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Surprise! A hidden B12 cofactor catalyzes a radical methylation
- Source :
- Journal of Biological Chemistry. 294:11726-11727
- Publication Year :
- 2019
- Publisher :
- Elsevier BV, 2019.
-
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.
- Subjects :
- 0301 basic medicine
chemistry.chemical_classification
030102 biochemistry & molecular biology
biology
Stereochemistry
Cell Biology
Methylation
Biochemistry
Cobalamin
Cofactor
03 medical and health sciences
chemistry.chemical_compound
030104 developmental biology
Enzyme
Sequence homology
chemistry
Methylcobalamin
biology.protein
Protein methylation
medicine
Molecular Biology
Radical SAM
medicine.drug
Subjects
Details
- ISSN :
- 00219258
- Volume :
- 294
- Database :
- OpenAIRE
- Journal :
- Journal of Biological Chemistry
- Accession number :
- edsair.doi...........58a3d5bf5c18223226fa51b5e76c8d81