Zinc Content of Promatrilysin, Matrilysin and the Stromelysin Catalytic Domain

Dulce Soler, Tsutomu Nomizu, Willis E. Brown, Ming Chen, Qi Zhuang Ye, Harold E. Van wart, David S. Auld

Research output: Contribution to journalArticle

23 Scopus citations

Abstract

Promatrilysin expressed in Escherichia coli and Chinese hamster ovary cells contains 2.36 ± 0.19 and 2.13 ± 0.39 moles of zinc per mole of protein, respectively, while the activated enzyme contains 2.22 ± 0.21. The catalytic domain of stromelysin-1 expressed in E. coli contains 2.22 ± 0.11. Thus these matrix metalloproteinases contain two metal binding sites at which zinc is bound firmly and possibly a third site at which it is bound weakly. Promatrilysin and matrilysin do not contain significant amounts of Fe, Cu, Mn, or Ni. All known matrix metalloproteinases have a sequence homologous to the zinc binding site of astacin, HExxHxxGxxH, suggesting that one of the zinc sites is catalytic in agreement with the known inhibition of these enzymes by chelators.

Original languageEnglish (US)
Pages (from-to)917-923
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume201
Issue number2
DOIs
StatePublished - Jan 1 1994
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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