2.1.1.281: phenylpyruvate C3-methyltransferase
This is an abbreviated version!
For detailed information about phenylpyruvate C3-methyltransferase, go to the full flat file.
Reaction
Synonyms
C-MT, ELQ87_35210, MppJ, MT SgvM, phenylpyruvate Cbeta-methyltransferase, phenylpyruvate methyltransferase, S-adenosylmethionine-dependent methyltransferase, SgvM
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General Information
General Information on EC 2.1.1.281 - phenylpyruvate C3-methyltransferase
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evolution
physiological function
S-adenosylmethionine-dependent methyltransferases (MTs) play a decisive role in the biosynthesis of natural products and in epigenetic processes. MTs catalyze the methylation of heteroatoms and even of carbon atoms, which, in many cases, is a challenging reaction in conventional synthesis. C-MTs are often highly substrate-specific. SgvM from Streptomyces griseoviridis features an extended substrate scope with respect to the nucleophile as well as the electrophile. It catalyze the transfer of the electrophilic methyl group of SAM to the C3 position of 4-methyl-2-oxovalerate (alpha-ketoleucine)
additional information
enzyme MppJ is structurally related to the MT protein family
evolution
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enzyme MppJ is structurally related to the MT protein family
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the enzyme is composed of two domains: a dimerization domain (DD) and a methyltransfer domain (MT). The substrate-binding pocket is situated at the occlusion of the DD and MT domains, in which the iron centre is solvent-accessible
additional information
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the enzyme is composed of two domains: a dimerization domain (DD) and a methyltransfer domain (MT). The substrate-binding pocket is situated at the occlusion of the DD and MT domains, in which the iron centre is solvent-accessible
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