EC Number   |
Substrates |
Products |
Reversibility |
|---|
  2.1.1.281 | more |
the enzyme has no nonheme oxygenase activity |
? |
- |
? |
| 2.1.1.281 | more |
aside from its physiological substrate 4-methyl-2-oxovalerate, enzyme SgvM catalyzes the (di)methylation of pyruvate, 2-oxobutyrate, 2-oxovalerate, and phenylpyruvate at the beta-carbon atom. SgvM acts stereoselectively. SgvM also catalyzes stereoselective ethylation reactions with S-adenosylethionine as the electrophile. The methylation of 2-oxovalerate occurs with R selectivity while the ethylation of 2-oxobutyrate with S-adenosylethionine results in the S enantiomer of 3-methyl-2-oxovalerate. Product analysis by 13C NMR spectroscopy |
? |
- |
- |
| 2.1.1.281 | S-adenosyl-L-ethionine + 2-oxobutyrate |
- |
S-adenosyl-L-homocysteine + (3S)-methyl-2-oxovalerate |
- |
? |
| 2.1.1.281 | S-adenosyl-L-methionine + 2-oxo-3-phenylpropanoate |
the enzyme is involved in synthesis of the nonproteinogenic amino acid (2S,3S)-beta-methyl-phenylalanine, a building block of the glycopeptide antibiotic mannopeptimycin |
S-adenosyl-L-homocysteine + (3S)-2-oxo-3-methyl-3-phenylpropanoate |
- |
? |
| 2.1.1.281 | S-adenosyl-L-methionine + 2-oxo-3-phenylpropanoate |
2-oxo-3-phenylpropanoate i.e. 3-phenylpyruvate. S-Adenosyl-L-methionine has higher binding affinity for the enzyme than 2-oxo-3-phenylpropanoate, and the C-C bond formation in (3S)-2-oxo-3-methyl-3-phenylpropanoate might be the rate-limiting step, as opposed to the C-S bond breakage in S-adenosyl-L-methionine. No enzyme activity on glutamic acid, cinnamic acid, phenyl acetic acid and benzoyl acetic acid. The alpha-keto and beta-phenyl functional groups are crucial in MppJ molecular recognition. The enzyme strictly transfers a methyl group from S-adenosyl-L-methionine the beta position of 2-oxo-3-phenylpropanoate |
S-adenosyl-L-homocysteine + (3S)-2-oxo-3-methyl-3-phenylpropanoate |
(3S)-2-oxo-3-methyl-3-phenylpropanoate i.e. (3S)-beta-methyl-phenylpyruvate |
? |
| 2.1.1.281 | S-adenosyl-L-methionine + 2-oxobutyrate |
- |
S-adenosyl-L-homocysteine + 3-methyl-2-oxobutyrate |
- |
? |
| 2.1.1.281 | S-adenosyl-L-methionine + 2-oxovalerate |
- |
S-adenosyl-L-homocysteine + (3R)-methyl-2-oxovalerate |
- |
? |
| 2.1.1.281 | S-adenosyl-L-methionine + 3-phenylpyruvate |
phenylpyruvate binding structure analysis |
S-adenosyl-L-homocysteine + (3R)-2-oxo-3-phenylbutanoate |
- |
? |
| 2.1.1.281 | S-adenosyl-L-methionine + 3-phenylpyruvate |
Arg127 is electrostatically associated with phenylpyruvate, binding structure analysis, enzyme MppJ is an R-configuration-specific methyltransferase, ratios of 5:1 and 1:1 for (2S,3R)-betaMePhe versus (2S,3S)-betaMePhe |
S-adenosyl-L-homocysteine + (3R)-2-oxo-3-phenylbutanoate |
- |
? |
| 2.1.1.281 | S-adenosyl-L-methionine + 3-phenylpyruvate |
- |
S-adenosyl-L-homocysteine + (3S)-2-oxo-3-phenylbutanoate |
- |
? |
