Sarcosine reductase
From Wikipedia, the free encyclopedia
In enzymology, a sarcosine reductase (EC 1.21.4.3) is an enzyme that catalyzes the chemical reaction
- acetyl phosphate + methylamine + thioredoxin disulfide N-methylglycine + phosphate + thioredoxin
The 3 substrates of this enzyme are acetyl phosphate, methylamine, and thioredoxin disulfide, whereas its 3 products are N-methylglycine, phosphate, and thioredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on X-H and Y-H to form an X-Y bond with a disulfide as acceptor. The systematic name of this enzyme class is acetyl-phosphate methylamine:thioredoxin disulfide oxidoreductase (N-methylglycine-forming).
[edit] References
- IUBMB entry for 1.21.4.3
- BRENDA references for 1.21.4.3 (Recommended.)
- PubMed references for 1.21.4.3
- PubMed Central references for 1.21.4.3
- Google Scholar references for 1.21.4.3
- Andreesen JR (1999). "Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum. Biochemical and molecular analysis". Eur. J. Biochem. 260: 38–49. doi: . PMID 10091582.
- Hormann K and Andreesen JR (1989). "Reductive cleavage of sarcosine and betaine by Eubacterium acidaminophilum via enzyme systems different from glycine reductase". Arch. Microbiol. 153: 50–59. doi: .