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Literature summary extracted from

  • Blinkovsky, A.M.; Byun, T.; Brown, K.M.; Golightly, E.J.; Klotz, A.V.
    A non-specific aminopeptidase from Aspergillus (2000), Biochim. Biophys. Acta, 1480, 171-181.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.11.22 DNA and amino acid sequence determination and analysis, functional overexpression in Fusarium venenatum and Aspergillus oryzae Aspergillus oryzae

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.11.22 EDTA 10% inhibition at 1 mM Aspergillus oryzae
3.4.11.22 o-phenanthroline 91% inhibition at 1 mM Aspergillus oryzae
3.4.11.22 PMSF 5% inhibition at 1 mM Aspergillus oryzae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.11.22 1.5
-
 Glu-4-nitroanilide pH 7.5, 21°C, recombinant enzyme Aspergillus oryzae
3.4.11.22 3.5
-
 Ala-4-nitroanilide pH 7.5, 21°C, recombinant enzyme Aspergillus oryzae
3.4.11.22 7
-
 Leu-4-nitroanilide pH 7.5, 21°C, recombinant enzyme Aspergillus oryzae
3.4.11.22 9
-
 Lys-4-nitroanilide pH 7.5, 21°C, recombinant enzyme Aspergillus oryzae
3.4.11.22 13
-
 Val-4-nitroanilide pH 7.5, 21°C, recombinant enzyme Aspergillus oryzae
3.4.11.22 15
-
 L-Pro-4-nitroanilide pH 7.5, 21°C, recombinant enzyme Aspergillus oryzae
3.4.11.22 51
-
 Ile-4-nitroanilide pH 7.5, 21°C, recombinant enzyme Aspergillus oryzae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.11.22 extracellular secretion to the culture medium Aspergillus oryzae
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.11.22 Zn2+ required, metalloenzyme, bound at the active site, enzyme contains the HEXXH motif Aspergillus oryzae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.11.22 51950
-
 x * 56000, deglycosylated recombinant enzyme, SDS-PAGE, x * 51950, mature enzyme, amino acid sequence calculation Aspergillus oryzae
3.4.11.22 56000
-
 x * 56000, deglycosylated recombinant enzyme, SDS-PAGE, x * 51950, mature enzyme, amino acid sequence calculation Aspergillus oryzae

Organism

EC Number Organism UniProt Comment Textmining
3.4.11.22 Aspergillus oryzae
-
 strain ATCC 20386
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.11.22 glycoprotein N-glycosylation Aspergillus oryzae

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.11.22 from culture supernatant Aspergillus oryzae

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.11.22 additional information
-
 reaction velocity in descending order with Xaa being Pro, Ala, Leu, Gly, and Glu Aspergillus oryzae
3.4.11.22 4.12
-
 with Leu-4-nitroanilide as substrate, measurement of absorption Aspergillus oryzae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.11.22 Ala-4-nitroanilide + H2O
-
 Aspergillus oryzae Ala + 4-nitroaniline
-
 ?
3.4.11.22 Ala-Ala-Pro-Tyr-Lys-amide + H2O
-
 Aspergillus oryzae Ala + Ala-Pro-Tyr-Lys-amide
-
 ?
3.4.11.22 Glu-4-nitroanilide + H2O
-
 Aspergillus oryzae Glu + 4-nitroaniline
-
 ?
3.4.11.22 Glu-Ala-Pro-Tyr-Lys-amide + H2O
-
 Aspergillus oryzae Glu + Ala-Pro-Tyr-Lys-amide
-
 ?
3.4.11.22 Gly-Ala-Pro-Tyr-Lys-amide + H2O
-
 Aspergillus oryzae Gly + Ala-Pro-Tyr-Lys-amide
-
 ?
3.4.11.22 Ile-4-nitroanilide + H2O
-
 Aspergillus oryzae Ile + 4-nitroaniline
-
 ?
3.4.11.22 L-Pro-4-nitroanilide + H2O
-
 Aspergillus oryzae L-Pro + 4-nitroaniline
-
 ?
3.4.11.22 Leu-4-nitroanilide + H2O best Xaa-4-nitroanilide substrate Aspergillus oryzae Leu + 4-nitroaniline
-
 ?
3.4.11.22 Leu-Ala-Pro-Tyr-Lys-amide + H2O
-
 Aspergillus oryzae Leu + Ala-Pro-Tyr-Lys-amide
-
 ?
3.4.11.22 Lys-4-nitroanilide + H2O
-
 Aspergillus oryzae Lys + 4-nitroaniline
-
 ?
3.4.11.22 additional information non-specific enzyme, broad substrate spectrum, but no hydrolysis of Xaa-Pro bonds Aspergillus oryzae ?
-
 ?
3.4.11.22 Pro-Ala-Pro-Tyr-Lys-amide + H2O best pentapeptide substrate Aspergillus oryzae Pro + Ala-Pro-Tyr-Lys-amide
-
 ?
3.4.11.22 Val-4-nitroanilide + H2O
-
 Aspergillus oryzae Val + 4-nitroaniline
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.11.22 ? x * 56000, deglycosylated recombinant enzyme, SDS-PAGE, x * 51950, mature enzyme, amino acid sequence calculation Aspergillus oryzae

Synonyms

EC Number Synonyms Comment Organism
3.4.11.22 aminopeptidase II
-
 Aspergillus oryzae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.11.22 55
-
-
 Aspergillus oryzae

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.11.22 70
-
 20 min, 65% residual activity, compared to the activity at 37°C Aspergillus oryzae
3.4.11.22 75
-
 20 min, 46% residual activity, compared to the activity at 37°C Aspergillus oryzae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.11.22 additional information
-
 Pro-Ala-Pro-Tyr-Lys-amide pH 7.5, 21°C, recombinant enzyme Aspergillus oryzae
3.4.11.22 0.08
-
 L-Pro-4-nitroanilide pH 7.5, 21°C, recombinant enzyme Aspergillus oryzae
3.4.11.22 0.1
-
 Val-4-nitroanilide pH 7.5, 21°C, recombinant enzyme Aspergillus oryzae
3.4.11.22 0.13
-
 Glu-4-nitroanilide pH 7.5, 21°C, recombinant enzyme Aspergillus oryzae
3.4.11.22 0.18
-
 Ile-4-nitroanilide pH 7.5, 21°C, recombinant enzyme Aspergillus oryzae
3.4.11.22 0.68
-
 Ala-4-nitroanilide pH 7.5, 21°C, recombinant enzyme Aspergillus oryzae
3.4.11.22 0.72
-
 Glu-Ala-Pro-Tyr-Lys-amide pH 7.5, 21°C, recombinant enzyme Aspergillus oryzae
3.4.11.22 0.88
-
 Gly-Ala-Pro-Tyr-Lys-amide pH 7.5, 21°C, recombinant enzyme Aspergillus oryzae
3.4.11.22 1.8
-
 Lys-4-nitroanilide pH 7.5, 21°C, recombinant enzyme Aspergillus oryzae
3.4.11.22 3.13
-
 Ala-Ala-Pro-Tyr-Lys-amide pH 7.5, 21°C, recombinant enzyme Aspergillus oryzae
3.4.11.22 3.13
-
 Leu-Ala-Pro-Tyr-Lys-amide pH 7.5, 21°C, recombinant enzyme Aspergillus oryzae
3.4.11.22 3.5
-
 Leu-4-nitroanilide pH 7.5, 21°C, recombinant enzyme Aspergillus oryzae
3.4.11.22 3.67
-
 Leu-Ala-Pro-Tyr-Lys-amide pH 7.5, 21°C, recombinant enzyme Aspergillus oryzae
3.4.11.22 4.34
-
 Ala-Ala-Pro-Tyr-Lys-amide pH 7.5, 21°C, recombinant enzyme Aspergillus oryzae
3.4.11.22 6.08
-
 Ala-4-nitroanilide pH 7.5, 21°C, recombinant enzyme Aspergillus oryzae
3.4.11.22 6.08
-
 Gly-Ala-Pro-Tyr-Lys-amide pH 7.5, 21°C, recombinant enzyme Aspergillus oryzae
3.4.11.22 6.08
-
 Glu-Ala-Pro-Tyr-Lys-amide pH 7.5, 21°C, recombinant enzyme Aspergillus oryzae
3.4.11.22 6.17
-
 Pro-Ala-Pro-Tyr-Lys-amide pH 7.5, 21°C, recombinant enzyme Aspergillus oryzae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.11.22 9.5
-
-
 Aspergillus oryzae