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Appl Environ Microbiol. 1984 December; 48(6): 1118-1122
Copyright © 1984, American Society for Microbiology. All Rights Reserved.

Production of Coenzyme A by a Mutant of Brevibacterium ammoniagenes Resistant to Oxypantetheine

Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto University, Kyoto 606, Japan

ABSTRACT

For improved production of coenzyme A (CoA), a mutant of Brevibacterium ammoniagenes IFO127071 resistant to oxypantetheine, the corresponding oxygen analog of pantetheine, was obtained. In the mutant, activity of pantothenate kinase (EC 2.7.1.33), the first-step enzyme for the biosynthesis of CoA from pantothenic acid, L-cysteine, and ATP, was about threefold higher than that in the parent strain. As the main regulation mechanism of CoA biosynthesis in this bacterium is negative feedback inhibition of pantothenate kinase by CoA, the mutant is very useful as a catalyst for practical production of CoA. When added to culture broth of the mutant, pantothenate, L-cysteine, and AMP gave 9.3 mg of CoA per ml. With pantetheine and AMP, 11.5 mg of CoA per ml accumulated. These values were about threefold higher than those with the parent strain, and more than 70% of the added AMP was converted to CoA.

^* Corresponding author.

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