The prephenate dehydrogenase component of the bifunctional T-protein in enteric bacteria can utilize L-arogenate.
The prephenate dehydrogenase component of the bifunctional T-protein (chorismate mutase:prephenate dehydrogenase) has been shown to utilize L-arogenate, a common precursor of phenylalanine and tyrosine in nature, as a substrate. Partially purified T-protein from Klebsiella pneumoniae and from Escherichia coli strains K 12, B, C and W was used to demonstrate the utilization of L-arogenate as an alternative substrate for prephenate in the presence of nicotinamide adenine dinucleotide as cofactor. The formation of L-tyrosine from L-arogenate by the T-protein dehydrogenase was confirmed by high-performance liquid chromatography. As expected of a common catalytic site, dehydrogenase activity with either prephenate or L-arogenate was highly sensitive to inhibition by L-tyrosine.
D000600:Amino Acids, Dicarboxylic / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D001665:Binding Sites; D002826:Chorismate Mutase / Q000378:metabolism*; D053138:Cyclohexenes; D004926:Escherichia coli / Q000201:enzymology*; D007535:Isomerases / Q000378:metabolism*; D007711:Klebsiella pneumoniae / Q000201:enzymology*; D010088:Oxidoreductases / Q000378:metabolism*; D011303:Prephenate Dehydrogenase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D013045:Species Specificity; D013379:Substrate Specificity; D014443:Tyrosine / Q000031:analogs & derivatives* / Q000096:biosynthesis / Q000378:metabolism / Q000494:pharmacology
D000600:Amino Acids, Dicarboxylic; D001426:Bacterial Proteins; D053138:Cyclohexenes; D014443:Tyrosine; C015478:pretyrosine; D010088:Oxidoreductases; D011303:Prephenate Dehydrogenase; C027017:cyclohexadienyl dehydrogenase; D007535:Isomerases; D002826:Chorismate Mutase