| IED ID | IndEnz0002014201 |
| Enzyme Type ID | protease014201 |
| Protein Name |
Leucine aminopeptidase 1 EC 3.4.11.1 |
| Gene Name | lap-1 ZK353.6 |
| 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 | MTQVLVRNGIQAVGDGLTSLIIVGKKSVLKNVTFEGKFKEVAQKFVTDGDSWNSMISRIPASGRHPLHYELAHLITVPDASSRGNTPTNAHSIYKELKPINYPEDTKNVHFVLFAEYPDVLSHVAAIARTFCKFSMKTSGIRELNVNIDVVCDKLTNEDAVFLTDLSESVRETARLIDTPANILTTDALVDEAVKVGNATGSKITVIRGEELLKAGFGGIYHVGKAGPTPPAFVVLSHEVPGSTEHIALVGKGVVYDTGGLQIKTKTGMPNMKRDMGGAAGMLEAYSALVKHGFSQTLHACLCIVENNVSPIANKPDDIIKMLSGKTVEINNTDAEGRLILADGVFYAKETLKATTIFDMATLTGAQAWLSGRLHGAAMTNDEQLENEIIKAGKASGDLVAPMLFAPDLFFGDLKSSIADMKNSNLGKMDGPPSAVAGLFIGAHIGFGEGLRWLHLDIAAPAEVGDRGTGYGPALFSTLLGKYTSVPMLKQ |
| Enzyme Length | 491 |
| Uniprot Accession Number | P34629 |
| Absorption | |
| Active Site | ACT_SITE 264; /evidence=ECO:0000255; ACT_SITE 338; /evidence=ECO:0000255 |
| 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: Probably acts as a digestive enzyme. {ECO:0000269|PubMed:11295176}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (17); Chain (1); Helix (22); Metal binding (7); Turn (7) |
| Keywords | 3D-structure;Aminopeptidase;Hydrolase;Metal-binding;Protease;Reference proteome;Zinc |
| Interact With | Itself; O01812 |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 2HB6; 2HC9; |
| Mapped Pubmed ID | 10778742; 12097347; 14704431; 14992718; 19123269; 21110867; 21177967; 21367940; 21408619; 22267497; 22560298; 23800452; 24884423; 25487147; 25635455; 27506200; 29348603; 6593563; |
| Motif | |
| Gene Encoded By | |
| Mass | 52,449 |
| Kinetics | |
| Metal Binding | METAL 252; /note=Zinc 2; /evidence=ECO:0000250; METAL 257; /note=Zinc 1; /evidence=ECO:0000250; METAL 257; /note=Zinc 2; /evidence=ECO:0000250; METAL 275; /note=Zinc 2; /evidence=ECO:0000250; METAL 334; /note=Zinc 1; /evidence=ECO:0000250; METAL 336; /note=Zinc 1; /evidence=ECO:0000250; METAL 336; /note=Zinc 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |