Enzymic Reaction Selectivity by Negative Catalysis or How Do Enzymes Deal with Highly Reactive Intermediates?
- 1 April 1990
- journal article
- review article
- Published by Wiley in Angewandte Chemie International Edition in English
- Vol. 29 (4) , 355-361
- https://doi.org/10.1002/anie.199003551
Abstract
No abstract availableKeywords
This publication has 56 references indexed in Scilit:
- Antikörper als KatalysatorenAngewandte Chemie, 1989
- Catalytic‐site mapping of pyruvate formate lyaseEuropean Journal of Biochemistry, 1988
- Die enzymatische Umwandlung von Isobutyryl- zun-Butyrylcarba(dethia)-Coenzym A: Eine coenzym-B12-abhängige GerüstumlagerungAngewandte Chemie, 1988
- The error in the cryptic stereospecificity of methylmalonyl‐CoA mutaseEuropean Journal of Biochemistry, 1988
- Cobalt-carbon bond dissociation energy of coenzyme B12Journal of the American Chemical Society, 1984
- Ribonucleotide Reductase—a Radical EnzymeScience, 1983
- A Spectrophotometric Rapid Kinetic Study of Reactions Catalysed by Coenzyme‐B12‐Dependent Ethanolamine Ammonia‐LyaseEuropean Journal of Biochemistry, 1978
- Coenzym B12 als gemeinsamer Wasserstoffüberträger der Dioldehydrase- und der Methylmalonyl-CoA-Mutase-ReaktionCellular and Molecular Life Sciences, 1966
- GLUTAMATE MUTASE REACTION*Annals of the New York Academy of Sciences, 1964
- An intramolecular rearrangement in the methylmalonyl isomerase reaction as demonstrated by positive and negative ion mass analysis of succinic acidBiochemical and Biophysical Research Communications, 1962