| IED ID | IndEnz0002005578 |
| Enzyme Type ID | protease005578 |
| Protein Name |
Leucyl aminopeptidase EC 3.4.11.1 |
| Gene Name | ape2 lap SSO2154 C01_030 |
| Organism | Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus) |
| Taxonomic Lineage | cellular organisms Archaea TACK group Crenarchaeota Thermoprotei Sulfolobales Sulfolobaceae Saccharolobus Saccharolobus solfataricus (Sulfolobus solfataricus) Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus) |
| Enzyme Sequence | MIKVNRYEIFLDFSFQTGDYKGYEKIEMESDEETVVLDAVGLKIVKAKVNGKEIEFSQDESRVNVKSGSFSGILEVEFEGKVTERKLVGIYKASYKDGYVISTQFEATHARDFIPCFDHPAMKARFKLTVRVDKGLKVISNMPVVREKEENGKVVYEFDETPKMSTYLLYLGIGNFEEIRDEGKIPTIIVATIPGKVQKGRFSMQISRNSIEFYEKYFEIPYQLPKVHLIAIPEFAYGAMENWGAITFRETALLADDSSSVYQKFRVAEVVAHELAHQWFGNLVTLKWWDDLWLNESFATFMSHKAISQLFPSWNFWDYFVLNQTSRALEKDSVSTTHPIEAHVRDPNEVEQMFDDISYGKGASILRMIEAYVGEENFRRGVVNYLKKFSYSNAQGSDLWNSISEVYGSDISPIMADWITKPGYPMVRVSVSGKRVSLEQERFSLIGNVENLLYKIPLTMEVNGKVVTHLLDKERDTMVFEEDVKSLKVNVNRTGFYRVFYYNNSDLVFNSNLSELDKWGIINDYWAFLLAGKIGFKEYERVISKFFNDKDFLPVNELSNELFTLHAINPDKYQGIAKEFHRIQLKNWRNSKDELGRLTYSNILYRLAAIDDEFSLGLSELFRFYGSLDSDTRQGVAVAYAITYEDNSVDELLERFRKETFDEEKLRYLTAMLFFRKPYLVGNTLSLILSGEIKKQDIPLTLSTAAYNPYAKSAVLNWIKMHINFMREAYKGTGILGRRLAEVIPLIGIGAERETEQFFSNLNMPEAERGIGTGLELLKAYSRLK |
| Enzyme Length | 785 |
| Uniprot Accession Number | P95928 |
| Absorption | |
| Active Site | ACT_SITE 274; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | BINDING 106; /note=Substrate; /evidence=ECO:0000250 |
| 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: Preferentially acts as a leucyl-aminopeptidase, although it also has activity against other substrates. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 80 degrees Celsius.; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (1); Chain (1); Metal binding (3); Region (1); Site (1) |
| Keywords | Aminopeptidase;Cytoplasm;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | PTM: Can be phosphorylated by cell extracts. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 90,515 |
| Kinetics | |
| Metal Binding | METAL 273; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 277; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 296; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.B3; |