Regulation of Enzymes Involved in the Conversion of Tryptophan to Nicotinamide Adenine Dinucleotide in a Colorless Strain of Xanthomonas pruni

Author:

Brown Albert T.1,Wagner Conrad1

Affiliation:

1. Department of Biochemistry, Vanderbilt University, and Biochemistry Research Laboratory, Veterans Administration Hospital, Nashville, Tennessee 37203

Abstract

A colorless strain of Xanthomonas pruni was isolated which is capable of converting tryptophan to nicotinamide adenine dinucleotide (NAD). The enzymes responsible for the conversion of tryptophan to quinolinic acid were shown to be present. Nicotinic acid-requiring mutants were isolated, and it was found that the growth of these mutants can be supported by various intermediates on the pathway from tryptophan to NAD. The first three enzymes on this pathway are induced coordinately by l -tryptophan. Gratuitous inducers of these enzymes include d -tryptophan, α-methyl- dl -tryptophan, and 4-methyl- dl -tryptophan; formyl- l -kynurenine and l -kynurenine were not effective as inducers. These data suggest that at least the first three enzymes in the pathway from tryptophan to NAD are under common regulatory control.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference23 articles.

1. Nicotinic acid biosynthesis in prototrophs and tryptophan auxotrophs of Saccharomyces cerevisiae;Ahmad F.;J. Biol. Chem.,1966

2. Kynurenine as an intermediate in the formation of nicotinic acid from tryptophan by Neurospora;Beadle G. W.;Proc. Nat. Acad. Sci. U.S.A.,1947

3. Campbell D. H. J.! S. Garvey N. E. Cremer and D. H. Sussdorf. 1963. Methods in immunology. W. A. Benjamin New York.

4. Nicotinamide coenzymes;Chaykin S.;Ann. Rev. Biochem.,1967

5. The niacintryptophan relationship in the metabolism of Xanthomonas pruni;Davis D.;J. Biol. Chem.,1951

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