Inhibition of transketolase by p-hydroxyphenylpyruvate.
The effect of p-hydroxyphenylpyruvate, a natural analogue of transketolase substrate, on the catalytic activity of the enzyme was investigated. p-Hydroxyphenylpyruvate proved to be a reversible and competitive inhibitor of transketolase with respect to substrate; it was also able to displace thiamine diphosphate from holotransketolase. The data suggest that p-hydroxyphenylpyruvate participates in the regulation of tyrosine biosynthesis by influencing the catalytic activity of transketolase.
Solovjeva
O N
ON
A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russia.
Kochetov
G A
GA
D001667:Binding, Competitive; D003067:Coenzymes / Q000378:metabolism; D020035:Holoenzymes / Q000378:metabolism; D007700:Kinetics; D010667:Phenylpyruvic Acids / Q000494:pharmacology*; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D013997:Time Factors; D014174:Transketolase / Q000037:antagonists & inhibitors* / Q000378:metabolism
D003067:Coenzymes; D020035:Holoenzymes; D010667:Phenylpyruvic Acids; C010590:4-hydroxyphenylpyruvic acid; D014174:Transketolase