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2.1.1.281
evolution
enzyme MppJ is structurally related to the MT protein family
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,
735362
2.1.1.281
more
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
2.1.1.281
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)
755790
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