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Sarcosine reductase

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Sarcosine reductase
Identifiers
EC no.1.21.4.3
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IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
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In enzymology, a sarcosine reductase (EC 1.21.4.3) is an enzyme that catalyzes the chemical reaction

acetyl phosphate + methylamine + thioredoxin disulfide {\displaystyle \rightleftharpoons } 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 oxydoreductases, 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 methilamine:thioredoxin disulfide oxydoreductase (M-methylglycine-forming).

References

Further reading

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
Enzymes
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