Betaine reductase (EC 1.21.4.4) is an enzyme that catalyzes the chemical reaction

Betaine reductase
Identifiers
EC no.1.21.4.4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
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NCBIproteins
acetyl phosphate + trimethylamine + thioredoxin disulfide 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).

References

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  • Andreesen JR; Sonntag, D; Grimm, R; Pich, A; Eckerskorn, C; Söhling, B; Andreesen, JR (1999). "Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum. Biochemical and molecular analysis". Eur. J. Biochem. 260 (1): 38–49. doi:10.1046/j.1432-1327.1999.00107.x. PMID 10091582.
  • 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 (12): 3538–44. doi:10.1046/j.1432-1327.2001.02257.x. PMID 11422384.