CoA-glutathione reductase

CoA-glutathione reductase
Identifiers
EC number	1.8.1.10
CAS number	37256-33-0
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 / EGO
Search PMC articles PubMed articles

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

CoA + glutathione + NADP⁺ $\rightleftharpoons$ CoA-glutathione + NADPH + H⁺

The 3 substrates of this enzyme are CoA, glutathione, and NADP⁺, whereas its 3 products are CoA-glutathione, 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 glutathione:NADP+ oxidoreductase (CoA-acylating). Other names in common use include coenzyme A glutathione disulfide reductase, NADPH-dependent coenzyme A-SS-glutathione reductase, coenzyme A disulfide-glutathione reductase, and NADPH:CoA-glutathione oxidoreductase. This enzyme participates in cysteine metabolism. It employs one cofactor, FAD.

References

• Ondarza RN, Abney R, Lopez-Colome AM (1969). "Characterization of a NADPH-dependent coenzyme A-SS-glutathione reductase from yeast". Biochim. Biophys. Acta. 191 (2): 239–48. PMID 4390951. 
• Ondarza RN, Escamilla E, Gutierrez J, De la Chica G (1974). "CoAS-Sglutathione and GSSG reductases from rat liver. Two disulfide oxidoreductase activities in one protein entity". Biochim. Biophys. Acta. 341 (1): 162–71. PMID 4151341. 
• Carlberg I, Mannervik B (1977). "Purification by affinity chromatography of yeast glutathione reductase, the enzyme responsible for the NADPH-dependent reduction of the mixed disulfide of coenzyme A and glutathione". Biochim. Biophys. Acta. 484 (2): 268–74. PMID 334266. 

This EC 1.8 enzyme-related article is a stub. You can help Wikipedia by expanding it.v · Categories: Oxidoreductase stubs EC 1.8.1 NADPH-dependent enzymes Flavin enzymes Enzymes of unknown structure Wikimedia Foundation. 2010. Игры ⚽ Нужно решить контрольную? Forked Run State Park Quentin Greenough Look at other dictionaries: Propionyl-CoA carboxylase — PCCA redirects here. For other uses, see PCCA (disambiguation). Propionyl CoA carboxylase Identifiers EC number 6.4.1.3 CAS number …   Wikipedia Methylmalonyl-CoA mutase — Rendering based on PDB 2XIJ …   Wikipedia Methylcrotonyl-CoA carboxylase — methylcrotonoyl Coenzyme A carboxylase 1 (alpha) Identifiers Symbol MCCC1 Entrez 56922 HUGO …   Wikipedia Methylmalonyl CoA epimerase — Ribbon diagram of methylmalonyl CoA epimerase from Propionibacterium shermanii. From PDB 1JC5 …   Wikipedia Methylglutaconyl-CoA hydratase — AU RNA binding protein/enoyl Coenzyme A hydratase Identifiers Symbol AUH Entrez 549 HUGO …   Wikipedia List of EC numbers (EC 1) — This list contains a list of EC numbers for the first group, EC 1, oxidoreducatases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology.EC 1.1 Acting on the CH OH …   Wikipedia Oxidoreductase — In biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule (the reductant, also called the hydrogen or electron donor) to another (the oxidant, also called the hydrogen or electron acceptor). This… …   Wikipedia List of enzymes — This article is a list of enzymes, sorted by their respective sub categories and EC number.See also: * List of EC numbers * List of EC numbers (EC 1) * List of EC numbers (EC 2) * List of EC numbers (EC 3) * List of EC numbers (EC 4) * List of EC …   Wikipedia Dihydrolipoamide dehydrogenase — PDB rendering based on 1zy8 …   Wikipedia Riboflavin — Riboflavin …   Wikipedia 18+ © Academic, 2000-2025 Contact us: Technical Support, Advertising Dictionaries export, created on PHP, Joomla, Drupal, WordPress, MODx. Mark and share Search through all dictionaries Translate… Search Internet Share the article and excerpts Direct link … Do a right-click on the link above and select “Copy Link”