[Inhibition of penicillin acylase from Escherichia coli by benzylalkylketones and benzylalkylcarbinols].
A number of benzylalkylketones and benzylalkylcarbinols have been synthesized as non-hydrolizable substrate analogues of penicillin acylase (EC 3.5.1.11), and their affinity to the enzyme has been studied. The compounds with plane trigonal carbonyl group (ketones) were established to has bind to the enzyme 20-40 times more tightly than their tetrahedral counterparts with a hydroxyl function (carbinols). 4-Oxo-5-phenylpentanoic acid was found to be one of the most potent reversible competitive inhibitors of penicillin acylase with Ki-31 microM.
Tserniuk
V N
VN
Solodenko
V A
VA
Kukhar'
V P
VP
D000478:Alkylation; D001593:Benzyl Compounds / Q000494:pharmacology*; D004926:Escherichia coli / Q000201:enzymology*; D006868:Hydrolysis; D007659:Ketones / Q000494:pharmacology*; D015394:Molecular Structure; D010399:Penicillin Amidase / Q000037:antagonists & inhibitors*; D010626:Phenylethyl Alcohol / Q000031:analogs & derivatives* / Q000494:pharmacology; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D001593:Benzyl Compounds; D007659:Ketones; D010399:Penicillin Amidase; D010626:Phenylethyl Alcohol