Sarcosine_reductase

Sarcosine reductase

Sarcosine reductase

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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
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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.


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