Kinetic and Mechanistic Studies on the Reactions of 2-Aminobenzoyl-CoA Monooxygenase/Reductase
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1995.0686h.x/fullpdf
Reference27 articles.
1. Anaerobic degradation of 2-aminobenzoate (anthranilic acid) by denitrifying bacteria
2. 2-Aminobenzoyl-CoA monooxygenase/reductase, a novel type of flavoenzyme. Purification and some properties of the enzyme
3. 2-Aminobenzoyl-CoA monooxygenase/reductase, a novel type of flavoenzyme. Studies on the stoichiometry and the course of the reaction
4. Partition analysis and concept of net rate constants as tools in enzyme kinetics
5. The interpretation of kinetic data for enzyme-catalysed reactions involving three substrates
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1. Anthranoyl-CoA monooxygenase/reductase from Azoarcus evansii possesses both FMN and FAD in two distinct and independent active sites;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2015-08
2. Flavin-Dependent Enzymes;Comprehensive Natural Products II;2010
3. Aerobic benzoyl-CoA catabolic pathway inAzoarcus evansii: studies on the non-oxygenolytic ring cleavage enzyme;Molecular Microbiology;2005-04-29
4. Two Similar Gene Clusters Coding for Enzymes of a New Type of Aerobic 2-Aminobenzoate (Anthranilate) Metabolism in the Bacterium Azoarcus evansii;Journal of Bacteriology;2001-09-15
5. NIH shift in flavin-dependent monooxygenation: Mechanistic studies with 2-aminobenzoyl-CoA monooxygenase/reductase;Proceedings of the National Academy of Sciences;1999-07-06
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