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Literature summary for 3.4.11.10 extracted from

  • Chevrier, B.; D'Orchymont, H.
    Vibrio aminopeptidase (2004), Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds), 1, 963-965.
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis Vibrio proteolyticus

Crystallization (Commentary)

Crystallization (Comment) Organism
free Zn-enzyme or enzyme in complex with synthetic inhibitor 4-iodo-D-phenylalanine hydroxamate, X-ray diffraction structure determination and analysis at 1.8 A resolution Vibrio proteolyticus

Inhibitors

Inhibitors Comment Organism Structure
4-iodo-D-phenylalanine hydroxamate
-
Vibrio proteolyticus
D-Leu-4-nitroanilide D-isomers of the substrates inhibit the enzyme Vibrio proteolyticus
D-Val-4-nitroanilide D-isomers of the substrates inhibit the enzyme Vibrio proteolyticus
L-leucinethiol
-
Vibrio proteolyticus
additional information inhibition mechanisms, overview Vibrio proteolyticus
N-mercapto-leucyl-4-nitroanilides
-
Vibrio proteolyticus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Vibrio proteolyticus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ the enzyme is a two-zinc metallopeptidase, zinc-binding involved residues His97, Asp117, Glu152, Asp179, and His256 Vibrio proteolyticus

Organism

Organism UniProt Comment Textmining
Vibrio proteolyticus
-
formerly Aeromonas proteolytica, marine bacterium
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the proenzyme contains a 21-amino acid-signal peptide, and a 84-amino acid N-terminal propeptide, 299 amino acids form the mature protein part, and 100 amino acids form the C-terminal propeptide Vibrio proteolyticus

Purification (Commentary)

Purification (Comment) Organism
extracellular enzyme to homogeneity by ion exchange and hydrophobic interaction chromatography, or by heat treatment at 70°C Vibrio proteolyticus

Reaction

Reaction Comment Organism Reaction ID
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. structure-activity relationship, active site structure involving zinc-binding ligands His97, Asp117, Asp179, Glu151, Glu152, and His256 Vibrio proteolyticus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Leu-4-nitroanilide + H2O
-
Vibrio proteolyticus L-Leu + 4-nitroaniline
-
?
additional information the enzyme prefers substrates with large and hydrophobic N-terminal amino acid residues Vibrio proteolyticus ?
-
?

Subunits

Subunits Comment Organism
monomer 1 * 30000-32000, mature active enzyme Vibrio proteolyticus
More the proenzyme contains a 21-amino acid-signal peptide, and a 84-amino acid N-terminal propeptide, 299 amino acids form the mature protein part, and 100 amino acids form the C-terminal propeptide Vibrio proteolyticus

Synonyms

Synonyms Comment Organism
aminopeptidase Ap1
-
Vibrio proteolyticus
More the enzyme belongs to the peptidase family M28A Vibrio proteolyticus
Vibrio aminopeptidase
-
Vibrio proteolyticus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70
-
several hours, stable Vibrio proteolyticus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0000025 0.000057 N-mercapto-leucyl-4-nitroanilides
-
Vibrio proteolyticus
0.000007
-
L-leucinethiol
-
Vibrio proteolyticus