Literature summary for 3.4.11.10 extracted from

Chi, M.C.; Chou, W.M.; Wang, C.H.; Chen, W.; Hsu, W.H.; Lin, L.L.
Generating oxidation-resistant variants of Bacillus kaustophilus leucine aminopeptidase by substitution of the critical methionine residues with leucine (2004), Antonie van Leeuwenhoek, 86, 355-362.

Search for more literature for 3.4.11.10

Cloned(Commentary)

Cloned (Comment)	Organism
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain M15	Geobacillus kaustophilus

Protein Variants

Protein Variants	Comment	Organism
M224L	site-directed mutagenesis, the mutant enzyme shows similar oxidative stability with H2O2 as the wild-type enzyme	Geobacillus kaustophilus
M282L	site-directed mutagenesis, the mutant enzyme shows over 43% reduced activity compared to the wild-type enzyme	Geobacillus kaustophilus
M285L	site-directed mutagenesis, the mutant enzyme shows over 43% reduced activity compared to the wild-type enzyme	Geobacillus kaustophilus
M289L	site-directed mutagenesis, the mutant enzyme shows over 43% reduced activity compared to the wild-type enzyme	Geobacillus kaustophilus
M299L	site-directed mutagenesis, the mutant enzyme shows increased oxidative stability with H2O2 compared to the wild-type enzyme	Geobacillus kaustophilus
M321L	site-directed mutagenesis, the mutant enzyme shows over 43% reduced activity and reduced oxidative stability with H2O2 compared to the wild-type enzyme	Geobacillus kaustophilus
M400L	site-directed mutagenesis, the mutant enzyme shows 191% increased activity and increased catalytic efficiency compared to the wild-type enzyme	Geobacillus kaustophilus
M426L	site-directed mutagenesis, the mutant enzyme shows 79% increased activity and increased catalytic efficiency compared to the wild-type enzyme	Geobacillus kaustophilus
M445L	site-directed mutagenesis, the mutant enzyme shows 313% increased activity and increased catalytic efficiency compared to the wild-type enzyme	Geobacillus kaustophilus
M485L	site-directed mutagenesis, the mutant enzyme shows 103% increased activity and increased catalytic efficiency compared to the wild-type enzyme	Geobacillus kaustophilus

Inhibitors

Inhibitors	Comment	Organism	Structure
H2O2	the enzyme is sensitive against oxidative damage by H2O2	Geobacillus kaustophilus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	kinetics of wild-type and methionine mutant enzymes, overview	Geobacillus kaustophilus
2.1	-	L-Leu-4-nitroanilide	pH 8.0, 55°C, recombinant wild-type enzyme	Geobacillus kaustophilus

Organism

Organism	UniProt	Comment	Textmining
Geobacillus kaustophilus	-	-	-

Oxidation Stability

Oxidation Stability	Organism
the enzyme is sensitive against oxidative damage by H2O2	Geobacillus kaustophilus

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain M15 by nickel affinity chromatography	Geobacillus kaustophilus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
91.6	-	purified recombinant wild-type enzyme	Geobacillus kaustophilus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-Leu-4-nitroanilide + H2O	-	Geobacillus kaustophilus	L-Leu + 4-nitroaniline	-	?

Synonyms

Synonyms	Comment	Organism
LAP	-	Geobacillus kaustophilus
leucine aminopeptidase	-	Geobacillus kaustophilus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
55	-	assay at	Geobacillus kaustophilus

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
6.31	-	L-Leu-4-nitroanilide	pH 8.0, 55°C, recombinant wild-type enzyme	Geobacillus kaustophilus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Geobacillus kaustophilus

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Release 2023.1 (January 2023)