1hax
From Proteopedia
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[[Category: serine proteinase]] | [[Category: serine proteinase]] | ||
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Revision as of 13:28, 30 October 2007
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SNAPSHOTS OF SERINE PROTEASE CATALYSIS: (A) ACYL-ENZYME INTERMEDIATE BETWEEN PORCINE PANCREATIC ELASTASE AND HUMAN BETA-CASOMORPHIN-7 AT PH 5
Overview
Studies on the catalytic mechanism and inhibition of serine proteases are, widely used as paradigms for teaching enzyme catalysis. Ground-breaking, work on the structures of chymotrypsin and subtilisin led to the idea of a, conserved catalytic triad formed by the active site Ser, His and Asp, residues. An oxyanion hole, consisting of the peptide amide of the active, site serine and a neighbouring glycine, was identified, and hydrogen, bonding in the oxyanion hole was suggested to stabilize the two proposed, tetrahedral intermediates on the catalytic pathway. Here we show electron, density changes consistent with the formation of a tetrahedral, intermediate during the hydrolysis of an acyl-enzyme complex formed, between a natural heptapeptide and elastase. No electron density for an, ... [(full description)]
About this Structure
1HAX is a [Single protein] structure of sequence from [Homo sapiens] and [Sus scrofa] with CA and SO4 as [ligands]. Active as [Transferred entry: 3.4.21.36], with EC number [3.4.21.11]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].
Reference
X-ray snapshots of serine protease catalysis reveal a tetrahedral intermediate., Wilmouth RC, Edman K, Neutze R, Wright PA, Clifton IJ, Schneider TR, Schofield CJ, Hajdu J, Nat Struct Biol. 2001 Aug;8(8):689-94. PMID:11473259
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