1yqs: Difference between revisions

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[[Image:1yqs.gif|left|200px]]
{{Seed}}
[[Image:1yqs.png|left|200px]]


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{{STRUCTURE_1yqs|  PDB=1yqs  |  SCENE=  }}  
{{STRUCTURE_1yqs|  PDB=1yqs  |  SCENE=  }}  


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




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_15909988}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15909988 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15909988}}


==About this Structure==
==About this Structure==
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[[Category: Peptidase]]
[[Category: Peptidase]]
[[Category: Sulfonylation]]
[[Category: Sulfonylation]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 16:39:53 2008''
 
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