-hydroxy-11,15-dioxoprosta-5,13-dienoate + NADPH + H+
Thus, the two substrates of this enzyme are (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate and NADP+, whereas its 3 products are (5Z,13E)-9alpha-hydroxy-11,15-dioxoprosta-5,13-dienoate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate:NADP+ 15-oxidoreductase. Other names in common use include prostaglandin-D 15-dehydrogenase (NADP+), dehydrogenase, prostaglandin D2, NADP+-PGD2 dehydrogenase, dehydrogenase, 15-hydroxyprostaglandin (nicotinamide adenine, dinucleotide phosphate), 15-hydroxy PGD2 dehydrogenase, 15-hydroxyprostaglandin dehydrogenase (NADP+), NADP+-dependent 15-hydroxyprostaglandin dehydrogenase, prostaglandin D2 dehydrogenase, NADP+-linked 15-hydroxyprostaglandin dehydrogenase, NADP+-specific 15-hydroxyprostaglandin dehydrogenase, NADP+-linked prostaglandin D2 dehydrogenase, and 15-hydroxyprostaglandin-D dehydrogenase (NADP+). This enzyme participates in arachidonic acid metabolism.
References
EC 1.1.1
NADPH-depende |
https://en.wikipedia.org/wiki/15-hydroxyprostaglandin%20dehydrogenase%20%28NAD%2B%29 | Hydroxyprostaglandin dehydrogenase 15-(NAD) (the HUGO-approved symbol = HPGD; HGNC ID, HGNC:5154), also called 15-hydroxyprostaglandin dehydrogenase (NAD+), (), is an enzyme that catalyzes the following chemical reaction:
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate + NAD+ (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate + NADH + H+
Thus, the two substrates of this enzyme are (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and NAD+, whereas its 3 products are (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate:NAD+ 15-oxidoreductase. Other names in common use include NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (type I), PGDH, 11alpha,15-dihydroxy-9-oxoprost-13-enoate:NAD+ 15-oxidoreductase, 15-OH-PGDH, 15-hydroxyprostaglandin dehydrogenase, 15-hydroxyprostanoic dehydrogenase, NAD+-specific 15-hydroxyprostaglandin dehydrogenase, prostaglandin dehydrogenase, and 15-hydroxyprostaglandin dehydrogenase (NAD+).
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/15-hydroxyprostaglandin%20dehydrogenase%20%28NADP%2B%29 | {{DISPLAYTITLE:15-hydroxyprostaglandin dehydrogenase (NADP+)}}
In enzymology, a 15-hydroxyprostaglandin dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
(13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate + NADP+ (13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate + NADPH + H+
Thus, the two substrates of this enzyme are (13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and NADP+, whereas its 3 products are (13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate:NADP+ 15-oxidoreductase. Other names in common use include NADP+-dependent 15-hydroxyprostaglandin dehydrogenase, NADP+-linked 15-hydroxyprostaglandin dehydrogenase, NADP+-specific 15-hydroxyprostaglandin dehydrogenase, type II 15-hydroxyprostaglandin dehydrogenase, and 15-hydroxyprostaglandin 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 1.1.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/15-hydroxyprostaglandin-I%20dehydrogenase%20%28NADP%2B%29 | {{DISPLAYTITLE:15-hydroxyprostaglandin-I dehydrogenase (NADP+)}}
In enzymology, a 15-hydroxyprostaglandin-I dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
(5Z,13E)-(15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13- dienoate + NADP+ (5Z,13E)-6,9alpha-epoxy-11alpha-hydroxy-15-oxoprosta-5,13-dienoate + NADPH + H+
The 3 substrates of this enzyme are (5Z,13E)-(15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13-, dienoate, and NADP+, whereas its 3 products are (5Z,13E)-6,9alpha-epoxy-11alpha-hydroxy-15-oxoprosta-5,13-dienoate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (5Z,13E)-(15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13-dienoa te:NADP+ 15-oxidoreductase. Other names in common use include prostacyclin dehydrogenase, PG I2 dehydrogenase, prostacyclin dehydrogenase, NADP+-linked 15-hydroxyprostaglandin (prostacyclin) dehydrogenase, NADP+-dependent PGI2-specific 15-hydroxyprostaglandin dehydrogenase, and 15-hydroxyprostaglandin-I dehydrogenase (NADP+).
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/16-alpha-hydroxysteroid%20dehydrogenase | In enzymology, a 16alpha-hydroxysteroid dehydrogenase () is an enzyme that catalyzes the chemical reaction
a 16alpha-hydroxysteroid + NAD(P)+ a 16-oxosteroid + NAD(P)H + H+
The 3 substrates of this enzyme are 16alpha-hydroxysteroid, NAD+, and NADP+, whereas its 4 products are 16-oxosteroid, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 16alpha-hydroxysteroid:NAD(P)+ 16-oxidoreductase. This enzyme is also called 16alpha-hydroxy steroid dehydrogenase.
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/20alpha-hydroxysteroid%20dehydrogenase | In enzymology, a 20-α-hydroxysteroid dehydrogenase () is an enzyme that catalyzes the chemical reaction
17alpha,20alpha-dihydroxypregn-4-en-3-one + NAD(P)+ 17alpha-hydroxyprogesterone + NAD(P)H + H+
The 3 substrates of this enzyme are 17alpha,20alpha-dihydroxypregn-4-en-3-one, NAD+, and NADP+, whereas its 4 products are 17-alpha-hydroxyprogesterone, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 20alpha-hydroxysteroid:NAD(P)+ 20-oxidoreductase. Other names in common use include 20alpha-hydroxy steroid dehydrogenase, 20alpha-hydroxy steroid dehydrogenase, 20alpha-HSD, and 20alpha-HSDH. This enzyme participates in c21-steroid hormone metabolism.
20alpha-HSD has been initially described as a progesterone metabolizing enzyme of the ovary. On a functional level, ovarian 20alpha-HSD is actively involved in the control of progesterone homeostasis in pregnancy of rats and mice. While 20alpha-HSD expression and activity is downregulated in the corpus luteum of pregnancy, 24 hrs prior to parturition ovarian 20alpha-HSD activity is acutely stimulated. Accordingly, in mice with targeted deletion of the 20alpha-HSD gene, progesterone blood concentration remain high throughout pregnancy which results in a delay of 2–4 days in parturition. Indicating that expression of 20alpha-HSD activity is mandatory for the induction of parturi |
https://en.wikipedia.org/wiki/21-hydroxysteroid%20dehydrogenase%20%28NAD%2B%29 | {{DISPLAYTITLE:21-hydroxysteroid dehydrogenase (NAD+)}}
In enzymology, a 21-hydroxysteroid dehydrogenase (NAD+) () is an enzyme that catalyzes the chemical reaction
pregnan-21-ol + NAD+ pregnan-21-al + NADH + H+
Thus, the two substrates of this enzyme are pregnan-21-ol and NAD+, whereas its 3 products are pregnan-21-al, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 21-hydroxysteroid:NAD+ 21-oxidoreductase. This enzyme is also called 21-hydroxysteroid dehydrogenase (NAD+).
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/21-hydroxysteroid%20dehydrogenase%20%28NADP%2B%29 | {{DISPLAYTITLE:21-hydroxysteroid dehydrogenase (NADP+)}}
In enzymology, a 21-hydroxysteroid dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
pregnan-21-ol + NADP+ pregnan-21-al + NADPH + H+
Thus, the two substrates of this enzyme are pregnan-21-ol and NADP+, whereas its 3 products are pregnan-21-al, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 21-hydroxysteroid:NADP+ 21-oxidoreductase. Other names in common use include 21-hydroxy steroid dehydrogenase, 21-hydroxy steroid (nicotinamide adenine dinucleotide phosphate), dehydrogenase, 21-hydroxy steroid dehydrogenase (nicotinamide adenine dinucleotide, phosphate), NADP+-21-hydroxysteroid dehydrogenase, and 21-hydroxysteroid dehydrogenase (NADP+).
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2%2C5-didehydrogluconate%20reductase | In enzymology, a 2,5-didehydrogluconate reductase () is an enzyme that catalyzes the chemical reaction
2-dehydro-D-gluconate + NADP+ 2,5-didehydro-D-gluconate + NADPH + H+
Thus, the two substrates of this enzyme are 2-dehydro-D-gluconate and NADP+, whereas its 3 products are 2,5-didehydro-D-gluconate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-dehydro-D-gluconate:NADP+ 2-oxidoreductase. Other names in common use include 2,5-diketo-D-gluconate reductase, and YqhE reductase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/2-alkyn-1-ol%20dehydrogenase | In enzymology, a 2-alkyn-1-ol dehydrogenase () is an enzyme that catalyzes the chemical reaction below:
2-butyne-1,4-diol + NAD+ 4-hydroxy-2-butynal + NADH + H+
The two substrates of this enzyme are 2-butyne-1,4-diol and NAD+, whereas its 3 products are 4-hydroxy-2-butynal, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-butyne-1,4-diol:NAD+ 1-oxidoreductase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycerol-3-phosphate%20dehydrogenase%20%28NAD%28P%29%2B%29 | {{DISPLAYTITLE:Glycerol-3-phosphate dehydrogenase (NAD(P)+)}}
In enzymology, a glycerol-3-phosphate dehydrogenase [NAD(P)+] () is an enzyme that catalyzes the chemical reaction
sn-glycerol 3-phosphate + NAD(P)+ glycerone phosphate + NAD(P)H + H+
The 3 substrates of this enzyme are sn-glycerol 3-phosphate, NAD+, and NADP+, whereas its 4 products are glycerone phosphate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is sn-glycerol-3-phosphate:NAD(P)+ 2-oxidoreductase. Other names in common use include L-glycerol-3-phosphate:NAD(P)+ oxidoreductase, glycerol phosphate dehydrogenase (nicotinamide adenine dinucleotide, (phosphate)), glycerol 3-phosphate dehydrogenase (NADP+), and glycerol-3-phosphate dehydrogenase [NAD(P)+]. This enzyme participates in glycerophospholipid metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/2-dehydro-3-deoxy-D-gluconate%205-dehydrogenase | In enzymology, a 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase () is an enzyme that catalyzes the chemical reaction
2-dehydro-3-deoxy-D-gluconate + NAD+ (4S)-4,6-dihydroxy-2,5-dioxohexanoate + NADH + H+
Thus, the two substrates of this enzyme are 2-dehydro-3-deoxy-D-gluconate and NAD+, whereas its 3 products are (4S)-4,6-dihydroxy-2,5-dioxohexanoate, NADH, and H+.
This enzyme participates in pentose and glucuronate interconversions.
Nomenclature
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-dehydro-3-deoxy-D-gluconate:NAD+ 5-oxidoreductase. Other names in common use include 2-keto-3-deoxygluconate 5-dehydrogenase, 2-keto-3-deoxy-D-gluconate dehydrogenase, 2-keto-3-deoxygluconate (nicotinamide adenine dinucleotide, (phosphate)) dehydrogenase, 2-keto-3-deoxy-D-gluconate (3-deoxy-D-glycero-2,5-hexodiulosonic, and acid) dehydrogenase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-dehydro-3-deoxy-D-gluconate%206-dehydrogenase | In enzymology, a 2-dehydro-3-deoxy-D-gluconate 6-dehydrogenase () is an enzyme that catalyzes the chemical reaction
2-dehydro-3-deoxy-D-gluconate + NADP+ (4S,5S)-4,5-dihydroxy-2,6-dioxohexanoate + NADPH + H+
Thus, the two substrates of this enzyme are 2-dehydro-3-deoxy-D-gluconate and NADP+, whereas its 3 products are (4S,5S)-4,5-dihydroxy-2,6-dioxohexanoate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-dehydro-3-deoxy-D-gluconate:NADP+ 6-oxidoreductase. Other names in common use include 2-keto-3-deoxy-D-gluconate dehydrogenase, and 2-keto-3-deoxygluconate dehydrogenase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/2-dehydropantoate%202-reductase | In enzymology, a 2-dehydropantoate 2-reductase () is an enzyme that catalyzes the chemical reaction
(R)-pantoate + NADP+ 2-dehydropantoate + NADPH + H+
Thus, the two substrates of this enzyme are (R)-pantoate and NADP+, whereas its 3 products are 2-dehydropantoate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-pantoate:NADP+ 2-oxidoreductase. Other names in common use include 2-oxopantoate reductase, 2-ketopantoate reductase, 2-ketopantoic acid reductase, ketopantoate reductase, and ketopantoic acid reductase. This enzyme participates in pantothenate and coa biosynthesis.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/2-dehydropantolactone%20reductase%20%28A-specific%29 | In enzymology, a 2-dehydropantolactone reductase (A-specific) () is an enzyme that catalyzes the chemical reaction
(R)-pantolactone + NADP+ 2-dehydropantolactone + NADPH + H+
Thus, the two substrates of this enzyme are (R)-pantolactone and NADP+, whereas its 3 products are 2-dehydropantolactone, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-pantolactone:NADP+ oxidoreductase (A-specific). Other names in common use include 2-oxopantoyl lactone reductase, ketopantoyl lactone reductase, 2-ketopantoyl lactone reductase, and 2-dehydropantoyl-lactone reductase (A-specific).
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-dehydropantolactone%20reductase%20%28B-specific%29 | In enzymology, a 2-dehydropantolactone reductase (B-specific) () is an enzyme that catalyzes the chemical reaction
(R)-pantolactone + NADP+ 2-dehydropantolactone + NADPH + H+
Thus, the two substrates of this enzyme are (R)-pantolactone and NADP+, whereas its 3 products are 2-dehydropantolactone, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-pantolactone:NADP+ oxidoreductase (B-specific). Other names in common use include 2-oxopantoyl lactone reductase, 2-ketopantoyl lactone reductase, ketopantoyl lactone reductase, and 2-dehydropantoyl-lactone reductase (B-specific).
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-deoxy-D-gluconate%203-dehydrogenase | 2-deoxy-D-gluconate 3-dehydrogenase () is an enzyme that catalyzes the chemical reaction
2-deoxy-D-gluconate + NAD+ 3-dehydro-2-deoxy-D-gluconate + NADH + H+
Thus, the two substrates of this enzyme are 2-deoxy-D-gluconate and NAD+, whereas its 3 products are 3-dehydro-2-deoxy-D-gluconate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-deoxy-D-gluconate:NAD+ 3-oxidoreductase. This enzyme is also called 2-deoxygluconate dehydrogenase. This enzyme participates in pentose and glucuronate interconversions.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/2-hydroxy-3-oxopropionate%20reductase | In enzymology, a 2-hydroxy-3-oxopropionate reductase () is an enzyme that catalyzes the chemical reaction
(R)-glycerate + NAD(P)+ 2-hydroxy-3-oxopropanoate + NAD(P)H + H+
The 3 substrates of this enzyme are (R)-glycerate, NAD+, and NADP+, whereas its 4 products are 2-hydroxy-3-oxopropanoate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-glycerate:NAD(P)+ oxidoreductase. This enzyme is also called tartronate semialdehyde reductase. This enzyme participates in glyoxylate and dicarboxylate metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/2-hydroxymethylglutarate%20dehydrogenase | In enzymology, a 2-hydroxymethylglutarate dehydrogenase () is an enzyme that catalyzes the chemical reaction
(S)-2-hydroxymethylglutarate + NAD+ 2-formylglutarate + NADH + H+
Thus, the two substrates of this enzyme are (S)-2-hydroxymethylglutarate and NAD+, whereas its 3 products are 2-formylglutarate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-2-hydroxymethylglutarate:NAD+ oxidoreductase. This enzyme is also called HgD.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-oxoadipate%20reductase | In enzymology, a 2-oxoadipate reductase () is an enzyme that catalyzes the chemical reaction
2-hydroxyadipate + NAD+ 2-oxoadipate + NADH + H+
Thus, the two substrates of this enzyme are 2-hydroxyadipate and NAD+, whereas its 3 products are 2-oxoadipate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-hydroxyadipate:NAD+ 2-oxidoreductase. Other names in common use include 2-ketoadipate reductase, alpha-ketoadipate reductase, and 2-ketoadipate reductase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-%28R%29-hydroxypropyl-CoM%20dehydrogenase | In enzymology, a 2-(R)-hydroxypropyl-CoM dehydrogenase () is an enzyme that catalyzes the chemical reaction
2-(R)-hydroxypropyl-CoM + NAD+ 2-oxopropyl-CoM + NADH + H+
Thus, the two substrates of this enzyme are 2-(R)-hydroxypropyl-CoM and NAD+, whereas its 3 products are 2-oxopropyl-CoM, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-[2-(R)-hydroxypropylthio]ethanesulfonate:NAD+ oxidoreductase. This enzyme is also called 2-(2-(R)-hydroxypropylthio)ethanesulfonate dehydrogenase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/2-%28S%29-hydroxypropyl-CoM%20dehydrogenase | In enzymology, a 2-(S)-hydroxypropyl-CoM dehydrogenase () is an enzyme that catalyzes the chemical reaction
2-(S)-hydroxypropyl-CoM + NAD+ 2-oxopropyl-CoM + NADH + H+
Thus, the two substrates of this enzyme are 2-(S)-hydroxypropyl-CoM and NAD+, whereas its 3 products are 2-oxopropyl-CoM, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-[2-(S)-hydroxypropylthio]ethanesulfonate:NAD+ oxidoreductase. This enzyme is also called 2-(2-(S)-hydroxypropylthio)ethanesulfonate dehydrogenase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3alpha%2817beta%29-hydroxysteroid%20dehydrogenase%20%28NAD%2B%29 | {{DISPLAYTITLE:3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+)}}
In enzymology, a 3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+) () is an enzyme that catalyzes the chemical reaction:
testosterone + NAD+ androst-4-ene-3,17-dione + NADH + H+
Thus, the two substrates of this enzyme are testosterone and NAD+, whereas its 3 products are androst-4-ene-3,17-dione, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3alpha(or 17beta)-hydroxysteroid:NAD+ oxidoreductase. Other names in common use include 3alpha,17beta-hydroxy steroid dehydrogenase, 3alpha(17beta)-HSD, and 3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+). This enzyme participates in androgen and estrogen metabolism.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3alpha-hydroxy-5beta-androstane-17-one%203alpha-dehydrogenase | In enzymology, a 3alpha-hydroxy-5beta-androstane-17-one 3alpha-dehydrogenase () is an enzyme that catalyzes the chemical reaction
3alpha-hydroxy-5beta-androstane-17-one + NAD+ 5beta-androstane-3,17-dione + NADH + H+
Thus, the two substrates of this enzyme are 3alpha-hydroxy-5beta-androstane-17-one and NAD+, whereas its 3 products are 5beta-androstane-3,17-dione, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3alpha-hydroxy-5beta-steroid:NAD+ 3-oxidoreductase. Other names in common use include etiocholanolone 3alpha-dehydrogenase, etiocholanolone 3alpha-dehydrogenase, and 3alpha-hydroxy-5beta-steroid dehydrogenase. This enzyme participates in androgen and estrogen metabolism.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3alpha-hydroxycholanate%20dehydrogenase | In enzymology, a 3alpha-hydroxycholanate dehydrogenase () is an enzyme that catalyzes the chemical reaction
3alpha-hydroxy-5beta-cholanate + NAD+ 3-oxo-5beta-cholanate + NADH + H+
Thus, the two substrates of this enzyme are 3alpha-hydroxy-5beta-cholanate and NAD+, whereas its 3 products are 3-oxo-5beta-cholanate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3alpha-hydroxy-5beta-cholanate:NAD+ oxidoreductase. This enzyme is also called alpha-hydroxy-cholanate dehydrogenase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/3alpha-hydroxyglycyrrhetinate%20dehydrogenase | In enzymology, a 3alpha-hydroxyglycyrrhetinate dehydrogenase () is an enzyme that catalyzes the chemical reaction
3alpha-hydroxyglycyrrhetinate + NADP+ 3-oxoglycyrrhetinate + NADPH + H+
Thus, the two substrates of this enzyme are 3alpha-hydroxyglycyrrhetinate and NADP+, whereas its 3 products are 3-oxoglycyrrhetinate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3alpha-hydroxyglycyrrhetinate:NADP+ 3-oxidoreductase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3alpha-hydroxysteroid%20dehydrogenase%20%28A-specific%29 | In enzymology, a 3alpha-hydroxysteroid dehydrogenase (A-specific) () is an enzyme that catalyzes the chemical reaction
androsterone + NAD(P)+ 5alpha-androstane-3,17-dione + NAD(P)H + H+
The 3 substrates of this enzyme are androsterone, NAD+, and NADP+, whereas its 4 products are 5alpha-androstane-3,17-dione, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor, more specifically it is part of the group of hydroxysteroid dehydrogenases. The systematic name of this enzyme class is 3alpha-hydroxysteroid:NAD(P)+ oxidoreductase (A-specific).
Structural studies
As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , and .
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/3alpha-hydroxysteroid%20dehydrogenase%20%28B-specific%29 | In enzymology, a 3alpha-hydroxysteroid dehydrogenase (B-specific) () is an enzyme that catalyzes the chemical reaction
androsterone + NAD(P)+ 5alpha-androstane-3,17-dione + NAD(P)H + H+
The 3 substrates of this enzyme are androsterone, NAD+, and NADP+, whereas its 4 products are 5alpha-androstane-3,17-dione, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor, more specifically it is part of the group of hydroxysteroid dehydrogenases. The systematic name of this enzyme class is 3alpha-hydroxysteroid:NAD(P)+ oxidoreductase (B-specific). Other names in common use include hydroxyprostaglandin dehydrogenase, 3alpha-hydroxysteroid oxidoreductase, and sterognost 3alpha. This enzyme participates in 3 metabolic pathways: bile acid biosynthesis, c21-steroid hormone metabolism, and androgen and estrogen metabolism.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/3alpha%28or%2020beta%29-hydroxysteroid%20dehydrogenase | In enzymology, a 3alpha(or 20beta)-hydroxysteroid dehydrogenase () is an enzyme that catalyzes the chemical reaction
androstan-3alpha,17beta-diol + NAD+ 17beta-hydroxyandrostan-3-one + NADH + H+
Thus, the two substrates of this enzyme are androstan-3alpha,17beta-diol and NAD+, whereas its 3 products are 17beta-hydroxyandrostan-3-one, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3alpha(or 20beta)-hydroxysteroid:NAD+ oxidoreductase. Other names in common use include cortisone reductase, (R)-20-hydroxysteroid dehydrogenase, dehydrogenase, 20beta-hydroxy steroid, Delta4-3-ketosteroid hydrogenase, 20beta-hydroxysteroid dehydrogenase, 3alpha,20beta-hydroxysteroid:NAD+-oxidoreductase, NADH-20beta-hydroxysteroid dehydrogenase, and 20beta-HSD. This enzyme participates in bile acid biosynthesis and c21-steroid hormone metabolism.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/3beta-hydroxy-5alpha-steroid%20dehydrogenase | In enzymology, a 3β-hydroxy-5α-steroid dehydrogenase () is an enzyme that catalyzes the chemical reaction
3β-hydroxy-5α-pregnane-20-one + NADP+ 5α-pregnan-3,20-dione + NADPH + H+
Thus, the two substrates of this enzyme are 3β-hydroxy-5α-pregnane-20-one (allopregnanolone) and NADP+, whereas its 3 products are 5α-pregnan-3,20-dione, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3β-hydroxy-5α-steroid:NADP+ 3-oxidoreductase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3beta-hydroxy-5beta-steroid%20dehydrogenase | In enzymology, a 3beta-hydroxy-5beta-steroid dehydrogenase () is an enzyme that catalyzes the chemical reaction
3beta-hydroxy-5beta-pregnane-20-one + NADP+ 5beta-pregnan-3,20-dione + NADPH + H+
Thus, the two substrates of this enzyme are 3beta-hydroxy-5beta-pregnane-20-one and NADP+, whereas its 3 products are 5beta-pregnan-3,20-dione, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3beta-hydroxy-5beta-steroid:NADP+ 3-oxidoreductase. Other names in common use include 3beta-hydroxysteroid 5beta-oxidoreductase, and 3beta-hydroxysteroid 5beta-progesterone oxidoreductase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3beta%28or%2020alpha%29-hydroxysteroid%20dehydrogenase | In enzymology, a 3-β(or 20-α)-hydroxysteroid dehydrogenase () is an enzyme that catalyzes the chemical reaction
5α-androstan-3β,17β-diol + NADP+ 17β-hydroxy-5α-androstan-3-one + NADPH + H+
This enzyme possesses the combined activities of the 3-β-hydroxysteroid dehydrogenase/Δ-5-4 isomerase and 20-α-hydroxysteroid dehydrogenase enzymes.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3%22-deamino-3%22-oxonicotianamine%20reductase | In enzymology, a 3"-deamino-3"-oxonicotianamine reductase () is an enzyme that catalyzes the chemical reaction
2'-deoxymugineic acid + NAD(P)+ 3"-deamino-3"-oxonicotianamine + NAD(P)H + H+
The 3 substrates of this enzyme are 2'-deoxymugineic acid, NAD+, and NADP+, whereas its 4 products are 3-deamino-3-oxonicotianamine, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-deoxymugineic acid:NAD(P)+ 3-oxidoreductase.
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-dehydro-L-gulonate%202-dehydrogenase | In enzymology, a 3-dehydro-L-gulonate 2-dehydrogenase () is an enzyme that catalyzes the chemical reaction:
3-dehydro-L-gulonate + NAD(P)+ (4R,5S)-4,5,6-trihydroxy-2,3-dioxohexanoate + NAD(P)H + H+
The 3 substrates of this enzyme are 3-dehydro-L-gulonate, NAD+, and NADP+, whereas its 4 products are (4R,5S)-4,5,6-trihydroxy-2,3-dioxohexanoate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-dehydro-L-gulonate:NAD(P)+ 2-oxidoreductase. Other names in common use include 3-keto-L-gulonate dehydrogenase, 3-ketogulonate dehydrogenase, 3-keto-L-gulonate dehydrogenase, and 3-ketogulonate dehydrogenase. This enzyme participates in pentose and glucuronate interconversions and ascorbate and aldarate metabolism.
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/3-dehydrosphinganine%20reductase | 3-dehydrosphinganine reductase () also known as 3-ketodihydrosphingosine reductase (KDSR) or follicular variant translocation protein 1 (FVT1) is an enzyme that in humans is encoded by the KDSR gene.
Function
3-dehydrosphinganine reductase catalyzes the chemical reaction:
sphinganine + NADP+ 3-dehydrosphinganine + NADPH + H+
Thus, the two substrates of this enzyme are sphinganine and NADP+, whereas its 3 products are 3-dehydrosphinganine, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in sphingolipid metabolism.
Tissue distribution
Follicular lymphoma variant translocation 1 is a secreted protein which is weakly expressed in hematopoietic tissue.
Clinical significance
FVT1 shows a high rate of transcription in some T cell malignancies and in phytohemagglutinin-stimulated lymphocytes. The proximity of FVT1 to BCL2 suggests that it may participate in the tumoral process.
References
External links
Further reading
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-hydroxy-2-methylbutyryl-CoA%20dehydrogenase | In enzymology, a 3-hydroxy-2-methylbutyryl-CoA dehydrogenase () is an enzyme that catalyzes the chemical reaction
(2S,3S)-3-hydroxy-2-methylbutanoyl-CoA + NAD+ 2-methylacetoacetyl-CoA + NADH + H+
Thus, the two substrates of this enzyme are (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA and NAD+, whereas its 3 products are 2-methylacetoacetyl-CoA, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA:NAD+ oxidoreductase. Other names in common use include 2-methyl-3-hydroxybutyryl coenzyme A dehydrogenase, 2-methyl-3-hydroxybutyryl coenzyme A dehydrogenase, and 2-methyl-3-hydroxy-butyryl CoA dehydrogenase. This enzyme participates in valine, leucine and isoleucine degradation.
Structural studies
As of 20 January 2010, 6 structure have been solved for this class of enzymes, with the PDB accession code , , , , , .
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/3-hydroxyacyl-CoA%20dehydrogenase | In enzymology, a 3-hydroxyacyl-CoA dehydrogenase () is an enzyme that catalyzes the chemical reaction
(S)-3-hydroxyacyl-CoA + NAD+ 3-oxoacyl-CoA + NADH + H+
Thus, the two substrates of this enzyme are (S)-3-hydroxyacyl-CoA and NAD+, whereas its 3 products are 3-oxoacyl-CoA, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor.
Isozymes
In humans, the following genes encode proteins with 3-hydroxyacyl-CoA dehydrogenase activity:
HADH – Hydroxyacyl-Coenzyme A dehydrogenase
HSD17B10 – 3-Hydroxyacyl-CoA dehydrogenase type-2
EHHADH – Peroxisomal bifunctional enzyme
HSD17B4 – Peroxisomal multifunctional enzyme type 2
Function
3-Hydroxyacyl CoA dehydrogenase is classified as an oxidoreductase. It is involved in fatty acid metabolic processes. Specifically it catalyzes the third step of beta oxidation; the oxidation of L-3-hydroxyacyl CoA by NAD+. The reaction converts the hydroxyl group into a keto group.
The end product is 3-ketoacyl CoA.
Metabolic pathways
This enzyme participates in 8 metabolic pathways:
fatty acid elongation in mitochondria
fatty acid metabolism
valine, leucine and isoleucine degradation
lysine degradation
tryptophan metabolism
benzoate degradation via coa ligation
butanoate metabolism
caprolactam degradation
Nomenclature
The systematic name of this enzyme class is (S)-3-hydroxyacyl-CoA:NAD+ oxidoreductase. Other names in common use |
https://en.wikipedia.org/wiki/3-hydroxybenzyl-alcohol%20dehydrogenase | In enzymology, a 3-hydroxybenzyl-alcohol dehydrogenase () is an enzyme that catalyzes the chemical reaction
3-hydroxybenzyl alcohol + NADP+ 3-hydroxybenzaldehyde + NADPH + H+
Thus, the two substrates of this enzyme are 3-hydroxybenzyl alcohol and NADP+, whereas its 3 products are 3-hydroxybenzaldehyde, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-hydroxybenzyl-alcohol:NADP+ oxidoreductase. Other names in common use include m-hydroxybenzyl alcohol dehydrogenase, m-hydroxybenzyl alcohol (NADP+) dehydrogenase, and m-hydroxybenzylalcohol dehydrogenase. This enzyme participates in toluene and xylene degradation.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-Hydroxybutyrate%20dehydrogenase | In enzymology, 3-hydroxybutyrate dehydrogenase () is an enzyme that catalyzes the chemical reaction:
(R)-3-hydroxybutanoate + NAD+ acetoacetate + NADH + H+
Thus, the two substrates of this enzyme are (R)-3-hydroxybutanoate and NAD+, whereas its three products are acetoacetate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, to be specific, those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor.
This enzyme participates in the synthesis and degradation of ketone bodies and the metabolism of butyric acid.
Classification
This enzyme has a classification number of EC 1.1.1.30. The first digit means that this enzyme is an oxidoreductase which means the purpose is to catalyze oxidation and reduction reaction pathways. The following two 1s indicate the subclass and sub-sub of the enzyme. In this case, 1.1.1 means this enzyme is an oxidoreductase that acts on the CH-OH group of the donor molecule using NAD(+) or NADP(+) as the acceptor. The 4th number, or 30 in this case, is the serial number of the enzyme to define it within its sub-subclass. 3-Hydroxybutryate dehydrogenase is also known as beta-hydroxybutyric dehydrogenase and is abbreviated BHBDH. Other common synonyms are shown below.
The systematic name of this enzyme class is (R)-3-hydroxybutanoate:NAD+ oxidoreductase. Other names in common use include:
NAD+-β-hydroxybutyrate dehydrogenase
hydroxybutyrate oxidoreductase
β-hydroxybutyrate dehydrogenase
D-β-hydroxybutyrate dehydrogenase
|
https://en.wikipedia.org/wiki/3-Hydroxybutyryl-CoA%20dehydrogenase | In enzymology, a 3-hydroxybutyryl-CoA dehydrogenase () is an enzyme that catalyzes the chemical reaction
(S)-3-hydroxybutanoyl-CoA + NADP+ 3-acetoacetyl-CoA + NADPH + H+
Thus, the two substrates of this enzyme are (S)-3-hydroxybutanoyl-CoA and NADP+; its 3 products are acetoacetyl-CoA, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-3-hydroxybutanoyl-CoA:NADP+ oxidoreductase. Other names in common use include beta-hydroxybutyryl coenzyme A dehydrogenase, L-(+)-3-hydroxybutyryl-CoA dehydrogenase, BHBD, dehydrogenase, L-3-hydroxybutyryl coenzyme A (nicotinamide adenine, dinucleotide phosphate), L-(+)-3-hydroxybutyryl-CoA dehydrogenase, and beta-hydroxybutyryl-CoA dehydrogenase. This enzyme participates in benzoate degradation via coa ligation and butanoate metabolism.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/3-hydroxyisobutyrate%20dehydrogenase | In enzymology, a 3-hydroxyisobutyrate dehydrogenase () also known as β-hydroxyisobutyrate dehydrogenase or 3-hydroxyisobutyrate dehydrogenase, mitochondrial (HIBADH) is an enzyme that in humans is encoded by the HIBADH gene.
3-Hydroxyisobutyrate dehydrogenase catalyzes the chemical reaction:
3-hydroxy-2-methylpropanoate + NAD+ 2-methyl-3-oxopropanoate + NADH + H+
Thus, the two substrates of this enzyme are 3-hydroxy-2-methylpropanoate and NAD+, whereas its 3 products are 2-methyl-3-oxopropanoate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-hydroxy-2-methylpropanoate:NAD+ oxidoreductase. This enzyme participates in valine, leucine and isoleucine degradation.
Function
3-hydroxyisobutyrate dehydrogenase is a tetrameric mitochondrial enzyme that catalyzes the NAD+-dependent, reversible oxidation of 3-hydroxyisobutyrate, an intermediate of valine catabolism, to methylmalonate semialdehyde.
Structural studies
As of late 2007, five structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
References
Further reading
External links
PDBe-KB provides an overview of all the structure information available in the PDB for Human 3-hydroxyisobutyrate dehydrogenase, mitochondrial
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure
Human proteins |
https://en.wikipedia.org/wiki/3-hydroxypimeloyl-CoA%20dehydrogenase | In enzymology, a 3-hydroxypimeloyl-CoA dehydrogenase () is an enzyme that catalyzes the chemical reaction
3-hydroxypimeloyl-CoA + NAD+ 3-oxopimeloyl-CoA + NADH + H+
Thus, the two substrates of this enzyme are 3-hydroxypimeloyl-CoA and NAD+, whereas its 3 products are 3-oxopimeloyl-CoA, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-hydroxypimeloyl-CoA:NAD+ oxidoreductase. This enzyme participates in benzoate degradation via coa ligation.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-hydroxypropionate%20dehydrogenase | In enzymology, a 3-hydroxypropionate dehydrogenase () is an enzyme that catalyzes the chemical reaction
3-hydroxypropanoate + NAD+ 3-oxopropanoate + NADH + H+
Thus, the two substrates of this enzyme are 3-hydroxypropanoate and NAD+, whereas its 3 products are 3-oxopropanoate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-hydroxypropanoate:NAD+ oxidoreductase. This enzyme participates in beta-alanine metabolism and propanoate metabolism.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-Ketosteroid%20reductase | In enzymology, a 3-keto-steroid reductase () is an enzyme that catalyzes the chemical reaction
4alpha-methyl-5alpha-cholest-7-en-3beta-ol + NADP+ 4alpha-methyl-5alpha-cholest-7-en-3-one + NADPH + H+
Thus, the two substrates of this enzyme are 4alpha-methyl-5alpha-cholest-7-en-3beta-ol and NADP+, whereas its 3 products are 4alpha-methyl-5alpha-cholest-7-en-3-one, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3beta-hydroxy-steroid:NADP+ 3-oxidoreductase. This enzyme is also called 3-KSR. This enzyme participates in biosynthesis of steroids.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-methylbutanal%20reductase | In enzymology, a 3-methylbutanal reductase () is an enzyme that catalyzes the chemical reaction
3-methylbutan-1-ol + NAD(P)+ 3-methylbutanal + NAD(P)H + H+
The three substrates of this enzyme are 3-methylbutan-1-ol (isoamyl alcohol), NAD+, and NADP+, whereas its four products are 3-methylbutanal, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-methylbutanol:NAD(P)+ oxidoreductase.
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/5-amino-6-%285-phosphoribosylamino%29uracil%20reductase | In enzymology, a 5-amino-6-(5-phosphoribosylamino)uracil reductase () is an enzyme that catalyzes the chemical reaction
5-amino-6-(5-phosphoribitylamino)uracil + NADP+ 5-amino-6-(5-phosphoribosylamino)uracil + NADPH + H+
Thus, the two substrates of this enzyme are 5-amino-6-(5-phosphoribitylamino)uracil and NADP+, whereas its 3 products are 5-amino-6-(5-phosphoribosylamino)uracil, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 5-amino-6-(5-phosphoribitylamino)uracil:NADP+ 1'-oxidoreductase. This enzyme is also called aminodioxyphosphoribosylaminopyrimidine reductase. This enzyme participates in riboflavin metabolism.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/6-endo-hydroxycineole%20dehydrogenase | In enzymology, a 6-endo-hydroxycineole dehydrogenase () is an enzyme that catalyzes the chemical reaction
6-endo-hydroxycineole + NAD+ 6-oxocineole + NADH + H+
Thus, the two substrates of this enzyme are 6-endo-hydroxycineole and NAD+, whereas its 3 products are 6-oxocineole, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 6-endo-hydroxycineole:NAD+ 6-oxidoreductase. This enzyme participates in terpenoid biosynthesis.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/6-hydroxyhexanoate%20dehydrogenase | In enzymology, a 6-hydroxyhexanoate dehydrogenase () is an enzyme that catalyzes the chemical reaction
6-hydroxyhexanoate + NAD+ 6-oxohexanoate + NADH + H+
Thus, the two substrates of this enzyme are 6-hydroxyhexanoate and NAD+, whereas its 3 products are 6-oxohexanoate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 6-hydroxyhexanoate:NAD+ oxidoreductase. This enzyme participates in caprolactam degradation.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/6-pyruvoyltetrahydropterin%202%27-reductase | In enzymology, a 6-pyruvoyltetrahydropterin 2'-reductase () is an enzyme that catalyzes the chemical reaction
6-lactoyl-5,6,7,8-tetrahydropterin + NADP+ 6-pyruvoyltetrahydropterin + NADPH + H+
Thus, the two substrates of this enzyme are 6-lactoyl-5,6,7,8-tetrahydropterin and NADP+, whereas its 3 products are 6-pyruvoyltetrahydropterin, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 6-lactoyl-5,6,7,8-tetrahydropterin:NADP+ 2'-oxidoreductase. Other names in common use include 6-pyruvoyltetrahydropterin reductase, 6PPH4(2'-oxo) reductase, 6-pyruvoyl tetrahydropterin (2'-oxo)reductase, 6-pyruvoyl-tetrahydropterin 2'-reductase, and pyruvoyl-tetrahydropterin reductase. This enzyme participates in folate biosynthesis.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/7alpha-hydroxysteroid%20dehydrogenase | In enzymology, a 7alpha-hydroxysteroid dehydrogenase () is an enzyme that catalyzes the chemical reaction
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + NAD+ 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + NADH + H+
Thus, the two substrates of this enzyme are 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate and NAD+, whereas its 3 products are 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 7alpha-hydroxysteroid:NAD+ 7-oxidoreductase. Other names in common use include 7alpha-hydroxy steroid dehydrogenase, and 7alpha-HSDH.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/7beta-hydroxysteroid%20dehydrogenase%20%28NADP%2B%29 | {{DISPLAYTITLE:7beta-hydroxysteroid dehydrogenase (NADP+)}}
In enzymology, a 7beta-hydroxysteroid dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
a 7beta-hydroxysteroid + NADP+ a 7-oxosteroid + NADPH + H+
Thus, the two substrates of this enzyme are 7beta-hydroxysteroid and NADP+, whereas its 3 products are 7-oxosteroid, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 7beta-hydroxysteroid:NADP+ 7-oxidoreductase. Other names in common use include NADP+-dependent 7beta-hydroxysteroid dehydrogenase, and 7beta-hydroxysteroid dehydrogenase (NADP+).
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/8-oxocoformycin%20reductase | In enzymology, a 8-oxocoformycin reductase () is an enzyme that catalyzes the chemical reaction
coformycin + NADP+ 8-oxocoformycin + NADPH + H+
Thus, the two substrates of this enzyme are coformycin and NADP+, whereas its 3 products are 8-oxocoformycin, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is coformycin:NADP+ 8-oxidoreductase. This enzyme is also called 8-ketodeoxycoformycin reductase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28-%29-borneol%20dehydrogenase | In enzymology, a (−)-borneol dehydrogenase () is an enzyme that catalyzes the chemical reaction
(−)-borneol + NAD (−)-camphor + NADH + H
Thus, the two substrates of this enzyme are (−)-borneol and NAD, whereas its 3 products are (−)-camphor, NADH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (−)-borneol:NAD oxidoreductase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28%2B%29-borneol%20dehydrogenase | In enzymology, a (+)-borneol dehydrogenase () is an enzyme that increases the rate of, or catalyzes, the chemical reaction
(+)-borneol + NAD (+)-camphor + NADH + H
Thus, the two substrates of this enzyme are (+)-borneol and NAD, whereas its 3 products are (+)-camphor, NADH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (+)-borneol:NAD oxidoreductase. This enzyme is also called bicyclic monoterpenol dehydrogenase.
References
External links
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28-%29-menthol%20dehydrogenase | A (−)-menthol dehydrogenase () is an enzyme that catalyzes the chemical reaction
(−)-menthol + NADP (−)-menthone + NADPH + H,
i.e., catalyses the breakdown of menthol. Thus, the two substrates of this enzyme are (−)-menthol and NADP, whereas its 3 products are (−)-menthone, NADPH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (−)-menthol:NADP oxidoreductase. This enzyme is also called monoterpenoid dehydrogenase. This enzyme participates in monoterpenoid biosynthesis.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28%2B%29-neomenthol%20dehydrogenase | In enzymology, a (+)-neomenthol dehydrogenase () is an enzyme that catalyzes the chemical reaction
(+)-neomenthol + NADP (−)-menthone + NADPH + H
Thus, the two substrates of this enzyme are (+)-neomenthol and NADP, whereas its 3 products are (−)-menthone, NADPH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (+)-neomenthol:NADP oxidoreductase. This enzyme is also called monoterpenoid dehydrogenase. This enzyme participates in monoterpenoid biosynthesis.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28R%29-2-hydroxyacid%20dehydrogenase | In enzymology, a (R)-2-hydroxyacid dehydrogenase () is an enzyme that catalyzes the chemical reaction
(2R)-3-sulfolactate + NAD(P) 3-sulfopyruvate + NAD(P)H + H
The 3 substrates of this enzyme are (2R)-3-sulfolactic acid, NAD, and NADP, whereas its 4 products are 3-sulfopyruvic acid, NADH, NADPH, and H. This enzyme is important in the metabolism of archaea, particularly their biosynthesis of coenzymes such as coenzyme M, tetrahydromethanopterin and methanofuran.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (R)-2-hydroxyacid:NAD(P) oxidoreductase. Other names in common use include (R)-sulfolactate:NAD(P) oxidoreductase, L-sulfolactate dehydrogenase, ComC, and (R)-sulfolactate dehydrogenase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/%28R%29-2-hydroxy-fatty-acid%20dehydrogenase | In enzymology, a (R)-2-hydroxy-fatty-acid dehydrogenase () is an enzyme that catalyzes the chemical reaction
(R)-2-hydroxystearate + NAD 2-oxostearate + NADH + H
Thus, the two substrates of this enzyme are (R)-2-hydroxystearate and NAD, whereas its 3 products are 2-oxostearate, NADH, and H. This reaction is important in fatty acid metabolism.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (R)-2-hydroxystearate:NAD oxidoreductase. Other names in common use include D-2-hydroxy fatty acid dehydrogenase, and 2-hydroxy fatty acid oxidase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28R%29-3-hydroxyacid-ester%20dehydrogenase | In enzymology, a (R)-3-hydroxyacid-ester dehydrogenase () is an enzyme that catalyzes the chemical reaction
ethyl (R)-3-hydroxyhexanoate + NADP ethyl 3-oxohexanoate + NADPH + H
Thus, the two substrates of this enzyme are ethyl (R)-3-hydroxyhexanoate and NADP, whereas its 3 products are ethyl 3-oxohexanoate, NADPH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is ethyl-(R)-3-hydroxyhexanoate:NADP 3-oxidoreductase. This enzyme is also called 3-oxo ester (R)-reductase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28R%29-4-hydroxyphenyllactate%20dehydrogenase | (R)-4-hydroxyphenyllactate dehydrogenase () is an enzyme that catalyzes a chemical reaction
(R)-3-(4-hydroxyphenyl)lactate + NAD(P)+ 3-(4-hydroxyphenyl)pyruvate + NAD(P)H + H
The 3 substrates of this enzyme are (R)-3-(4-hydroxyphenyl)lactate, NAD, and NADP, whereas its 4 products are 3-(4-hydroxyphenyl)pyruvate, NADH, NADPH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (R)-3-(4-hydroxyphenyl)lactate:NAD(P) 2-oxidoreductase. Other names in common use include (R)-aromatic lactate dehydrogenase, and D-hydrogenase, D-aryllactate. This enzyme participates in tyrosine and phenylalanine catabolism.
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28R%29-aminopropanol%20dehydrogenase | In enzymology, a (R)-aminopropanol dehydrogenase () is an enzyme that catalyzes the chemical reaction
(R)-1-aminopropan-2-ol + NAD aminoacetone + NADH + H
Thus, the two substrates of this enzyme are (R)-1-aminopropan-2-ol and NAD, whereas its 3 products are aminoacetone, NADH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (R)-1-aminopropan-2-ol:NAD oxidoreductase. Other names in common use include L-aminopropanol dehydrogenase, 1-aminopropan-2-ol-NAD dehydrogenase, L()-1-aminopropan-2-ol:NAD oxidoreductase, 1-aminopropan-2-ol-dehydrogenase, DL-1-aminopropan-2-ol: NAD dehydrogenase, and L()-1-aminopropan-2-ol-NAD/NADP oxidoreductase. This enzyme participates in glycine, serine and threonine metabolism. It requires potassium as a cofactor.
References
EC 1.1.1
NADH-dependent enzymes
Potassium enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-%28imidazol-5-yl%29lactate%20dehydrogenase | In enzymology, a 3-(imidazol-5-yl)lactate dehydrogenase () is an enzyme that catalyzes the chemical reaction
(S)-3-(imidazol-5-yl)lactate + NAD(P)+ 3-(imidazol-5-yl)pyruvate + NAD(P)H + H+
The 3 substrates of this enzyme are (S)-3-(imidazol-5-yl)lactate, NAD+, and NADP+, whereas its 4 products are 3-(imidazol-5-yl)pyruvate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-3-(imidazol-5-yl)lactate:NAD(P)+ oxidoreductase. This enzyme is also called imidazol-5-yl lactate dehydrogenase.
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28S%29-2-hydroxy-fatty-acid%20dehydrogenase | In enzymology, a (S)-2-hydroxy-fatty-acid dehydrogenase () is an enzyme that catalyzes the chemical reaction
(S)-2-hydroxystearate + NAD 2-oxostearate + NADH + H
Thus, the two substrates of this enzyme are (S)-2-hydroxystearate and NAD, whereas its 3 products are 2-oxostearate, NADH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (S)-2-hydroxystearate:NAD oxidoreductase. Other names in common use include dehydrogenase, L-2-hydroxy fatty acid, L-2-hydroxy fatty acid dehydrogenase, and 2-hydroxy fatty acid oxidase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28S%29-3-hydroxyacid-ester%20dehydrogenase | In enzymology, a (S)-3-hydroxyacid-ester dehydrogenase () is an enzyme that catalyzes the chemical reaction
ethyl (S)-3-hydroxyhexanoate + NADP ethyl 3-oxohexanoate + NADPH + H
Thus, the two substrates of this enzyme are ethyl (S)-3-hydroxyhexanoate and NADP, whereas its 3 products are ethyl 3-oxohexanoate, NADPH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is ethyl-(S)-3-hydroxyhexanoate:NADP 3-oxidoreductase. This enzyme is also called 3-oxo ester (S)-reductase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
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