Sarcosine reductase | |||||||||
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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 | ||||||||
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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 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.
Other oxidoreductases (EC 1.15–1.21) | |
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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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Activity | |
Regulation | |
Classification | |
Kinetics | |
Types |
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