1elg: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:1elg.gif|left|200px]]
{{Seed}}
[[Image:1elg.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1elg|  PDB=1elg  |  SCENE=  }}  
{{STRUCTURE_1elg|  PDB=1elg  |  SCENE=  }}  


'''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.
The line below this paragraph, {{ABSTRACT_PUBMED_7779821}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 7779821 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_7779821}}


==About this Structure==
==About this Structure==
Line 28: Line 32:
[[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 Fri May 2 15:14:49 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:56:15 2008''