Cystine reductase

Cystine reductase
Identifiers
EC no.1.8.1.6
CAS no.9029-18-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Cystine reductase (EC 1.8.1.6) is an enzyme that catalyzes the chemical reaction

 
 
H+
 
H+
 
 
2
 
+ NAD+
 

The three substrates of this enzyme are L-cystine, reduced nicotinamide adenine dinucleotide (NADH) and a proton. Its products are L-cysteine and oxidised NAD+.[1][2][3][4]

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 L-cysteine:NAD+ oxidoreductase. Other names in common use include cystine reductase (NADH), NADH-dependent cystine reductase, cystine reductase (NADH2), and NADH2:L-cystine oxidoreductase. This enzyme participates in cysteine metabolism.

References

  1. ^ Enzyme 1.8.1.6 at KEGG Pathway Database.
  2. ^ Romano AH, Nickerson WJ (1954). "Cystine reductase of pea seeds and yeasts". J. Biol. Chem. 208 (1): 409–16. doi:10.1016/S0021-9258(18)65659-5. PMID 13174550.
  3. ^ Carroll JE, Kosicki GW, Thibert RJ (1970). "Alpha-substituted cystines as possible substrates for cystine reductase and L-amino acid oxidase". Biochim. Biophys. Acta. 198 (3): 601–3. doi:10.1016/0005-2744(70)90137-3. PMID 5436160.
  4. ^ Maresca B, Jacobson E, Medoff G, Kobayashi G (1978). "Cystine reductase in the dimorphic fungus Histoplasma capsulatum". J. Bacteriol. 135 (3): 987–92. doi:10.1128/jb.135.3.987-992.1978. PMC 222474. PMID 211119.