Betaine reductase explained
| Betaine reductase |
| Ec Number: | 1.21.4.4 |
Betaine reductase is an enzyme that catalyzes the chemical reaction
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
- Andreesen JR . 1999 . Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum. Biochemical and molecular analysis . Eur. J. Biochem. . 260 . 38 - 49 . 10091582 . 10.1046/j.1432-1327.1999.00107.x . Sonntag . D . Grimm . R . Pich . A . Eckerskorn . C . Söhling . B . Andreesen . JR . 1 .
- 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 . 11422384 . 10.1046/j.1432-1327.2001.02257.x . 12 . free .
