Mechanism of action of streptococcal proteinase. I. Active-site titration

Biochemistry ◽  
1973 ◽  
Vol 12 (2) ◽  
pp. 320-327 ◽  
Author(s):  
A. A. Kortt ◽  
Teh-Yung Liu
Keyword(s):  
Mechanism Of Action ◽  
Active Site ◽  
Streptococcal Proteinase

The active site and mechanism of action of recombinant acetohydroxy acid synthase from tobacco

FEBS Letters ◽  
2003 ◽  
Vol 555 (2) ◽  
pp. 185-191 ◽  
Author(s):  
Moon-Young Yoon ◽  
Ji-Hyun Hwang ◽  
Min-Kyung Choi ◽  
Dong-Kil Baek ◽  
Joungmok Kim ◽  
...  
Keyword(s):  
Mechanism Of Action ◽  
Active Site ◽  
Acetohydroxy Acid Synthase

scholarly journals Phosphonate monoester inhibitors of class A β-lactamases

1991 ◽  
Vol 275 (3) ◽  
pp. 793-795 ◽  
Author(s):  
J Rahil ◽  
R F Pratt
Keyword(s):  
Enzyme Inhibition ◽  
Mechanism Of Action ◽  
Active Site ◽  
General Structure ◽  
Beta Lactamase ◽  
Beta Lactamases ◽  
Inhibitory Ability ◽  
Class A ◽  
Structure Formula ◽  
Slow Turnover

Phosphonate monoesters with the general structure: [formula: see text] are inhibitors of representative class A and class C beta-lactamases. This result extends the range of this type of inhibitor to the class A enzymes. Compounds where X is an electron-withdrawing substituent are better inhibitors than the unsubstituted analogue (X = H), and enzyme inhibition is concerted with stoichiometric release of the substituted phenol. Slow turnover of the phosphonates also occurs. These observations support the proposition that the mechanism of action of these inhibitors involves phosphorylation of the beta-lactamase active site. The inhibitory ability of these phosphonates suggests that the beta-lactamase active site is very effective at stabilizing negatively charged transition states. One of the compounds described also inactivated the Streptomyces R61 D-alanyl-D-alanine carboxypeptidase/transpeptidase.

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