Substrate specificity of the cell envelope-located proteinase of Lactococcus lactis subsp. lactis NCDO 763.
1. The specificity of the cell envelope-located proteinase of Lactococcus lactis subsp. lactis NCDO 763 towards caseins has been submitted to a statistical study. Positive and negative relations have been evidenced between several amino acids and positions P6 to P'2 of the cleaved bonds. 2. Fragment 1-23 of alpha s1 and oxidized B chain of insulin are well cleaved by the proteinase while CMP (fragment 106-169 of kappa-casein) is a poor substrate. 3. Comparison with other cell envelope-located proteinase has been done. The enzyme of the strain 763 hydrolyses alpha s1-casein and fragment 1-23 of alpha s1-casein as the enzyme of the strain Sk11 and beta-casein as the enzyme of the strain Wg2. 4. The specificity of these proteinases and the comparison of their amino acid sequences let us postulate a more complex substrate binding area for these lactococcal proteinases than for the subtilisin.
Monnet
V
V
Station de Recherches Laitières, I.N.R.A. Jouy en josas, France.
Ley
J P
JP
Gonzàlez
S
S
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002364:Caseins / Q000378:metabolism; D002462:Cell Membrane / Q000201:enzymology; D010450:Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D013294:Lactococcus lactis / Q000201:enzymology*; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid; D013379:Substrate Specificity
D000596:Amino Acids; D002364:Caseins; D010450:Endopeptidases