1elg

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[[Image:1elg.gif|left|200px]]
[[Image:1elg.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1elg |SIZE=350|CAPTION= <scene name='initialview01'>1elg</scene>, resolution 1.65&Aring;
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The line below this paragraph, containing "STRUCTURE_1elg", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=BAA:(TERT-BUTYLOXYCARBONYL)-ALANYL-ALANYL-AMINE'>BAA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Pancreatic_elastase Pancreatic elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.36 3.4.21.36] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1elg| PDB=1elg | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1elg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1elg OCA], [http://www.ebi.ac.uk/pdbsum/1elg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1elg RCSB]</span>
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}}
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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'''
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[[Category: Ringe, D.]]
[[Category: Ringe, D.]]
[[Category: Steinmetz, A C.U.]]
[[Category: Steinmetz, A C.U.]]
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[[Category: complex (hydrolase/inhibitor)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:14:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:04:55 2008''
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Revision as of 12:14, 2 May 2008

Image:1elg.gif

Template:STRUCTURE 1elg

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.

About this Structure

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

Reference

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 Page seeded by OCA on Fri May 2 15:14:49 2008

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