| IED ID | IndEnz0002014206 |
| Enzyme Type ID | protease014206 |
| Protein Name |
Cytosol aminopeptidase EC 3.4.11.1 Cysteinylglycine-S-conjugate dipeptidase EC 3.4.13.23 Leucine aminopeptidase 3 LAP-3 Leucyl aminopeptidase Peptidase S Proline aminopeptidase EC 3.4.11.5 Prolyl aminopeptidase Fragments |
| Gene Name | LAP3 |
| Organism | Mesocricetus auratus (Golden hamster) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Cricetidae Cricetinae (hamsters) Mesocricetus Mesocricetus auratus (Golden hamster) |
| Enzyme Sequence | GVLFASGQNLARTLIEFLLR |
| Enzyme Length | 20 |
| Uniprot Accession Number | P86249 |
| Absorption | |
| Active Site | |
| 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; Evidence={ECO:0000250|UniProtKB:P28838}; CATALYTIC ACTIVITY: Reaction=an S-substituted L-cysteinylglycine + H2O = an S-substituted L-cysteine + glycine; Xref=Rhea:RHEA:60444, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305, ChEBI:CHEBI:58717, ChEBI:CHEBI:143103; EC=3.4.13.23; Evidence={ECO:0000250|UniProtKB:P00727};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60445; Evidence={ECO:0000250|UniProtKB:P00727}; CATALYTIC ACTIVITY: Reaction=H2O + L-cysteinylglycine = glycine + L-cysteine; Xref=Rhea:RHEA:28783, ChEBI:CHEBI:15377, ChEBI:CHEBI:35235, ChEBI:CHEBI:57305, ChEBI:CHEBI:61694; Evidence={ECO:0000250|UniProtKB:P00727};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28784; Evidence={ECO:0000250|UniProtKB:P00727}; CATALYTIC ACTIVITY: Reaction=H2O + S-benzyl-L-cysteinylglycine = glycine + S-benzyl-L-cysteine; Xref=Rhea:RHEA:62568, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305, ChEBI:CHEBI:145802, ChEBI:CHEBI:145803; Evidence={ECO:0000250|UniProtKB:Q68FS4};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62569; Evidence={ECO:0000250|UniProtKB:Q68FS4}; CATALYTIC ACTIVITY: Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5; Evidence={ECO:0000250|UniProtKB:P28839}; |
| DNA Binding | |
| EC Number | 3.4.11.1; 3.4.13.23; 3.4.11.5 |
| Enzyme Function | FUNCTION: Cytosolic metallopeptidase that catalyzes the removal of unsubstituted N-terminal hydrophobic amino acids from various peptides. The presence of Zn(2+) ions is essential for the peptidase activity, and the association with other cofactors can modulate the substrate spectificity of the enzyme. For instance, in the presence of Mn(2+), it displays a specific Cys-Gly hydrolyzing activity of Cys-Gly-S-conjugates. Involved in the metabolism of glutathione and in the degradation of glutathione S-conjugates, which may play a role in the control of the cell redox status. {ECO:0000250|UniProtKB:P00727}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Modified residue (1); Non-adjacent residues (1); Non-terminal residue (2) |
| Keywords | Aminopeptidase;Cytoplasm;Hydrolase;Magnesium;Manganese;Metal-binding;Phosphoprotein;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q68FS4}. |
| Modified Residue | MOD_RES 6; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P28838 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 2,219 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:60444; RHEA:60445; RHEA:28783; RHEA:28784; RHEA:62568; RHEA:62569 |
| Cross Reference Brenda |