Betaine reductase

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In enzymology, a betaine reductase (EC 1.21.4.4) is an enzyme that catalyzes the chemical reaction

acetyl phosphate + trimethylamine + thioredoxin disulfide $\rightleftharpoons$ N,N,N-trimethylglycine + phosphate + thioredoxin

The 3 substrates of this enzyme are acetyl phosphate, trimethylamine, and thioredoxin disulfide, whereas its 3 products are N,N,N-trimethylglycine, 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 trimethylamine:thioredoxin disulfide oxidoreductase (N,N,N-trimethylglycine-forming).

[edit] References

IUBMB entry for 1.21.4.4
BRENDA references for 1.21.4.4 (Recommended.)
PubMed references for 1.21.4.4
PubMed Central references for 1.21.4.4
Google Scholar references for 1.21.4.4
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Bednarski B, Andreesen JR, Pich A (2001). "In vitro processing of the proproteins GrdE of protein B of glycine reductase and PrdA of D-proline reductase from Clostridium sticklandii: formation of a pyruvoyl group from a cysteine residue". Eur. J. Biochem. 268: 3538–44. doi:10.1046/j.1432-1327.2001.02257.x. PMID 11422384.