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Protein Science, Vol 1, Issue 8 1007-1013, Copyright © 1992 by Cold Spring Harbor Laboratory Press

ARTICLE

Mapping of the catalytic site of CHO-t-PA and the t-PA variant BM 06.022 by synthetic inhibitors and substrates

J. STURZEBECHER, U. NEUMANN, U. KOHNERT, G. B. KRESSE and S. FISCHER
Institute of Pharmacology & Toxicology, Medical Academy Erfurt, D-(0)-5010 Erfurt, Germany

BM 06.022 is a t-PA deletion variant that is produced as inactive inclusion bodies in Escherichia coli and transformed into the native form by an in vitro refolding process. Until now, no X-ray and NMR structures of BM 06.022 were available. Therefore a detailed kinetic analysis of the hydrolysis of peptide substrates and of the inhibition by several benzamidine-derived inhibitors was carried out in order to assess that the active site region of the protease domain of BM 06.022 is correctly structured in comparison with t-PA. Our data reveal that the single-chain as well as the two-chain form of BM 06.022 and native t-PA are similar in catalytic and in inhibitor binding properties. This indicates that the active site and the highly complex rearrangement of t-PA upon cleavage of the Arg(275)-Ile(276) bond are maintained in BM 06.022.
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