Zinc Content of Promatrilysin, Matrilysin and the Stromelysin Catalytic Domain

D. Soler, T. Nomizu, W. E. Brown, M. Chen, Qizhuang Ye, H. E. Vanwart, D. S. Auld

Research output: Contribution to journalArticle

22 Citations (Scopus)

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 - Jun 15 1994
Externally publishedYes

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Matrix Metalloproteinase 7
Matrix Metalloproteinase 3
Zinc
Catalytic Domain
Matrix Metalloproteinases
Escherichia coli
Binding Sites
Enzymes
Chelating Agents
Sequence Homology
Cricetulus
Ovary
Metals
Cells
promatrilysin
Proteins

ASJC Scopus subject areas

  • Molecular Biology
  • Biophysics
  • Biochemistry

Cite this

Zinc Content of Promatrilysin, Matrilysin and the Stromelysin Catalytic Domain. / Soler, D.; Nomizu, T.; Brown, W. E.; Chen, M.; Ye, Qizhuang; Vanwart, H. E.; Auld, D. S.

In: Biochemical and Biophysical Research Communications, Vol. 201, No. 2, 15.06.1994, p. 917-923.

Research output: Contribution to journalArticle

Soler, D. ; Nomizu, T. ; Brown, W. E. ; Chen, M. ; Ye, Qizhuang ; Vanwart, H. E. ; Auld, D. S. / Zinc Content of Promatrilysin, Matrilysin and the Stromelysin Catalytic Domain. In: Biochemical and Biophysical Research Communications. 1994 ; Vol. 201, No. 2. pp. 917-923.
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