Literature summary for 3.4.11.10 extracted from

Bienvenue, D.L.; Mathew, R.S.; Ringe, D.; Holz, R.C.
The aminopeptidase from Aeromonas proteolytica can function as an esterase (2002), J. Biol. Inorg. Chem., 7, 129-135.

Search for more literature for 3.4.11.10

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	kinetics and thermodynamics	Vibrio proteolyticus
0.7	-	L-leucine ethyl ester	-	Vibrio proteolyticus

Organism

Organism	UniProt	Comment	Textmining
Vibrio proteolyticus	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.	catalytic mechanism	Vibrio proteolyticus	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-leucine 4-nitroanilide + H2O	-	Vibrio proteolyticus	L-leucine + 4-nitroaniline	-	?
L-leucine ethyl ester + H2O	-	Vibrio proteolyticus	L-leucine + ethanol	-	?
peptides + H2O	-	Vibrio proteolyticus	N-terminal amino acid + peptide(n-1)	-	?

Synonyms

Synonyms	Comment	Organism
AAP	-	Vibrio proteolyticus
Aeromonas proteolytica aminopeptidase	-	Vibrio proteolyticus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
additional information	-	-	Vibrio proteolyticus

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
67	-	peptide	-	Vibrio proteolyticus
96	-	L-leucine ethyl ester	-	Vibrio proteolyticus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
additional information	-	-	Vibrio proteolyticus

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Release 2023.1 (January 2023)