1ELF

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

Summary for 1ELF

• Entry DOI: 10.2210/pdb1elf/pdb
• Descriptor: PORCINE PANCREATIC ELASTASE, CALCIUM ION, SULFATE ION, ... (5 entities in total)
• Functional Keywords: complex (hydrolase-inhibitor), complex (hydrolase-inhibitor) complex, complex (hydrolase/inhibitor)
• Biological source: Sus scrofa (pig)
• Cellular location: Secreted: P00772
• Total number of polymer chains: 1
• Total formula weight: 26419.54

Authors

Ding, X.,Rasmussen, B.,Demuth, H.-U.,Ringe, D.,Steinmetz, A.C.U. (deposition date: 1995-03-13, release date: 1995-07-10, Last modification date: 2024-06-05)

Primary citation

Ding, X.,Rasmussen, B.F.,Demuth, H.U.,Ringe, D.,Steinmetz, A.C.
Nature of the inactivation of elastase by N-peptidyl-O-aroyl hydroxylamine as a function of pH.
Biochemistry, 34:7749-7756, 1995

PubMed Abstract: 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.

PubMed: 7779821
DOI: 10.1021/bi00023a022

Experimental method

X-RAY DIFFRACTION (1.7 Å)