| IED ID | IndEnz0002019106 |
| Enzyme Type ID | protease019106 |
| Protein Name |
Cytosol aminopeptidase EC 3.4.11.1 Leucine aminopeptidase LAP EC 3.4.11.10 Leucyl aminopeptidase |
| Gene Name | pepA HP_0570 |
| Organism | Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria delta/epsilon subdivisions Epsilonproteobacteria Campylobacterales Helicobacteraceae Helicobacter Helicobacter pylori (Campylobacter pylori) Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) |
| Enzyme Sequence | MLKIKLEKTTFENAKAECSLVFIINKDFSHAWVKNKELLETFKYEGEGVFLDQENKILYAGVKEDDVHLLRESACLAVRTLKKLAFKSVKVGVYTCGAHSKDNALLENLKALFLGLKLGLYEYDTFKSNKKESVLKEAIVALELHKPCEKTCANSLEKSAKEALKYAEIMTESLNIVKDLVNTPPMIGTPVYMAEVAQKVAKENHLEIHVHDEKFLEEKKMNAFLAVNKASLSVNPPRLIHLVYKPKKAKKKIALVGKGLTYDCGGLSLKPADYMVTMKADKGGGSAVIGLLNALAKLGVEAEVHGIIGATENMIGPAAYKPDDILISKEGKSIEVRNTDAEGRLVLADCLSYAQDLNPDVIVDFATLTGACVVGLGEFTSAIMGHNEELKNLFETSGLESGELLAKLPFNRHLKKLIESKIADVCNISSSRYGGAITAGLFLNEFIRDEFKDKWLHIDIAGPAYVEKEWDVNSFGASGAGVRACTAFVEELLKKA |
| Enzyme Length | 496 |
| Uniprot Accession Number | O25294 |
| Absorption | |
| Active Site | ACT_SITE 270; /evidence=ECO:0000255; ACT_SITE 344; /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; CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.; EC=3.4.11.10; |
| DNA Binding | |
| EC Number | 3.4.11.1; 3.4.11.10 |
| Enzyme Function | FUNCTION: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (20); Chain (1); Helix (18); Metal binding (7); Turn (5) |
| Keywords | 3D-structure;Aminopeptidase;Cytoplasm;Hydrolase;Manganese;Metal-binding;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 4ZI6; 4ZLA; |
| Mapped Pubmed ID | 11196647; 26616008; |
| Motif | |
| Gene Encoded By | |
| Mass | 54,433 |
| Kinetics | |
| Metal Binding | METAL 258; /note=Manganese 2; /evidence=ECO:0000250; METAL 263; /note=Manganese 1; /evidence=ECO:0000250; METAL 263; /note=Manganese 2; /evidence=ECO:0000250; METAL 281; /note=Manganese 2; /evidence=ECO:0000250; METAL 340; /note=Manganese 1; /evidence=ECO:0000250; METAL 342; /note=Manganese 1; /evidence=ECO:0000250; METAL 342; /note=Manganese 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.10; |