The prephenate dehydrogenase component of the bifunctional T‐protein in enteric bacteria can utilize L‐arogenate
Year: 1987
Type: article
Abstract: 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.
Source: FEBS Letters
Authors: Suhail Ahmad, Roy A. Jensen
Language: English
Subfield: Genetics
Domain: Life Sciences
Open Access status: bronze
Funder: National Science Foundation
OpenAlex ID: W2137173465