[Interaction of collagenases with certain peptide substrates and inhibitors].
Interactions of collagenases I and II (clostridiopeptidases) from Clostridium histolyticum with hexapeptide substrates in which some L-proline residues are replaced by their D-analogues, as well as with the tripeptide chloromethyl ketone Z-Gly-Pro-Gly-CH2Cl were studied. A role of stereochemistry of the amino acid residues in the substrate was established and differences between the collagenases, with regard to their specific requirements to substrates, were revealed. The tripeptide chloromethyl ketone is shown to be a specific collagenase inhibitor modifying at the substrate-binding site in the active centre of these enzymes, most likely lysine residues.
Solov'eva
N I
NI
Balaevskaia
T O
TO
Finogenova
M P
MP
Shibnev
V A
VA
D000590:Amino Acid Chloromethyl Ketones / Q000494:pharmacology; D000595:Amino Acid Sequence; D001665:Binding Sites; D003013:Clostridium / Q000201:enzymology; D017364:Collagenases / Q000378:metabolism*; D061965:Matrix Metalloproteinase Inhibitors; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry / Q000378:metabolism*; D013379:Substrate Specificity
D000590:Amino Acid Chloromethyl Ketones; D061965:Matrix Metalloproteinase Inhibitors; D009842:Oligopeptides; D017364:Collagenases
Vzaimodeĭstvie kollagenaz s nekotorymi peptidnymi substratami i ingibitorami.