Substrate specificity of coenzyme B12-dependent diol dehydrase: Glycerol as both a good substrate and a potent inactivator
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference7 articles.
1. Coenzyme action of adenosyl-13-epicobalamin in the diol dehydrase system
2. Purification and Properties of Dioldehydrase, an Enzyme Requiring a Cobamide Coenzyme
3. Coenzyme B12-dependent propanediol dehydratase system Ternary complex between apoenzyme, coenzyme, and substrate analog
4. A cobamide-requiring glycerol dehydrase from an acrolein-forming lactobacillus
5. Beiträge zur Papierchromatographie organischer Substanzen. VII. Die Dünnschichtchromatographie einiger Kohlehydratderivate und -Abbauprodukte
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1. The action of coenzyme B12-dependent diol dehydratase on 3,3,3-trifluoro-1,2-propanediol results in elimination of all the fluorides with formation of acetaldehyde;The Journal of Biochemistry;2024-07-11
2. Structural Basis for the Activation of the Cobalt‐Carbon Bond and Control of the Adenosyl Radical in Coenzyme B12 Catalysis;ChemBioChem;2023-06-13
3. Structural Insights into the Very Low Activity of the Homocoenzyme B 12 Adenosylmethylcobalamin in Coenzyme B 12 ‐Dependent Diol Dehydratase and Ethanolamine Ammonia‐Lyase;Chemistry – A European Journal;2022-09-19
4. Reactivating chaperones for coenzyme B12-dependent diol and glycerol dehydratases and ethanolamine ammonia-lyase;Methods in Enzymology;2022
5. Coenzyme B12-dependent eliminases: Diol and glycerol dehydratases and ethanolamine ammonia-lyase;Methods in Enzymology;2022
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