title: Coenzyme B(12) dependent glutamate mutase.
abstract: The crystal structure of glutamate mutase with bound coenzyme B(12) suggests a radical shuttling mechanism within the active site of the enzyme. Quantum chemical calculations of the rearrangement in combination with kinetic and mutational studies suggest the catalytic mechanism of this enzyme to proceed via a fragmentation/recombination sequence with intermediates stabilized by partial protonation/deprotonation. Crucial residues in the active site have been identified. Solution structure studies indicate the mechanism of B(12) binding to the apoenzyme.
authors.affiliation: Institut für Chemie, Universität Graz, Heinrichstrasse 28, Austria. karl.gruber@uni-graz.at
authors.forename: Karl
authors.initials: K
authors.lastname: Gruber
authors.forename: Christoph
authors.initials: C
authors.lastname: Kratky
mesh_terms: D001665:Binding Sites; D003013:Clostridium / Q000201:enzymology; D003038:Cobamides / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D005609:Free Radicals / Q000737:chemistry; D019751:Intramolecular Transferases / Q000737:chemistry* / Q000378:metabolism; D007700:Kinetics; D008956:Models, Chemical; D008958:Models, Molecular; D009154:Mutation; D011522:Protons; D011789:Quantum Theory; D012996:Solutions
chemical_list: D003038:Cobamides; D005609:Free Radicals; D011522:Protons; D012996:Solutions; D019751:Intramolecular Transferases; C021570:methylaspartate mutase