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.[1]References
- The prephenate dehydrogenase component of the bifunctional T-protein in enteric bacteria can utilize L-arogenate. Ahmad, S., Jensen, R.A. FEBS Lett. (1987) [Pubmed]
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