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J. Biol. Chem., Vol. 266, Issue 21, 13489-13491, Jul, 1991
NR Matheson, H van Halbeek and J Travis
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
tetrahedral) is unknown. Until now, 13C NMR spectroscopy studies have only
been useful in examining complexes formed with either peptide-related or
small protein inhibitors, where 13C-labeled amino acids can be inserted
semi-synthetically. Recombinant DNA technology has, however, made it
possible to specifically enrich larger proteins with 13C. In the case of
serpins we have examined the structure of the complex formed between human
alpha 1-proteinase inhibitor uniformally labeled with [13C]methionine and
porcine pancreatic elastase. 13C NMR spectroscopic studies revealed a large
upfield chemical shift of the carbonyl signal of Met-358 upon complex
formation suggesting for the first time that a tetrahedral adduct is formed
between a serpin inhibitor and a serine proteinase.
Evidence for a tetrahedral intermediate complex during serpin- proteinase interactions
Department of Biochemistry, University of Georgia, Athens 30602.
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