1scn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1scn.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1scn.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1scn| PDB=1scn | SCENE= }}
{{STRUCTURE_1scn| PDB=1scn | SCENE= }}
-
'''INACTIVATION OF SUBTILISIN CARLSBERG BY N-(TERT-BUTOXYCARBONYL-ALANYL-PROLYL-PHENYLALANYL)-O-BENZOYL HYDROXYLAMINE: FORMATION OF COVALENT ENZYME-INHIBITOR LINKAGE IN THE FORM OF A CARBAMATE DERIVATIVE'''
+
===INACTIVATION OF SUBTILISIN CARLSBERG BY N-(TERT-BUTOXYCARBONYL-ALANYL-PROLYL-PHENYLALANYL)-O-BENZOYL HYDROXYLAMINE: FORMATION OF COVALENT ENZYME-INHIBITOR LINKAGE IN THE FORM OF A CARBAMATE DERIVATIVE===
-
==Overview==
+
<!--
-
The mechanism of inactivation of serine proteases by N-peptidyl-O-aroylhydroxylamines was studied by X-ray crystallography. Cocrystals of subtilisin Carlsberg inactivated with N-((tert-butoxycarbonyl)alanylprolylphenylalanyl)-O-nitrobenzoy lhydroxylamine were grown, and diffraction data to 1.8-A resolution were obtained. The resulting electron density maps clearly reveal that the gamma-oxygen of the catalytic serine forms a carbamate derivative with the inhibitor. The peptide part of the inhibitor does not form the usual antiparallel beta-sheet in the P binding cleft but protrudes out of the active site and is stabilized by a network of water molecules. These results, combined with kinetic characterization reported previously [Demuth, H.-U., Schoenlein, C., &amp; Barth, A. (1989b) Biochim. Biophys. Acta 996, 19-22; Schmidt, C., Schmidt, R., &amp; Demuth, H.-U. (1990) Peptides (Giralt, E., &amp; Andreu, D., Eds.) ESCOM Science Publishers B.V., Amsterdam] support the existence of at least one intermediate between the formation of the Michaelis complex and the final product. We suggest a mechanism for the inactivation of subtilisin Carlsberg by N-((tert-butoxycarbonyl)alanylprolylphenylalanyl)-O-benzoylhydr oxylamine whereby a negatively charged Michaelis complex undergoes a Lossen rearrangement giving rise to an isocyanate intermediate that reacts with the side chain of the active site serine.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8068694}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8068694 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8068694}}
==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Ringe, D.]]
[[Category: Ringe, D.]]
[[Category: Steinmetz, A C.U.]]
[[Category: Steinmetz, A C.U.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:33:02 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:42:17 2008''

Revision as of 00:42, 29 July 2008

Image:1scn.png

Template:STRUCTURE 1scn

INACTIVATION OF SUBTILISIN CARLSBERG BY N-(TERT-BUTOXYCARBONYL-ALANYL-PROLYL-PHENYLALANYL)-O-BENZOYL HYDROXYLAMINE: FORMATION OF COVALENT ENZYME-INHIBITOR LINKAGE IN THE FORM OF A CARBAMATE DERIVATIVE

Template:ABSTRACT PUBMED 8068694

About this Structure

1SCN is a Single protein structure. Full crystallographic information is available from OCA.

Reference

Inactivation of subtilisin Carlsberg by N-((tert-butoxycarbonyl)alanylprolylphenylalanyl)-O-benzoylhydroxyl- amine: formation of a covalent enzyme-inhibitor linkage in the form of a carbamate derivative., Steinmetz AC, Demuth HU, Ringe D, Biochemistry. 1994 Aug 30;33(34):10535-44. PMID:8068694

Page seeded by OCA on Tue Jul 29 03:42:17 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1scn"
Personal tools