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Literature summary for 3.4.11.10 extracted from

  • Bzymek, K.P.; D'Souza, V.M.; Chen, G.; Campbell, H.; Mitchell, A.; Holz, R.C.
    Function of the signal peptide and N- and C-terminal propeptides in the leucine aminopeptidase from Aeromonas proteolytica (2004), Protein Expr. Purif., 37, 294-305.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene AAP, overexpression of different forms of AAP in Escherichia coli, i.e as MBP-fusion protein, with or without N- and/or C-terminal propeptides, or with the native leader sequence of the enzyme Vibrio proteolyticus

Inhibitors

Inhibitors Comment Organism Structure
additional information the propeptides internally inhibits the enzyme in the 54 kDa zymogen in a cooperative inhibitory interaction Vibrio proteolyticus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics of different native and recombinant enzyme forms, overview Vibrio proteolyticus
0.0106
-
L-Leu-4-nitroanilide pH 8.0, 25°C, mature wild-type enzyme Vibrio proteolyticus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the enzyme contains a signal peptide sequence for protein secretion Vibrio proteolyticus
-
-
periplasm
-
Vibrio proteolyticus
-
-
soluble
-
Vibrio proteolyticus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ AAP is a metalloenzyme containing two Zn2+ per enzyme molecule Vibrio proteolyticus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
32000
-
processed enzyme form Vibrio proteolyticus
43000
-
unprocessed enzyme form Vibrio proteolyticus

Organism

Organism UniProt Comment Textmining
Vibrio proteolyticus Q01693 i.e. Vibrio proteolyticus
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the enzyme contains N- and C-terminal propeptides, processing of a 54 kDa zymogen to the 32 kDa mature enzyme, overview, modeling of the processing of wild-type enzyme, mechanism Vibrio proteolyticus

Purification (Commentary)

Purification (Comment) Organism
native periplasmic enzyme by ion exchange and hydrophobic interaction chromatography, recombinant MBP-fusion enzyme and recombinant extracellular or mature intracellular wild-type enzyme from Escherichia coli by amylose affinity chromatography and ultrafiltration, and by ammonium sulfate fractionation, dialysis, hydrophobic interaction and anion exchange chromatography, and a second hydrophobic interaction chromatography step Vibrio proteolyticus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
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 shows broad substrate specificity Vibrio proteolyticus ?
-
?

Subunits

Subunits Comment Organism
? x * 44000-46300, unprocessed periplasmic enzyme, SDS-PAGE, x * 31000-32000, processed extracellular and periplasmic enzyme, SDS-PAGE, x * 39000-40000, unprocessed extracellular enzyme, SDS-PAGE,x * 51000-52000, unprocessed recombinant enzyme, SDS-PAGE Vibrio proteolyticus

Synonyms

Synonyms Comment Organism
AAP
-
Vibrio proteolyticus
leucine aminopeptidase
-
Vibrio proteolyticus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Vibrio proteolyticus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.6
-
L-Leu-4-nitroanilide pH 8.0, 25°C, mature wild-type enzyme Vibrio proteolyticus
71.33
-
L-Leu-4-nitroanilide pH 8.0, 25°C, mature wild-type enzyme Vibrio proteolyticus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Vibrio proteolyticus