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
General Information
General Information on EC 3.4.11.10 - bacterial leucyl aminopeptidase
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evolution
sequence analysis and phylogenetic relationship of M17 LAPs
evolution
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sequence analysis and phylogenetic relationship of M17 LAPs
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physiological function
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immunization with recombinant Fasciola gigantica LAP (FgLAP) elicits high levels of immune responses and protection against Fasciola gigantica in mice
physiological function
the M17 aminopeptidase from the carcinogenic gastric bacterium Helicobacter pylori (HpM17AP) is an important housekeeping enzyme involved in catabolism of endogenous and exogenous peptides. It is implicated in Helicobacter pylori defence against the human innate immune response and in the mechanism of metronidazole resistance
physiological function
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the M17 aminopeptidase from the carcinogenic gastric bacterium Helicobacter pylori (HpM17AP) is an important housekeeping enzyme involved in catabolism of endogenous and exogenous peptides. It is implicated in Helicobacter pylori defence against the human innate immune response and in the mechanism of metronidazole resistance
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physiological function
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the M17 aminopeptidase from the carcinogenic gastric bacterium Helicobacter pylori (HpM17AP) is an important housekeeping enzyme involved in catabolism of endogenous and exogenous peptides. It is implicated in Helicobacter pylori defence against the human innate immune response and in the mechanism of metronidazole resistance
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additional information
structural basis of catalysis and inhibition of the enzyme, active site of the free enzyme, overview
additional information
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structural basis of catalysis and inhibition of the enzyme, active site of the free enzyme, overview
additional information
temperature-dependent UV-CD spectra and fluorescent measurements
additional information
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structural basis of catalysis and inhibition of the enzyme, active site of the free enzyme, overview
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additional information
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structural basis of catalysis and inhibition of the enzyme, active site of the free enzyme, overview
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