1yqs
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1yqs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yqs, resolution 1.05Å" /> '''Inhibition of the R6...)
Next diff →
Revision as of 04:52, 21 November 2007
|
Inhibition of the R61 DD-Peptidase by N-benzoyl-beta-sultam
Overview
N-Acyl-beta-sultams are time-dependent, irreversible active site-directed, inhibitors of Streptomyces R61 DD-peptidase. The rate of inactivation is, first order with respect to beta-sultam concentration, and the, second-order rate constants show a dependence on pH similar to that for, the hydrolysis of a substrate. Inactivation is due to the formation of a, stable 1:1 enzyme-inhibitor complex as a result of the active site serine, being sulfonylated by the beta-sultam as shown by ESI-MS analysis and by, X-ray crystallography. A striking feature of the sulfonyl enzyme is that, the inhibitor is not bound to the oxyanion hole but interacts extensively, with the "roof" of the active site where the Arg 285 is located.
About this Structure
1YQS is a Single protein structure of sequence from Streptomyces sp. with BSA and GOL as ligands. Active as Serine-type D-Ala-D-Ala carboxypeptidase, with EC number 3.4.16.4 Full crystallographic information is available from OCA.
Reference
Inactivation of bacterial DD-peptidase by beta-sultams., Llinas A, Ahmed N, Cordaro M, Laws AP, Frere JM, Delmarcelle M, Silvaggi NR, Kelly JA, Page MI, Biochemistry. 2005 May 31;44(21):7738-46. PMID:15909988
Page seeded by OCA on Wed Nov 21 06:59:34 2007
