Influence of pH, temperature and concentration of substrate on the activity of L1 metallo-β-lactamase

Chinese Journal of Antibiotics

Volumn 35, Issue 1, 2010, Pages

  Qing, Peng ^a   Bing, Hou ^b   Fen, Yao ^a   Yuan Shu, Qian ^a  

^a SHANTOU UNIVERSITY   (China)

^b Clinical Laboratory of Dermatosis Hospital   (China)

Author keywords

Lactamase; pH; Substrate; Temperature

Indexed keywords

IMIPENEM; L1 METALLO BETA LACTAMASE; METALLO BETA LACTAMASE; UNCLASSIFIED DRUG;

ARTICLE; ENZYME ACTIVITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; INHIBITION KINETICS; PH; SPECTROPHOTOMETER; TEMPERATURE;

EID: 77950807378     PISSN: 10018689     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (7)

1. Page M I, Badarau A. The mechanisms of catalysis by metallo β-lactamases[J]. Bioinorg Chem, 2008,5(7):62-97.
2. Berg J M, Tymoczko J L, Stryer L. Biochemistry 5th ed[M]. New York: W. H. Freeman and Company, 2002.
3. Goto M, Yasuzawa H, Higashi T, et al. Dependence of hydrolysis of beta-lactams with a zinc (II)-beta-lactamase produced from Serratia marcescens (IMP-1) on pH and concentration of zinc (II) ion: dissociation of Zn (II) from IMP-1 in acidic medium[J]. Biol Pharm Bull. 2003, 26:589-594. (Pubitemid 39663546)
4. Ohsuka S, Arakawa Y, Horii T, et al. Effect of pH on activities of novel β-lactamase and β-lactamase inhibitors against the β-lactamase[J]. Antimicrob Agents chemother, 1995, 39:1856-1858.
5. Peterson M E, Daniel R M, Danson M J, et al. The dependence of enzyme activity on temperature: determination and validation of parameters[J]. Biochem J, 2007, 402:331-337.