| IED ID | IndEnz0002006571 |
| Enzyme Type ID | protease006571 |
| Protein Name |
Aminopeptidase EC 3.4.11.1 Leucine aminopeptidase PaAP Cleaved into: Aminopeptidase AP58; Aminopeptidase AP56; Aminopeptidase AP28 |
| Gene Name | lap PA2939 |
| Organism | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas aeruginosa group Pseudomonas aeruginosa Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Enzyme Sequence | MSNKNNLRYALGALALSVSAASLAAPSEAQQFTEFWTPGKPNPSICKSPLLVSTPLGLPRCLQASNVVKRLQKLEDIASLNDGNRAAATPGYQASVDYVKQTLQKAGYKVSVQPFPFTAYYPKGPGSLSATVPQPVTYEWEKDFTYLSQTEAGDVTAKVVPVDLSLGAGNTSTSGCEAEDFANFPAGSIALIQRGTCNFEQKAENAAAAGAAGVIIFNQGNTDDRKGLENVTVGESYEGGIPVIFATYDNGVAWSQTPDLQLHLVVDVVRKKTETYNVVAETRRGNPNNVVMVGAHLDSVFEGPGINDNGSGSAAQLEMAVLLAKALPVNKVRFAWWGAEEAGLVGSTHYVQNLAPEEKKKIKAYLNFDMIGSPNFGNFIYDGDGSDFGLQGPPGSAAIERLFEAYFRLRGQQSEGTEIDFRSDYAEFFNSGIAFGGLFTGAEGLKTEEQAQKYGGTAGKAYDECYHSKCDGIANINQDALEIHSDAMAFVTSWLSLSTKVVDDEIAAAGQKAQSRSLQMQKSASQIERWGHDFIK |
| Enzyme Length | 536 |
| Uniprot Accession Number | Q9HZQ8 |
| Absorption | |
| Active Site | ACT_SITE 340; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P80561 |
| Activity Regulation | ACTIVITY REGULATION: Mature protein inhibited by dithiothreitol and Zn(2+) chelators such as 1,10-phenanthroline, EDTA and EGTA. Not inhibited by serine-protease inhibitors, N-ethylmaleimide or phosphoramidon (which inhibits elastase). {ECO:0000269|PubMed:11533066}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.; EC=3.4.11.1; Evidence={ECO:0000269|PubMed:11533066}; |
| DNA Binding | |
| EC Number | 3.4.11.1 |
| Enzyme Function | FUNCTION: A secreted aminopeptidase. Acts on free N-terminal amino groups with a very strong preference for Leu- followed by Met- and Ala-, and no activity on Glu- or Gly- peptides (an exhaustive analysis was not performed). Both the AP56 and AP28 forms have activity. {ECO:0000269|PubMed:11533066}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5, active between pH 7 and 9.5. {ECO:0000269|PubMed:11533066}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (3); Disulfide bond (1); Domain (1); Metal binding (6); Natural variant (1); Signal peptide (1); Site (1) |
| Keywords | Aminopeptidase;Direct protein sequencing;Disulfide bond;Hydrolase;Metal-binding;Protease;Reference proteome;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11533066}. |
| Modified Residue | |
| Post Translational Modification | PTM: Processing of the 56 kDa pro-protein to mature protein requires elastase (lasB); in vitro it only occurs at greater than 55 degrees Celsius. {ECO:0000269|PubMed:11533066}.; PTM: Several forms of the enzyme have been identified by molecular weight, exactly which part of the sequence they correspond to is not always clear. The AP58 form may be subject to proteolysis to give rise to AP56. {ECO:0000305|PubMed:11533066, ECO:0000305|PubMed:9642203}. |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000269|PubMed:9642203 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 57,511 |
| Kinetics | |
| Metal Binding | METAL 296; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 308; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 308; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 341; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 369; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 467; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.1; |