Literature summary for 3.4.11.1 extracted from

Laslo, A.C.; Ganea, E.; Obinger, C.
Refolding of hexameric porcine leucine aminopeptidase using a cationic detergent and dextrin-10 as artificial chaperones (2009), J. Biotechnol., 140, 162-168.

General Stability

General Stability	Organism
hexameric LAP is almost completely inactivated, showing 0.6% residual activity, by incubation with 2.5 M GuHCl and 40 mM DTT for 3 h at room temperature	Sus scrofa

Inhibitors

Inhibitors	Comment	Organism	Structure
guanidinium hydrochloride	hexameric LAP is almost completely inactivated, showing 0.6% residual activity, by incubation with 2.5 M GuHCl and 40 mM DTT for 3 h at room temperature	Sus scrofa

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
14.2	-	L-leucylamide	native enzyme, pH 8.0, 25°C	Sus scrofa

Organism

Organism	UniProt	Comment	Textmining
Sus scrofa	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
guanidinium hydrochloride-denatured hexameric leucine aminopeptidase is efficiently refolded by using the cationic detergent cetyltrimethylammonium bromide and the linear polysaccharide dextrin-10 as artificial chaperones leading to 92% of fully active and correct folded LAP, method and kinetics, overview. Recovery of the enzymatic activity using methyl-beta-cyclodextrin was calculated to be 37%, 55%, 64% and 72% after 1 h, 5 h, 10 h and 20 h of incubation, respectively	Sus scrofa

Renatured (Comment)

Organism

guanidinium hydrochloride-denatured hexameric leucine aminopeptidase is efficiently refolded by using the cationic detergent cetyltrimethylammonium bromide and the linear polysaccharide dextrin-10 as artificial chaperones leading to 92% of fully active and correct folded LAP, method and kinetics, overview. Recovery of the enzymatic activity using methyl-beta-cyclodextrin was calculated to be 37%, 55%, 64% and 72% after 1 h, 5 h, 10 h and 20 h of incubation, respectively

Sus scrofa

Source Tissue

Source Tissue	Comment	Organism	Textmining
commercial preparation	-	Sus scrofa	-
kidney	-	Sus scrofa	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-leucylamide + H2O	-	Sus scrofa	L-leucine + NH3	-	?

Subunits

Subunits	Comment	Organism
hexamer	oligomeric structure, overview	Sus scrofa

Synonyms

Synonyms	Comment	Organism
leucine aminopeptidase	-	Sus scrofa

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Sus scrofa

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
112	-	L-leucylamide	native enzyme, pH 8.0, 25°C	Sus scrofa

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Sus scrofa