Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.11.2 extracted from

  • Yamauchi, Y.; Ejiri, Y.; Tanaka, K.
    Purification of an aminopeptidase preferentially releasing N-terminal alanine from cucumber leaves and its identification as a plant aminopeptidase N (2001), Biosci. Biotechnol. Biochem., 65, 2802-2805.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline complete inhibition Cucumis sativus
bestatin strong inhibition Cucumis sativus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.092
-
L-Lys-2-naphthylamide pH 8.0, 37°C Cucumis sativus
0.099
-
L-Arg-2-naphthylamide pH 8.0, 37°C Cucumis sativus
0.197
-
L-Ala-2-naphthylamide pH 8.0, 37°C Cucumis sativus
0.31
-
L-Met-4-nitroanilide pH 8.0, 37°C Cucumis sativus
0.45
-
L-Ala-4-nitroanilide pH 8.0, 37°C Cucumis sativus
1.72
-
Gly-4-nitroanilide pH 8.0, 37°C Cucumis sativus
7.83
-
L-Ser-2-naphthylamide pH 8.0, 37°C Cucumis sativus
9.23
-
L-Leu-4-nitroanilide pH 8.0, 37°C Cucumis sativus

Metals/Ions

Metals/Ions Comment Organism Structure
additional information metallopeptidase Cucumis sativus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
95000
-
2 * 95000, SDS-PAGE Cucumis sativus
200000
-
gel filtration Cucumis sativus

Organism

Organism UniProt Comment Textmining
Cucumis sativus
-
var. suyo
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme 365fold from leaves by ammonium sulfate fractionation, ion exchange chromatography, hydrophobic interaction chromatography, hydroxyapatite chromatography, again ion exchange chromatography, and gel filtration Cucumis sativus

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Cucumis sativus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.86
-
purified enzyme, substrate L-Ala-2-naphthylamide Cucumis sativus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Gly-4-nitroanilide + H2O
-
Cucumis sativus Gly + 4-nitroaniline
-
?
L-Ala-2-naphthylamide + H2O best substrate Cucumis sativus L-Ala + 2-naphthylamine
-
?
L-Ala-4-nitroanilide + H2O
-
Cucumis sativus L-Ala + 4-nitroaniline
-
?
L-Arg-2-naphthylamide + H2O
-
Cucumis sativus L-Arg + 2-naphthylamine
-
?
L-Leu-4-nitroanilide + H2O very low activity Cucumis sativus L-Leu + 4-nitroaniline
-
?
L-Lys-2-naphthylamide + H2O
-
Cucumis sativus L-Lys + 2-naphthylamine
-
?
L-Met-4-nitroanilide + H2O
-
Cucumis sativus L-Met + 4-nitroaniline
-
?
L-Ser-2-naphthylamide + H2O low activity Cucumis sativus L-Ser + 2-naphthylamine
-
?
additional information the enzyme prefers substrates with N-terminal L-Ala residues Cucumis sativus ?
-
?

Subunits

Subunits Comment Organism
dimer 2 * 95000, SDS-PAGE Cucumis sativus

Synonyms

Synonyms Comment Organism
APase2
-
Cucumis sativus
More the enzyme probably belongs to the M1 family of peptidases Cucumis sativus
plant aminopeptidase N
-
Cucumis sativus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Cucumis sativus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.052 2.1 L-Met-4-nitroanilide pH 8.0, 37°C Cucumis sativus
6.7
-
L-Leu-4-nitroanilide pH 8.0, 37°C Cucumis sativus
9.72
-
L-Met-4-nitroanilide pH 8.0, 37°C Cucumis sativus
19.3
-
L-Arg-2-naphthylamide pH 8.0, 37°C Cucumis sativus
23.1
-
L-Lys-2-naphthylamide pH 8.0, 37°C Cucumis sativus
34.3
-
L-Ala-4-nitroanilide pH 8.0, 37°C Cucumis sativus
45.2
-
Gly-4-nitroanilide pH 8.0, 37°C Cucumis sativus
87
-
L-Ser-2-naphthylamide pH 8.0, 37°C Cucumis sativus
149
-
L-Ala-2-naphthylamide pH 8.0, 37°C Cucumis sativus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8 9
-
Cucumis sativus