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Literature summary for 3.4.11.9 extracted from

  • Mc Donnell, M.; Fitzgerald, R.; Fhaolain, I.N.; Jennings, P.V.; O'Cuinn, G.
    Purification and characterization of aminopeptidase P from Lactococcus lactis subsp. cremoris (1997), J. Dairy Res., 64, 399-407.
    View publication on PubMed
Search for more literature for 3.4.11.9

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline
-
 Lactococcus lactis
8-hydroxyquinoline
-
 Lactococcus lactis
amastatin
-
 Lactococcus lactis
Ba2+
-
 Lactococcus lactis
bestatin
-
 Lactococcus lactis
EDTA
-
 Lactococcus lactis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.9
-
 Leu-Pro-Pro
-
 Lactococcus lactis
1.2
-
 Tyr-Pro-Phe
-
 Lactococcus lactis
1.4
-
 Arg-Pro-Pro
-
 Lactococcus lactis
1.4
-
 Tyr-Pro-Phe-Pro-Gly-Pro-Ile
-
 Lactococcus lactis
1.6
-
 Tyr-Pro-Phe-Pro-Gly
-
 Lactococcus lactis

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
 Lactococcus lactis 5737
-

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ stimulates Lactococcus lactis
Mn2+ 1 mM, 6.8fold stimulates Lactococcus lactis
Ni2+ 1 mM, 26% increase in activity Lactococcus lactis
Zn2+ 1 mM, 2fold increase in activity Lactococcus lactis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
 1 * 40000, SDS-PAGE Lactococcus lactis
41600
-
 gel filtration Lactococcus lactis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Lactococcus lactis aminopeptidase P appears to be an important enzyme for debittering of casein-derived peptides ?
-
 ?

Organism

Organism UniProt Comment Textmining
Lactococcus lactis
-
 subsp. cremonis AM2
-

Purification (Commentary)

Purification (Comment) Organism
-
 Lactococcus lactis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.343
-
-
 Lactococcus lactis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Ala-Pro-Gly + H2O
-
 Lactococcus lactis Ala + Pro-Gly
-
 ?
Arg-Pro-Lys-Pro + H2O
-
 Lactococcus lactis ?
-
 ?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Leu-Gly-Met-NH2 + H2O
-
 Lactococcus lactis ?
-
 ?
Arg-Pro-Pro + H2O
-
 Lactococcus lactis Arg + Pro-Pro
-
 ?
Arg-Pro-Pro-Gly-Phe-Ser + H2O
-
 Lactococcus lactis ?
-
 ?
Arg-Pro-Pro-Gly-Phe-Ser-Pro + H2O
-
 Lactococcus lactis ?
-
 ?
Asp-Pro-Gly-Phe-Tyr + H2O
-
 Lactococcus lactis ?
-
 ?
Gly-Pro-Arg-Pro + H2O
-
 Lactococcus lactis ?
-
 ?
Gly-Pro-Gly-Gly + H2O
-
 Lactococcus lactis ?
-
 ?
Leu-Ala-Pro + H2O
-
 Lactococcus lactis Leu + Ala-Pro
-
 ?
Leu-Pro-Pro + H2O
-
 Lactococcus lactis Leu + Pro-Pro
-
 ?
Lys-Pro-Arg + H2O
-
 Lactococcus lactis Lys + Pro-Arg
-
 ?
additional information the enzyme removes the N-terminal amino acid from peptides only where Pro, and in one case Ala, is present in the penultimate position. No hydrolysis of dipeptides even when Pro is present in the C-terminal position or when either N-termial Pro or pyroglutamate is present preceeding a Pro residue in the penultimate position of longer peptides Lactococcus lactis ?
-
 ?
additional information aminopeptidase P appears to be an important enzyme for debittering of casein-derived peptides Lactococcus lactis ?
-
 ?
Tyr-Pro-Phe + H2O
-
 Lactococcus lactis ?
-
 ?
Tyr-Pro-Phe-Pro + H2O
-
 Lactococcus lactis ?
-
 ?
Tyr-Pro-Phe-Pro-Gly + H2O
-
 Lactococcus lactis ?
-
 ?
Tyr-Pro-Phe-Pro-Gly-Pro-Ile + H2O
-
 Lactococcus lactis ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 40000, SDS-PAGE Lactococcus lactis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
 Lactococcus lactis