Zinc content of promatrilysin, matrilysin and the stromelysin catalytic domain.
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.
Soler
D
D
Center for Biochemical and Biophysical Sciences and Medicine, Harvard Medical School, Boston, MA.
Nomizu
T
T
Brown
W E
WE
Chen
M
M
Ye
Q Z
QZ
Van Wart
H E
HE
Auld
D S
DS
D000595:Amino Acid Sequence; D000818:Animals; D001051:Apoenzymes / Q000096:biosynthesis / Q000737:chemistry*; D001665:Binding Sites; D016466:CHO Cells; D003001:Cloning, Molecular; D006224:Cricetinae; D004792:Enzyme Precursors / Q000096:biosynthesis / Q000737:chemistry*; D004926:Escherichia coli; D006801:Humans; D019278:Matrix Metalloproteinase 3; D020783:Matrix Metalloproteinase 7; D008666:Metalloendopeptidases / Q000096:biosynthesis / Q000737:chemistry*; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D014162:Transfection; D015032:Zinc / Q000032:analysis*
D001051:Apoenzymes; D004792:Enzyme Precursors; D011994:Recombinant Proteins; D008666:Metalloendopeptidases; D019278:Matrix Metalloproteinase 3; D020783:Matrix Metalloproteinase 7; D015032:Zinc