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- W2964754151 abstract "Radical S-adenosylmethionine (SAM) (RS) methylases perform methylation reactions at unactivated carbon and phosphorus atoms. RS enzymes typically abstract a hydrogen from their substrates, generating a substrate-centered radical; class B RS methylases catalyze methyl transfer from SAM to cobalamin and then to a substrate-centered carbon or phosphorus radical. Radle et al. now show that Mmp10, an RS enzyme implicated in the methylation of Arg-285 in methyl coenzyme M reductase, binds a methylcobalamin cofactor required for methyl transfer from SAM to a peptide substrate. However, Mmp10 has little sequence homology to known methylases, suggesting this enzyme belongs to a new subclass of B12-dependent RS methylases." @default.
- W2964754151 created "2019-08-13" @default.
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- W2964754151 date "2019-08-01" @default.
- W2964754151 modified "2023-10-16" @default.
- W2964754151 title "Surprise! A hidden B12 cofactor catalyzes a radical methylation" @default.
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- W2964754151 doi "https://doi.org/10.1074/jbc.h119.009976" @default.
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