A new mode of B12 binding and the direct participation of a potassium ion in enzyme catalysis: X-ray structure of diol dehydratase
Open Access
- 1 August 1999
- Vol. 7 (8) , 997-1008
- https://doi.org/10.1016/s0969-2126(99)80126-9
Abstract
No abstract availableKeywords
This publication has 38 references indexed in Scilit:
- Dioldehydratase Binds Coenzyme B12 in the “Base-On” Mode: ESR Investigations on Cob(II)alaminAngewandte Chemie International Edition in English, 1998
- Refinement of Macromolecular Structures by the Maximum-Likelihood MethodActa Crystallographica Section D-Biological Crystallography, 1997
- Glutamate and 2-methyleneglutarate mutase: from microbial curiosities to paradigms for coenzyme B12-dependent enzymesChemical Society Reviews, 1996
- Coordination of a histidine residue of the protein‐component S to the cobalt atom in coenzyme B12‐dependent glutamate mutase from Clostridium cochleariumFEBS Letters, 1995
- Molecular Cloning, Sequencing, and Expression of the Genes Encoding Adenosylcobalamin-dependent Diol Dehydrase of Klebsiella oxytocaPublished by Elsevier ,1995
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Adenosylcobinamide methyl phosphate as a pseudocoenzyme for diol dehydraseBiochemistry, 1993
- Mechanism of action of adenosylcobalamin: glycerol and other substrate analogs as substrates and inactivators for propanediol dehydratase - kinetics, stereospecificity, and mechanismBiochemistry, 1977
- The mechanism of action of adenosylcobalaminJournal of the American Chemical Society, 1976
- Acid-base properties of free radicals in solutionAccounts of Chemical Research, 1974