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

A Abou-Zeid, G Euverink, G I Hessels, R A Jensen, L Dijkhuizen
1995 Applied and Environmental Microbiology  
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
more » ... 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 branchedchain amino acid AT.
doi:10.1128/aem.61.4.1298-1302.1995 fatcat:5eucijjdbjcstpnobakghgxw5m