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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

12 Issues per year


IMPACT FACTOR 2015: 2.710
Rank 142 out of 289 in category Biochemistry & Molecular Biology in the 2015 Thomson Reuters Journal Citation Report/Science Edition

SCImago Journal Rank (SJR) 2015: 1.607
Source Normalized Impact per Paper (SNIP) 2015: 0.751
Impact per Publication (IPP) 2015: 2.609

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ISSN
1437-4315
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Volume 385, Issue 6 (Jun 2004)

Issues

Human kallikrein 6 activity is regulated via an autoproteolytic mechanism of activation/inactivation

A. Bayés / T. Tsetsenis / S. Ventura / J. Vendrell / F.X. Aviles / G. Sotiropoulou
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2004.061

Abstract

Human kallikrein 6 (protease M/zyme/neurosin) is a serine protease that has been suggested to be a serum biomarker for ovarian cancer and may also be involved in pathologies of the CNS. The precursor form of human kallikrein 6 (proh-K6) was overexpressed in Pichia pastoris and found to be autoprocessed to an active but unstable mature enzyme that subsequently yielded the inactive, self-cleavage product, hK6 (D[81]K[244]). Site-directed mutagenesis was used to investigate the basis for the intrinsic catalytic activity and the activation mechanism of pro-hK6. A single substitution R[80]->Q stabilized the activity of the mature enzyme, while substitution of the active site serine (S[197]->A) resulted in complete loss of hK6 proteolytic activity and facilitated protein production. Our data suggest that the enzymatic activity of hK6 is regulated by an autoactivation/autoinactivation mechanism. Mature hK6 displayed a trypsin-like activity against synthetic substrates and human plasminogen was identified as a putative physiological substrate for hK6, as specific cleavage at the plasminogen internal bond S[460]-V[461] resulted in the generation of angiostatin, an endogenous inhibitor of angiogenesis and metastatic growth.

About the article

Published Online: 2005-06-01

Published in Print: 2004-06-07


Citation Information: Biological Chemistry, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2004.061. Export Citation

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