Inhibition of a Putative Dihydropyrimidinase from Pseudomonas aeruginosa PAO1 by Flavonoids and Substrates of Cyclic Amidohydrolases

• Published in: PloS one Vol. 10; no. 5; p. e0127634
• Main Author: Huang, Cheng-Yang
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 19.05.2015; Public Library of Science (PLoS)
• Subjects: Acetic acid; Allantoin; Allantoinase; Amidohydrolases - antagonists & inhibitors; Amidohydrolases - metabolism; Analogs; Analysis; Antibiotics; Catalysis; Deoxyribonucleic acid; Dihydroorotase; Dihydropyrimidinase; DNA; Drugs; Enzymes; Flavonoids; Flavonoids - pharmacology; Flavonols; Fluorescence; Hydantoin; Hydantoinase; Inhibitors; Isoflavones; Kaempferol; Microorganisms; Organic acids; Orotic acid; Plasmids; Proteins; Pseudomonas aeruginosa; Pseudomonas aeruginosa - enzymology; Quenching; Quercetin; Substrate inhibition; Substrate Specificity; Substrates

Dihydropyrimidinase is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase. These metalloenzymes possess very similar active sites and may use a similar mechanism for catalysis. However, whether the substrates and inhibitors of ot...