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.
Reaction
release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids
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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
Application
Application on EC 3.4.11.10 - bacterial leucyl aminopeptidase
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medicine
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recombinant FgLAP has a potential as a vaccine candidate against Fasciola gigantica
nutrition
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debittering of casein- and soyprotein-derived peptide solutions
analysis
evaluation of a single-stage MS-based technique for amino acid sequencing involving partial, heterogenous digestion of a peptide by a processive, non-specific, thermotropic Bacillus subtilis-derived aminopeptidase (BsuAP), which allows single-shot sequencing to be carried out through simultaneous accumulation, and detection of subpopulations of peptides of progressively reducing length
analysis
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evaluation of a single-stage MS-based technique for amino acid sequencing involving partial, heterogenous digestion of a peptide by a processive, non-specific, thermotropic Bacillus subtilis-derived aminopeptidase (BsuAP), which allows single-shot sequencing to be carried out through simultaneous accumulation, and detection of subpopulations of peptides of progressively reducing length
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pharmacology
the enzyme ia a target for development of drugs in therapy of Lyme disease caused by Borrelia burgdorferi
pharmacology
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the enzyme is a target for development of anti-Helicobacter pylori agents
synthesis
LAP is an important enzyme for the industrial production of enantiomerically pure amino acids
synthesis
leucine aminopeptidase from Vibrio proteolyticus is a broad specificity N-terminal aminopeptidase that is widely used in pharmaceutical processes where the removal of N-terminal residues in recombinant proteins is required