1elf: Difference between revisions

Revision as of 00:56, 1 July 2008

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File:1elf.png

Template:STRUCTURE 1elf

NATURE OF THE INACTIVATION OF ELASTASE BY N-PEPTIDYL-O-AROYL HYDROXYLAMINE AS A FUNCTION OF PHNATURE OF THE INACTIVATION OF ELASTASE BY N-PEPTIDYL-O-AROYL HYDROXYLAMINE AS A FUNCTION OF PH

Template:ABSTRACT PUBMED 7779821

About this StructureAbout this Structure

1ELF is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

ReferenceReference

Nature of the inactivation of elastase by N-peptidyl-O-aroyl hydroxylamine as a function of pH., Ding X, Rasmussen BF, Demuth HU, Ringe D, Steinmetz AC, Biochemistry. 1995 Jun 13;34(23):7749-56. PMID:7779821

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OCA

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-'''NATURE OF THE INACTIVATION OF ELASTASE BY N-PEPTIDYL-O-AROYL HYDROXYLAMINE AS A FUNCTION OF PH'''
+===NATURE OF THE INACTIVATION OF ELASTASE BY N-PEPTIDYL-O-AROYL HYDROXYLAMINE AS A FUNCTION OF PH===
-==Overview==
+<!--
-The mechanism of inactivation of porcine pancreatic elastase (PPE) by N-peptidyl-O-aroylhydroxylamine was studied by X-ray crystallography. The inactivator forms a stable complex with the enzyme by means of a covalent attachment to the active site Ser 203(195) O gamma. The nature of the complex is, however, different depending on the pH at which the inactivation reaction occurs. At pH 5, the complex formed is a hydroxylamine derivative of Ser 203(195) in which the O gamma of serine is the oxygen of the hydroxylamine derivative. At pH 7.5, the complex formed is a carbamate derivative at Ser 203(195) O gamma. In both types of complexes, the inactivator binds in the S' subsites of the enzyme instead of forming the usual antiparallel beta-sheet with the S subsites. The implication for the mechanism of inactivation at different pHs is discussed.
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