Literature DB >> 3872609

A direct spectrophotometric assay for D-alanine carboxypeptidases and for the esterase activity of beta-lactamases.

R F Pratt, W S Faraci, C P Govardhan.   

Abstract

A direct spectrophotometric pH indicator method has been devised to assay the activity of the D-Ala carboxypeptidase/transpeptidase of Streptomyces R61, and which should be of general application to D-Ala carboxypeptidases. The substrate employed is N,N'-diacetyl-L-lysyl-D-alanyl-D-lactate. The method allows the determination of steady-state kinetic parameters, and can also be used for the assay of the esterase activity of beta-lactamases against specific depsipeptides.

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Year:  1985        PMID： 3872609     DOI： 10.1016/0003-2697(85)90106-x

Source DB:  PubMed          Journal:  Anal Biochem        ISSN： 0003-2697            Impact factor:   3.365


  3 in total

1.  Active-site-serine D-alanyl-D-alanine-cleaving-peptidase-catalysed acyl-transfer reactions. Procedures for studying the penicillin-binding proteins of bacterial plasma membranes.

Authors:  J M Ghuysen; J M Frère; M Leyh-Bouille; M Nguyen-Distèche; J Coyette
Journal:  Biochem J       Date:  1986-04-01       Impact factor: 3.857

2.  Importance of the His-298 residue in the catalytic mechanism of the Streptomyces R61 extracellular DD-peptidase.

Authors:  A M Hadonou; M Jamin; M Adam; B Joris; J Dusart; J M Ghuysen; J M Frère
Journal:  Biochem J       Date:  1992-03-01       Impact factor: 3.857

3.  Statistical Evaluation of HTS Assays for Enzymatic Hydrolysis of β-Keto Esters.

Authors:  O Buß; S Jager; S-M Dold; S Zimmermann; K Hamacher; K Schmitz; J Rudat
Journal:  PLoS One       Date:  2016-01-05       Impact factor: 3.240
  3 in total

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