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Front Cover: Structures in Tetrahydrofolate Methylation in Desulfitobacterial Glycine Betaine Metabolism at Atomic Resolution (ChemBioChem 6/2020)
Author(s) -
Badmann Thomas,
Groll Michael
Publication year - 2020
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.202000086
Subject(s) - chemistry , betaine , methylation , moiety , methylcobalamin , glycine cleavage system , stereochemistry , glycine , cobalamin , enzyme , biochemistry , vitamin b12 , amino acid , dna
Enzymes that orchestrate methylation between tetrahydrofolate (THF) and cobalamin are abundant among all domains of life. During the energy‐producing catabolism of glycine betaine in Desulfitobacterium hafniense , MtgA catalyzes methyl transfer from methylcobalamin to THF. Atomic insights into the substrate–enzyme interactions of MtgA and THF as well as analysis of a trapped (THF‐CH 3 ) + reaction intermediate in sp 3 hybridization reveal a unique binding mode for the THF glutamyl‐ p ‐aminobenzoate moiety during methyl transfer. More information can be found in the communication by M. Groll and T. Badmann on page 776 in Issue 6, 2020 (DOI: 10.1002/cbic.201900515).