1YQS

Inhibition of the R61 DD-Peptidase by N-benzoyl-beta-sultam

Summary for 1YQS

• Entry DOI: 10.2210/pdb1yqs/pdb
• Related: 1MPL 1SCW 1SDE
• Descriptor: D-alanyl-D-alanine carboxypeptidase, 2-(BENZOYLAMINO)ETHANESULFONIC ACID, GLYCEROL, ... (4 entities in total)
• Functional Keywords: cell well biosynthesis, beta-lactam, beta-sultam, peptidase, sulfonylation, hydrolase
• Biological source: Streptomyces sp.
• Cellular location: Secreted: P15555
• Total number of polymer chains: 1
• Total formula weight: 38065.27

Authors

Ahmed, N.,Cordaro, M.,Laws, A.P.,Delmarcelle, M.,Silvaggi, N.R.,Kelly, J.A.,Page, M.I. (deposition date: 2005-02-02, release date: 2005-06-28, Last modification date: 2024-10-30)

Primary citation

Ahmed, N.,Cordaro, M.,Laws, A.P.,Delmarcelle, M.,Silvaggi, N.R.,Kelly, J.A.,Page, M.I.
Inactivation of Bacterial dd-Peptidase by beta-Sultams.
Biochemistry, 44:7738-7746, 2005

PubMed Abstract: 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.

PubMed: 15909988
DOI: 10.1021/bi050110o

Experimental method

X-RAY DIFFRACTION (1.05 Å)