The prephenate dehydrogenase component of the bifunctional T‐protein in enteric bacteria can utilize L‐arogenate

FEBS Letters

Jensen, Roy A.¹  Ahmad, Suhail¹ 

[1] Department of Microbiology and Cell Science, McCarty Hall, IFAS, University of Florida, Gainesville, FL 32611, USA

关键词: Tyrosine synthesis;    T-protein;    Enteric bacteria;    Regulatory enzyme;   

DOI  :  10.1016/0014-5793(87)80771-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 K12, 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.

【 授权许可】

Unknown