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

BRENDA support

Literature summary for 3.4.11.22 extracted from

  • Motoshima, H.; Kaminogawa, S.
    Bacillus aminopeptidase I (2004), Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds), 1, 968-970.
No PubMed abstract available

Activating Compound

Activating Compound Comment Organism Structure
tert-butanol 20% activation at 10% at 20-90°C Geobacillus stearothermophilus

Inhibitors

Inhibitors Comment Organism Structure
EDTA 10 mM, no inhibition at pH 8.1, but conversion into the apoenzyme at pH 6.0 Geobacillus stearothermophilus
Urea at 8 M, inhibition of 7% of the enzyme activity with Gly-Leu-Tyr, but 75% of the activity with L-Leu-4-nitroanilide Geobacillus stearothermophilus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane the enzyme exists in a membrane and a soluble variant with slightly differing substrate specificities and thermostabilities Geobacillus stearothermophilus 16020
-
soluble the enzyme exists in a membrane and a soluble variant with slightly differing substrate specificities and thermostabilities Geobacillus stearothermophilus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ binding results in much higher activity compared to Zn2+, Co2+ or Zn2+ is required for maximal activity, metallopeptidase Geobacillus stearothermophilus
Zn2+ binding results in much lower activity compared to Co2+, very tight binding, Co2+ or Zn2+ is required for maximal activity, metallopeptidase Geobacillus stearothermophilus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
36500
-
12 * 36500, heterododecamer with two types of subunits with similar MW, the enzyme shows different hybrid types, overview, the enzymatic activity of the alpha-subunit differs from that of the beta-subunit Geobacillus stearothermophilus
400000
-
sedimentation equilibrium centrifugation analysis Geobacillus stearothermophilus

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme 19fold Geobacillus stearothermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Gly-Leu-Tyr + H2O
-
Geobacillus stearothermophilus Gly + Leu-Tyr
-
?
L-Leu-4-nitroanilide + H2O substrate of the alpha-subunit, but not of the beta-subunit Geobacillus stearothermophilus L-Leu + 4-nitroaniline
-
?
additional information the alpha-subunits hydrolyzes peptides with neutral N-terminal amino acids while the beta-subunit acts on peptides with acidic N-terminal Glu or Asp residues Geobacillus stearothermophilus ?
-
?

Subunits

Subunits Comment Organism
dodecamer 12 * 36500, heterododecamer with two types of subunits with similar MW, the enzyme shows different hybrid types, overview, the enzymatic activity of the alpha-subunit differs from that of the beta-subunit Geobacillus stearothermophilus

Synonyms

Synonyms Comment Organism
API
-
Geobacillus stearothermophilus
Bacillus aminopeptidase I
-
Geobacillus stearothermophilus
More the enzyme belongs to the peptidase family M42 Geobacillus stearothermophilus
thermophilic aminopeptidase
-
Geobacillus stearothermophilus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
-
with substrate Gly-Leu-Tyr Geobacillus stearothermophilus
90
-
with substrate L-Leu-4-nitroanilide Geobacillus stearothermophilus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
the apo- and cobalt-free enzyme is thermolabile Geobacillus stearothermophilus
80
-
loss of 20% activity within 30 min, stable for several hours Geobacillus stearothermophilus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 8 with substrate L-Leu-4-nitroanilide Geobacillus stearothermophilus
9.2 9.5 with substrate Gly-Leu-Tyr Geobacillus stearothermophilus