Detail Information for IndEnz0002018760
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