Sarcosine reductase

Sarcosine reductase
Identifiers
EC no.	1.21.4.3
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Search PMC articles PubMed articles NCBI proteins

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

• Wagner M, Sonntag D, Grimm R, Pich A, Eckerskorn C, Söhling B, Andreesen JR (February 1999). "Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum. Biochemical and molecular analysis". European Journal of Biochemistry. 260 (1): 38–49. doi:10.1046/j.1432-1327.1999.00107.x. PMID 10091582.
• Hormann K, Andreesen JR (1989). "Reductive cleavage of sarcosine and betaine by Eubacterium acidaminophilum via enzyme systems different from glycine reductase". Archives of Microbiology. 153: 50–59. doi:10.1007/BF00277541.