| IED ID | IndEnz0002018760 |
| Enzyme Type ID | protease018760 |
| Protein Name |
Aminopeptidase ltah-1.1 EC 3.4.11.6 Aminopeptidase-1 AP-1 Arginine aminopeptidase 1 Leukotriene A4 hydrolase homolog ltah-1.1 |
| Gene Name | ltah-1.1 C42C1.11 |
| Organism | Caenorhabditis elegans |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans |
| Enzyme Sequence | MAPPHPRDPSTAANYEQVTVSHYALKWKVDFEKKHIAGDVSITLDVKQDTERIVLDTRDLSVQSVALNLNGEPKKAGFTLEDNQALGQKLVITTESLKSGDRPVLEIKYESSNNAAALQFLTAEQTTDRVAPYLFSQCQAINARSIVPCMDTPSVKSTYEAEVCVPIGLTCLMSAIGQGSTPSECGKRTIFSFKQPVSIPSYLLAIVVGHLERKEISERCAVWAEPSQAEASFYEFAETEKILKVAEDVAGPYVWGRYDLVVLPATFPFGGMENPCLTFITPTLLAGDRSLVNVIAHEISHSWTGNLVTNFSWEHFWLNEGFTVFLERKIHGKMYGELERQFESESGYEEALVRTVNDVFGPDHEYTKLVQNLGNADPDDAFSSVPYEKGSALLFTIEQALGDNSRFEQFLRDYIQKYAYKTVSTEEWKEYLYDSFTDKKVILDNIDWNLWLHKAGLPPKPKYDSTPMQACKDLAAKWTTEGSEAPTDGEVFAKMSNSQKLAVLDAVRVNKTMFGDRMPALTATYKLDQAKNAELKFSWLMLGLETKWSPIVDASLAFALAVGRMKYCKPIYRSLFGWSATRDRAISQFKANIPNMHPITVKAIQSLLK |
| Enzyme Length | 609 |
| Uniprot Accession Number | G5EFT4 |
| Absorption | |
| Active Site | ACT_SITE 298; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P09960; ACT_SITE 387; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P09960 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys.; EC=3.4.11.6; Evidence={ECO:0000305|PubMed:9774412}; |
| DNA Binding | |
| EC Number | 3.4.11.6 |
| Enzyme Function | FUNCTION: Aminopeptidase which preferentially removes N-terminal Arg and Lys residues from peptides and proteins. {ECO:0000269|PubMed:9774412}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Alternative sequence (3); Chain (1); Metal binding (3); Region (3) |
| Keywords | Alternative splicing;Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9774412}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10778742; 21177967; 21367940; 22267497; 22286215; 22560298; 23800452; 24884423; 25487147; 29348603; 6593563; |
| Motif | |
| Gene Encoded By | |
| Mass | 68,249 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.39 mM for L-Lys-pNitroaniline {ECO:0000269|PubMed:9774412}; KM=0.43 mM for L-Arg-pNitroaniline {ECO:0000269|PubMed:9774412}; KM=0.46 mM for L-Met-pNitroaniline {ECO:0000269|PubMed:9774412}; KM=0.90 mM for L-Val-pNitroaniline {ECO:0000269|PubMed:9774412}; KM=1.90 mM for L-Pro-pNitroaniline {ECO:0000269|PubMed:9774412}; KM=2.00 mM for L-Leu-pNitroaniline {ECO:0000269|PubMed:9774412}; KM=5.53 mM for L-Ala-pNitroaniline {ECO:0000269|PubMed:9774412}; Note=No activity with L-Asp-pNA, L-Glu-pNA or D-Leu-pNA. {ECO:0000269|PubMed:9774412}; |
| Metal Binding | METAL 297; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 301; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 320; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P09960 |
| Rhea ID | |
| Cross Reference Brenda |