title: An aminopeptidase P from Lactococcus lactis with original specificity.
abstract: An aminopeptidase P (E.C. 3.4.11.9) that cleaves the Arg-1-Pro-2 bond of bradykinin has been isolated for the first time from Lactococcus lactis. The peptidase was purified to homogeneity in a 3-step procedure and characterized. It is a monomeric metalloenzyme with a 43 kDa molecular mass, activated by Mn2+ and inhibited by DTT. It differs from the majority of aminopeptidases P already described by displaying a specificity for X-Pro-Pro N-terminal and probably an extended binding site that could accommodate amino acid residues beyond the P'2 position of the substrate.
authors.affiliation: Station de Recherches Laitières, I.N.R.A., Jouy en Josas, France.
authors.forename: I
authors.initials: I
authors.lastname: Mars
authors.forename: V
authors.initials: V
authors.lastname: Monnet
mesh_terms: D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000737:chemistry / Q000302:isolation & purification*; D001665:Binding Sites; D002364:Caseins / Q000378:metabolism; D013294:Lactococcus lactis / Q000201:enzymology*; D008969:Molecular Sequence Data; D013379:Substrate Specificity
chemical_list: D002364:Caseins; D000626:Aminopeptidases; C022750:X-Pro aminopeptidase