Essential histidine residues in coenzyme B12-dependent diol dehydrase: Dye-sensitized photooxidation and ethoxycarbonylation
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference23 articles.
1. Substrate specificity of coenzyme B12-dependent diol dehydrase: Glycerol as both a good substrate and a potent inactivator
2. Purification and Properties of Dioldehydrase, an Enzyme Requiring a Cobamide Coenzyme
3. Coenzyme B12-dependent diol dehydrase: Chemical modification with 2,3-butanedione and phenylglyoxal
4. Reactive sulfhydryl groups of coenzyme B12-dependent diol dehydrase: Differential modification of essential and nonessential ones
5. Chemical modification of coenzyme B12-dependent diol dehydrase with pyridoxal 5′-phosphate: Lysyl residue essential for interaction between two components of the enzyme
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1. Coenzyme B12-dependent eliminases: Diol and glycerol dehydratases and ethanolamine ammonia-lyase;Methods in Enzymology;2022
2. Histidine-α143 Assists 1,2-Hydroxyl Group Migration and Protects Radical Intermediates in Coenzyme B12-Dependent Diol Dehydratase;Biochemistry;2008-02-09
3. Photosensitized Oxidation of 13C,15N-Labeled Imidazole Derivatives;Journal of the American Chemical Society;2002-07-19
4. Chemical Modification and Site-Directed Mutagenesis of Human Liver Arginase: Evidence That the Imidazole Group of Histidine-141 Is Not Involved in Substrate Binding;Archives of Biochemistry and Biophysics;1999-11
5. Evidence That Histidine-163 Is Critical for Catalytic Activity, but Not for Substrate Binding to Escherichia coli Agmatinase;Biochemical and Biophysical Research Communications;1999-10
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