3.4.11.10: bacterial leucyl aminopeptidase
This is an abbreviated version!
For detailed information about bacterial leucyl aminopeptidase, go to the full flat file.
Word Map on EC 3.4.11.10
Reaction
release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids =
Synonyms
AAP, Aeromonas proteolytica aminopeptidase, Aminopeptidase, aminopeptidase A, aminopeptidase A (bacteria), aminopeptidase Ap1, aminopeptidase II, AP-II, API, APII, AVP, bacterial leucine aminopeptidase, bacterial M17 aminopeptidase, BSAP, Bsu aminopeptidase, BsuAP, CGase, cysteinylglycinase, double-zinc aminopeptidase, extracellular aminopeptidase, FgLAP, HpM17AP, LAP, LAPII, leucine aminopeptidase, leucine aminopeptidase II, leucine APN, Leucyl aminopeptidase, M17 aminopeptidase, M17 metallo-aminopeptidase, More, MtLAP, PepA, Peptidase A, pepZ, PhpA, ribosomal-bound aminopeptidase, rLAP55, Rv2213, SSAP, TAP, TH-2, thermophilic aminopeptidase, thermostable leucine aminopeptidase, Vibrio aminopeptidase, VpAP, ywaD
ECTree
3.4.11.10 bacterial leucyl aminopeptidaseAdvanced search results
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results (Engineering
Engineering on EC 3.4.11.10 - bacterial leucyl aminopeptidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
M224L
-
site-directed mutagenesis, the mutant enzyme shows similar oxidative stability with H2O2 as the wild-type enzyme
M282L
-
site-directed mutagenesis, the mutant enzyme shows over 43% reduced activity compared to the wild-type enzyme
M285L
-
site-directed mutagenesis, the mutant enzyme shows over 43% reduced activity compared to the wild-type enzyme
M289L
-
site-directed mutagenesis, the mutant enzyme shows over 43% reduced activity compared to the wild-type enzyme
M299L
-
site-directed mutagenesis, the mutant enzyme shows increased oxidative stability with H2O2 compared to the wild-type enzyme
M321L
-
site-directed mutagenesis, the mutant enzyme shows over 43% reduced activity and reduced oxidative stability with H2O2 compared to the wild-type enzyme
M400L
-
site-directed mutagenesis, the mutant enzyme shows 191% increased activity and increased catalytic efficiency compared to the wild-type enzyme
M426L
-
site-directed mutagenesis, the mutant enzyme shows 79% increased activity and increased catalytic efficiency compared to the wild-type enzyme
M445L
-
site-directed mutagenesis, the mutant enzyme shows 313% increased activity and increased catalytic efficiency compared to the wild-type enzyme
M485L
-
site-directed mutagenesis, the mutant enzyme shows 103% increased activity and increased catalytic efficiency compared to the wild-type enzyme
D380E
-
the mutation causes more than 2fold decrease in kcat as compared to the wild type enzyme
D380N
-
the mutation causes more than 2fold decrease in kcat as compared to the wild type enzyme
D380V
-
the mutation causes over 5fold decrease in kcat as compared to the wild type enzyme
H191L
site-directed mutagenesis, the mutant enzyme shows similar catalytic effciency compared to the wild-type enzyme, with 30% increased Km
H227L
site-directed mutagenesis, the mutant enzyme shows a 39% decreased catalytic effciency compared to the wild-type enzyme, with a 3.9fold increased Km
H345L
site-directed mutagenesis, inactive mutant enzyme
H378L
site-directed mutagenesis, inactive mutant enzyme
Y352D
-
the mutation results in about 3.5fold decrease in specific activity
Y352L
-
the mutation results in about 3.5fold decrease in specific activity
D198A/F221T
-
decreased activity towards L-Leu-p-nitroanilide, highest activity towards L-Phe-p-nitroanilide
D198F/F221D
-
decreased activity towards L-Leu-p-nitroanilide, highest activity towards L-Arg-p-nitroanilide
D198H/F221N
-
decreased activity towards L-Leu-p-nitroanilide, highest activity towards L-Phe-p-nitroanilide
D198I/F221W
-
decreased activity towards L-Leu-p-nitroanilide, highest activity towards L-cystinyl-p-nitroanilide
D198L/F221E
-
decreased activity towards L-Leu-p-nitroanilide, highest activity towards L-Arg-p-nitroanilide
D198L/F221M
-
decreased activity towards L-Leu-p-nitroanilide, highest activity towards L-Phe-p-nitroanilide
D198L/F221T
-
decreased activity towards L-Leu-p-nitroanilide, highest activity towards L-Phe-p-nitroanilide
D198L/F221W
-
decreased activity towards L-Leu-p-nitroanilide, highest activity towards L-cystinyl-p-nitroanilide
D198M/F221A
-
decreased activity towards L-Leu-p-nitroanilide, highest activity towards L-Phe-p-nitroanilide
D198M/F221G
-
decreased activity towards L-Leu-p-nitroanilide, highest activity towards L-Phe-p-nitroanilide
D198M/F221V
-
decreased activity towards L-Leu-p-nitroanilide, highest activity towards L-Phe-p-nitroanilide
D198M/F221W
-
highest activity towards L-Leu-p-nitroanilide like the wild type enzyme
D198P/F221E
-
decreased activity towards L-Leu-p-nitroanilide, highest activity towards L-Arg-p-nitroanilide
D198S/F221E
-
decreased activity towards L-Leu-p-nitroanilide, highest activity towards L-Arg-p-nitroanilide
D198S/F221N
-
decreased activity towards L-Leu-p-nitroanilide, highest activity towards L-Phe-p-nitroanilide
D198V/F221D
-
decreased activity towards L-Leu-p-nitroanilide, highest activity towards L-Lys-p-nitroanilide
D198V/F221N
-
decreased activity towards L-Leu-p-nitroanilide, highest activity towards L-Phe-p-nitroanilide
D198W/F221D
-
decreased activity towards L-Leu-p-nitroanilide, highest activity towards L-Arg-p-nitroanilide
D118N
mutant shows similar activity compared to the wild type enzyme
E151H
site-directed mutagenesis, the mutant enzyme shows a highly reduced reaction rate compared to the wild-type enzyme
M180A
mutant shows severly reduced activity (approximately 100fold less active) compared to the wild type enzyme
S228A
mutant shows strongly reduced activity (approximately 10fold less active) compared to the wild type enzyme
additional information
additional information
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construction of a chimeric enzyme comprising the raw-starch-binding domain of Bacillus sp. strain TS-23 alpha-amylase and the Bacillus stearothermophilus LAPII, the chimeric mutant enzyme binds raw starch, overview
additional information
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preparation of C-terminally Lys-tagged aminopeptidase II, with either tri- or nona-lysines, and immobilization of the modified enzymes on carboxylated magnetic particles, method and evaluation of enzyme properties, overview. The carboxylated magnetic particles are prepared by the simple co-precipitation of Fe3+/Fe2+ in aqueous medium and then subsequently modified with adipic acid. The immobilized enzymes, especially BsAPII-Lys9, can be recovered magnetically and used repeatedly, thermal and storage stabilities of the immobilized BsAPII-Lys9 are greatly improved
