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Betaine reductase

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Enzyme
Betaine reductase
Identifiers
EC no.1.21.4.4
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BRENDABRENDA entry
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MetaCycmetabolic pathway
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Betaine reductase (EC 1.21.4.4) is an enzyme that catalyzes the chemical reaction

acetyl phosphate + trimethylamine + thioredoxin disulfide {\displaystyle \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).

References

Other oxidoreductases (EC 1.15–1.21)
1.15: Acting on superoxide as acceptor
1.16: Oxidizing metal ions
1.17: Acting on CH or CH2 groups
1.18: Acting on iron–sulfur proteins as donors
1.19: Acting on reduced flavodoxin as donor
1.20: Acting on phosphorus or arsenic in donors
1.21: Acting on X-H and Y-H to form an X-Y bond
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