Biosynthesis of l-Phenylalanine and l-Tyrosine in the Actinomycete Amycolatopsis methanolica.

Applied and Environmental Microbiology
A Abou-ZeidL Dijkhuizen

Abstract

Auxotrophic mutants of the actinomycete Amycolatopsis methanolica requiring l-Phe or l-Tyr were isolated and identified as strains lacking prephenate dehydratase (strain GH71) or arogenate dehydrogenase (strain GH70), respectively. A. methanolica thus employs single pathways only for the biosynthesis of these aromatic amino acids. Anion-exchange chromatography of extracts revealed two peaks with Phe as well as Tyr aminotransferase (AT) activity (Phe/Tyr ATI and Phe/Tyr ATII) and three peaks with prephenate AT activity (Ppa ATI to Ppa ATIII). Phe/Tyr ATI and Ppa ATI coeluted and appear to function as the A. methanolica branched-chain amino acid AT. Ppa ATII probably functions as the aspartate AT. Mutant studies showed that Phe/Tyr ATII is the dominant AT in l-Phe biosynthesis and in l-Tyr catabolism but not in l-Tyr biosynthesis. Biochemical studies showed that Ppa ATIII is highly specific for prephenate and provided evidence that Ppa ATIII is the dominant AT in l-Tyr biosynthesis.

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Citations

Oct 2, 2002·European Journal of Biochemistry·Pascal Rippert, Michel Matringe
Mar 11, 1998·Natural Product Reports·P M Dewick
Mar 7, 2008·Microbiology and Molecular Biology Reviews : MMBR·Carol A BonnerRoy A Jensen
Jul 19, 2011·International Journal of Systematic and Evolutionary Microbiology·Tiago Domingues ZucchiMichael Goodfellow
Jul 30, 2011·International Journal of Biological Macromolecules·Hyung-Keun KuSoo Jae Lee

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