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EC Number General Information Commentary Reference
Display the reaction diagram Show all sequences 2.1.1.281evolution enzyme MppJ is structurally related to the MT protein family -, 735362
Display the reaction diagram Show all sequences 2.1.1.281more 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 -, 735362
Display the reaction diagram Show all sequences 2.1.1.281physiological 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) 755790
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