Inactivation of beta-lactamase I from B. cereus 569/H with phenylglyoxal, an arginine-selective reagent

Inactivation of beta-lactamase I from B. cereus 569/H with phenylglyoxal, an arginine-selective reagent

beta -Lactamase (EC 3.5.2.6: penicillin amido- beta -lactam hydrolase) I from B. cereus 569/H is inactivated by treatment with phenylglyoxal. Inactivation depends on the pH and the presence of bicarbonate in a manner which suggests that it is due to the modification of arginyl residues. Total inacti...

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Veröffentlicht in:Biochemical and biophysical research communications 1982-11, Vol.109 (1), p.242-249
Hauptverfasser: Borders, Jr, C L, Patrick, S L, Davis, T L, Mézes, P S, Viswanatha, T
Format: Artikel
Sprache:eng
Schlagworte:
Aldehydes - pharmacology
Arginine
Bacillus cereus - enzymology
beta -Lactamase
beta-Lactamases - metabolism
Hydrogen-Ion Concentration
Kinetics
Penicillinase - metabolism
phenylglyoxal
Phenylglyoxal - pharmacology
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Zusammenfassung:beta -Lactamase (EC 3.5.2.6: penicillin amido- beta -lactam hydrolase) I from B. cereus 569/H is inactivated by treatment with phenylglyoxal. Inactivation depends on the pH and the presence of bicarbonate in a manner which suggests that it is due to the modification of arginyl residues. Total inactivation correlates with the loss of 8 arginines per beta -lactamase, and a competitive inhibitor provides full protection from inactivation and protects ca. 2 arginines from modification.
ISSN:0006-291X
DOI:10.1016/0006-291X(82)91591-1