Regulation of isofunctional enzymes in Pseudomonas alcaligenes mutants defective in the gentisate pathway

• Published in: Journal of applied bacteriology Vol. 64; no. 5; p. 451
• Main Authors: Poh, C L, Bayly, R C
• Format: Journal Article
• Language: English
• Published: England 01.05.1988
• Subjects: Enzyme Induction; Gentisates - metabolism; Mixed Function Oxygenases - biosynthesis; Mixed Function Oxygenases - genetics; Mutation; Oxygenases - biosynthesis; Oxygenases - genetics; Pseudomonas - enzymology; Pseudomonas - genetics; Pseudomonas - metabolism; Substrate Specificity
• ISSN: 0021-8847
• DOI: 10.1111/j.1365-2672.1988.tb05102.x

The regulation of the inducible set of gentisate pathway enzymes used by Pseudomonas alcaligenes (P25X1) has been studied in strains derived from mutant strains of P25X1 that had lost the constitutive enzymes that degrade m-cresol, 2,5-xylenol and 3,5-xylenol. The enzyme, 3-hydroxybenzoate 6-hydroxylase II, that catalyzes the oxidation of 3-hydroxybenzoate to gentisate is substrate- and product-induced while gentisate dioxygenase II is substrate induced. Neither 3-hydroxybenzoate nor gentisate could induce the synthesis of maleylpyruvate hydrolase II and fumarylpyruvate hydrolase II. The results suggest that the structural genes encoding these four inducible enzymes and malepylpyruvate hydrolase I (a constitutive enzyme) exist in at least four operons. There is strict induction specificity of expression of this inducible set of gentisate pathway enzymes. 3-Hydroxy-4-methylbenzoate failed to induce whilst 3-hydroxybenzoate and 3-hydroxy-5-methylbenzoate served as inducers of 6-hydroxylase II. Degradation of 2,5-xylenol is mediated by constitutive enzymes whereas the inducible set of enzymes are responsible for the metabolism of m-cresol and 3,5-xylenol.