Regulation of enzymes involved in the conversion of tryptophan to nicotinamide adenine dinucleotide in a colorless strain of Xanthomonas pruni.

Brown AT, Wagner C
J Bacteriol. 1970 101 (2): 456-63

PMID: 4313053 · PMCID: PMC284928 · DOI:10.1128/JB.101.2.456-463.1970

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, alpha-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.

MeSH Terms (11)

Amidohydrolases Enzyme Induction Hydrolases Kynurenine Mutation NAD ortho-Aminobenzoates Oxygenases Tryptophan Tryptophan Oxygenase Xanthomonas

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