Evidence for a tetrahedral intermediate complex during serpin-proteinase interactions

Proteinase inhibitors in the serpin family form complexes with serine proteinases by interactions between the gamma-OH group at serine 195 of the enzyme and a specific peptide bond within the reactive site loop of the inhibitor. However, the type of complex formed (i.e. Michaelis, acyl, or tetrahedr...

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Veröffentlicht in:	The Journal of biological chemistry 1991-07, Vol.266 (21), p.13489-13491
Hauptverfasser:	MATHESON, N. R, VAN HALBEEK, H, TRAVIS, J
Format:	Artikel
Sprache:	eng
Schlagworte:	alpha 1-Antitrypsin - chemistry Analytical, structural and metabolic biochemistry Animals Biological and medical sciences complex Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hydrolases In Vitro Techniques intermediates Macromolecular Substances Magnetic Resonance Spectroscopy N.M.R Pancreatic Elastase - chemistry Recombinant Proteins serine proteinase serpins Swine
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