| Literature DB >> 8955363 |
A Lichte1, H Kolkenbrock, H Tschesche.
Abstract
A truncated form of the membrane-type matrix metalloproteinase-1 [(Ala21-Ile318)proMT1-MMP] lacking the hemopexin-like and trans-membrane domain was produced in E. coli. We demonstrate that the recombinant proenzyme was autoproteolytically processed to a fully active catalytic domain with N-terminal Ile114. The catalytic domain of MT1-MMP initiated the activation of progelatinase A and progelatinase A complexed with tissue inhibitor of metalloproteinases-2 (TIMP-2). As a typical soluble metalloproteinase it was able to cleave physiologic as well as synthetic substrates. Our kinetic data demonstrate that TIMP-2 is a potent inhibitor for the recombinant enzyme.Entities:
Mesh:
Substances:
Year: 1996 PMID: 8955363 DOI: 10.1016/s0014-5793(96)01206-9
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124