Interstitial collagenase
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.24 Metalloendopeptidases > 3.4.24.7 interstitial collagenase
Oligopeptidase A is a zinc metalloendopeptidase from Escherichia coli and Salmonella typhimurium, in peptidase family M3 (thimet oligopeptidase family), differing from thimet oligopeptidase in lacking thiol activation. It hydrolyzes oligopeptides broadly; Gly or Ala commonly occur as P1 or P1' residues, but more distant residues matter, as shown by cleavage of Z-Gly-Pro-Gly-/-Gly-Pro-Ala but not Z-(Gly)5. In the bacterial periplasm it processes oligopeptides. It features an M3-family zinc catalytic chamber.
Oligopeptidase A is a zinc metalloendopeptidase from Escherichia coli and Salmonella typhimurium, in peptidase family M3 (thimet oligopeptidase family), differing from thimet oligopeptidase in lacking thiol activation. It hydrolyzes oligopeptides broadly; Gly or Ala commonly occur as P1 or P1' residues, but more distant residues matter, as shown by cleavage of Z-Gly-Pro-Gly-/-Gly-Pro-Ala but not Z-(Gly)5. In the bacterial periplasm it processes oligopeptides. It features an M3-family zinc catalytic chamber.
References:
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