| IED ID | IndEnz0002004553 |
| Enzyme Type ID | protease004553 |
| Protein Name |
Aminopeptidase EC 3.4.11.1 Leucine aminopeptidase PaAP |
| Gene Name | lap PA14_26020 |
| Organism | Pseudomonas aeruginosa (strain UCBPP-PA14) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas aeruginosa group Pseudomonas aeruginosa Pseudomonas aeruginosa (strain UCBPP-PA14) |
| Enzyme Sequence | MSNKNNLRYALGALALSVSAASLAAPSEAQQFTEFWTPGKPNPSICKSPLLVSTPLGLPRCLQASNVVKRLQKLEDIASLNDGNRAAATPGYQASVDYVKQTLQKAGYKVSVQPFPFTAYYPKGPGSLSATVPQPVTYEWEKDFTYLSQTEAGDVTAKVVPVDLSLGAGNTSTSGCEAEDFANFPAGSIALIQRGTCNFEQKAENAAAAGAAGVIIFNQGNTDDRKGLENVTVGESYEGGIPVIFATYDNGVAWSQTPDLQLHLVVDVVRKKTETYNVVAETRRGNPNNVVMVGAHLDSVFEGPGINDNGSGSAAQLEMAVLLAKALPVNKVRFAWWGAEEAGLVGSTHYVQNLAPEEKKKIKAYLNFDMIGSPNFGNFIYDGDGSDFGLQGPPGSAAIERLFEAYFRLRGQQSEGTEIDFRSDYAEFFNSGIAFGGLFTGAEGLKTEEQAQKYGGTAGKAYDECYHSKCDGIANINQDALEIHSDAMAFVTSWLSLSTKVVDDEIAAAGQKAQSRSLQMQKSASQIERWGHDFIK |
| Enzyme Length | 536 |
| Uniprot Accession Number | Q02PA2 |
| Absorption | |
| Active Site | ACT_SITE 340; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P80561 |
| Activity Regulation | |
| 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; |
| 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 in the first position. {ECO:0000250|UniProtKB:Q9HZQ8}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (1); Domain (1); Metal binding (6); Modified residue (1); Signal peptide (1); Site (1) |
| Keywords | Aminopeptidase;Disulfide bond;Hydrolase;Metal-binding;Phosphoprotein;Protease;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24965220}. |
| Modified Residue | MOD_RES 196; /note=Phosphothreonine; /evidence=ECO:0000269|PubMed:24965220 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
| 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 |