3tgk
TRYPSINOGEN MUTANT D194N AND DELETION OF ILE 16-VAL 17 COMPLEXED WITH BOVINE PANCREATIC TRYPSIN INHIBITOR (BPTI)
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OverviewOverview
The contribution of induced fit to enzyme specificity has been much, debated, although with little experimental data. Here we probe the effect, of induced fit on enzyme specificity using the trypsin(ogen) system. BPTI, is known to induce trypsinogen to assume a trypsinlike conformation., Correlations are observed between BPTI affinity and the values of, k(cat)/K(m) for the hydrolysis of two substrates by eight trypsin(ogen), variants. The slope of both correlations is -1.8. The crystal structures, of the BPTI complexes of four variant trypsinogens were also solved. Three, of these enzymes, K15A, DeltaI16V17/D194N, and DeltaI16V17/Q156K, trypsinogen, are 10- to 100-fold more active than trypsinogen. The fourth, variant, DeltaI16V17 trypsinogen, is the lone outlier in the correlations;, its ... [(full description)]
About this StructureAbout this Structure
3TGK is a [Protein complex] structure of sequences from [Bos taurus] and [Rattus norvegicus] with CA and SO4 as [ligands]. Active as [Trypsin], with EC number [3.4.21.4]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].
ReferenceReference
The energetic cost of induced fit catalysis: Crystal structures of trypsinogen mutants with enhanced activity and inhibitor affinity., Pasternak A, White A, Jeffery CJ, Medina N, Cahoon M, Ringe D, Hedstrom L, Protein Sci. 2001 Jul;10(7):1331-42. PMID:11420435
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