The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

EC 2.1.1.281     
Accepted name: phenylpyruvate C3-methyltransferase
Reaction: S-adenosyl-L-methionine + 3-phenylpyruvate = S-adenosyl-L-homocysteine + (3S)-2-oxo-3-phenylbutanoate
Glossary: 3-phenylpyruvate = 2-oxo-3-phenylpropanoate
(3S)-2-oxo-3-phenylbutanoate = (3S)-β-methyl-phenylpyruvate
Other name(s): phenylpyruvate Cβ-methyltransferase; phenylpyruvate methyltransferase; mppJ (gene name)
Systematic name: S-adenosyl-L-methionine:2-oxo-3-phenylpropanoate C3-methyltransferase
Comments: The enzyme from the bacterium Streptomyces hygroscopicus NRRL3085 is involved in synthesis of the nonproteinogenic amino acid (2S,3S)-β-methyl-phenylalanine, a building block of the antibiotic mannopeptimycin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Huang, Y.T., Lyu, S.Y., Chuang, P.H., Hsu, N.S., Li, Y.S., Chan, H.C., Huang, C.J., Liu, Y.C., Wu, C.J., Yang, W.B. and Li, T.L. In vitro characterization of enzymes involved in the synthesis of nonproteinogenic residue (2S,3S)-β-methylphenylalanine in glycopeptide antibiotic mannopeptimycin. Chembiochem 10 (2009) 2480–2487. [PMID: 19731276]
[EC 2.1.1.281 created 2013]
 
 


Data © 2001–2017 IUBMB
Web site © 2005–2017 Andrew McDonald