CoA-disulfide reductase

Last updated
CoA-disulfide reductase
Identifiers
EC no. 1.8.1.14
CAS no. 206770-55-0
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

In enzymology, a CoA-disulfide reductase (EC 1.8.1.14) is an enzyme that catalyzes the chemical reaction

2 CoA + NAD(P)+ CoA-disulfide + NAD(P)H + H+

The 3 substrates of this enzyme are CoA, NAD+, and NADP+, whereas its 4 products are CoA-disulfide, NADH, NADPH, and H+.

This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is CoA:NAD(P)+ oxidoreductase. Other names in common use include CoA-disulfide reductase (NADH2), NADH2:CoA-disulfide oxidoreductase, CoA:NAD+ oxidoreductase, CoADR, and coenzyme A disulfide reductase.

Related Research Articles

<span class="mw-page-title-main">Nicotinamide adenine dinucleotide</span> Chemical compound which is reduced and oxidized

Nicotinamide adenine dinucleotide (NAD) is a coenzyme central to metabolism. Found in all living cells, NAD is called a dinucleotide because it consists of two nucleotides joined through their phosphate groups. One nucleotide contains an adenine nucleobase and the other, nicotinamide. NAD exists in two forms: an oxidized and reduced form, abbreviated as NAD+ and NADH (H for hydrogen), respectively.

<span class="mw-page-title-main">L-xylulose reductase</span> Enzyme

Dicarbonyl/L-xylulose reductase, also known as carbonyl reductase II, is an enzyme that in human is encoded by the DCXR gene located on chromosome 17.

<span class="mw-page-title-main">Hydroxymethylglutaryl-CoA reductase (NADPH)</span>

In enzymology, a hydroxymethylglutaryl-CoA reductase (NADPH) (EC 1.1.1.34) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">3-hydroxyacyl-CoA dehydrogenase</span> Enzyme

In enzymology, a 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Acyl-CoA dehydrogenase (NADP+)</span> Class of enzymes

In enzymology, an acyl-CoA dehydrogenase (NADP+) (EC 1.3.1.8) is an enzyme that catalyzes the chemical reaction

In enzymology, an anthraniloyl-CoA monooxygenase (EC 1.14.13.40) is an enzyme that catalyzes the chemical reaction

In enzymology, a hexadecanal dehydrogenase (acylating) (EC 1.2.1.42) is an enzyme that catalyzes the chemical reaction

Arsenate reductase (glutaredoxin) (EC 1.20.4.1) is an enzyme that catalyzes the chemical reaction

In enzymology, a ferric-chelate reductase (EC 1.16.1.7) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">(Methionine synthase) reductase</span> Class of enzymes

[Methionine synthase] reductase, or Methionine synthase reductase, encoded by the gene MTRR, is an enzyme that is responsible for the reduction of methionine synthase inside human body. This enzyme is crucial for maintaining the one carbon metabolism, specifically the folate cycle. The enzyme employs one coenzyme, flavoprotein.

In enzymology, a CoA-glutathione reductase (EC 1.8.1.10) is an enzyme that catalyzes the chemical reaction

In enzymology, a cystine reductase (EC 1.8.1.6) is an enzyme that catalyzes the chemical reaction

In enzymology, an FMN reductase (EC 1.5.1.29) is an enzyme that catalyzes the chemical reaction

In enzymology, a hydroxylamine reductase (NADH) (EC 1.7.1.10) is an enzyme that catalyzes the chemical reaction.

In enzymology, a mycothione reductase (EC 1.8.1.15) is an enzyme that catalyzes the chemical reaction

In enzymology, a peptide-methionine (R)-S-oxide reductase (EC 1.8.4.12) is an enzyme that catalyzes the chemical reaction

In enzymology, a protein-disulfide reductase (EC 1.8.1.8) is an enzyme that catalyzes the chemical reaction

In enzymology, a trypanothione-disulfide reductase (EC 1.8.1.12) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">NADH:ubiquinone reductase (non-electrogenic)</span> Class of enzymes

NADH:ubiquinone reductase (non-electrogenic) (EC 1.6.5.9, NDH-2, ubiquinone reductase, coenzyme Q reductase, dihydronicotinamide adenine dinucleotide-coenzyme Q reductase, DPNH-coenzyme Q reductase, DPNH-ubiquinone reductase, NADH-coenzyme Q oxidoreductase, NADH-coenzyme Q reductase, NADH-CoQ oxidoreductase, NADH-CoQ reductase) is an enzyme with systematic name NADH:ubiquinone oxidoreductase. This enzyme catalyses the following chemical reaction:

Peptide-methionine (S)-S-oxide reductase (EC 1.8.4.11, MsrA, methionine sulphoxide reductase A, methionine S-oxide reductase (S-form oxidizing), methionine sulfoxide reductase A, peptide methionine sulfoxide reductase, formerly protein-methionine-S-oxide reductase) is an enzyme with systematic name peptide-L-methionine:thioredoxin-disulfide S-oxidoreductase (L-methionine (S)-S-oxide-forming). This enzyme catalyses the following chemical reaction

References