| IED ID | IndEnz0002016756 |
| Enzyme Type ID | protease016756 |
| 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 Proline aminopeptidase EC 3.4.11.5 Prolyl aminopeptidase |
| Gene Name | lap3 |
| Organism | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Silurana Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
| Enzyme Sequence | MLPFRTLLKWSVNRNCCRGFAVSQQNYNSVKKGLVLGVYEKEKEEESLTLTNAGDAVDNAVLGKLRDQLARSGPSLKKGKSRIFYGLHEDFPSIVVVGLGKKSAGVNQHELWNEAKENIRAAVSVGCRQMQDMEIVQVEVDPCGDAQAAAEGAVLGLFEYNEMKKKKKKAVTTHLHGSSEITAWEKGVLYAEGQNLARHLMEAPANYITPTKFAETFEQRLANMGSNVKVFTRSKQWIEEQQMGAFLSVAKGSEEPPVFLEIHYSGSSDASQPPLVFVGKGVTFDSGGISLKPSSGMDAMRGDMGGAATVCSAITTAAKLKLPINIISLAPLCENMPNGRANKPGDVVKAKNGKTIQVDNTDAEGRLLLADALCYAHSFNPRAIVNAATLTGAMDVALGSAAAGVFTNSSWLWTHLQEASVVTGDRVWRMPLFEHYSKQVTESALADLNNIGKYSRSGGACTAAAFLKEFVTAPHWAHLDIAGVMSNKDEVPYLRKGMSGRPTRTLIEFAARLSEDKQTI |
| Enzyme Length | 520 |
| Uniprot Accession Number | Q5XGB9 |
| Absorption | |
| Active Site | ACT_SITE 292; /evidence=ECO:0000250|UniProtKB:P00727; ACT_SITE 366; /evidence=ECO:0000250|UniProtKB:P00727 |
| Activity Regulation | |
| Binding Site | BINDING 280; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00727; BINDING 285; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00727; BINDING 290; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00727; BINDING 292; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00727; BINDING 303; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00727; BINDING 362; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00727 |
| 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:P00727}; 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 | Active site (2); Binding site (6); Chain (1); Metal binding (13) |
| Keywords | Aminopeptidase;Cytoplasm;Hydrolase;Magnesium;Manganese;Metal-binding;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q68FS4}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 56,333 |
| Kinetics | |
| Metal Binding | METAL 200; /note=Zinc 3; via carbonyl oxygen; structural; /evidence=ECO:0000250|UniProtKB:P00727; METAL 201; /note=Zinc 3; via carbonyl oxygen; structural; /evidence=ECO:0000250|UniProtKB:P00727; METAL 280; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P00727; METAL 285; /note=Magnesium; catalytic; /evidence=ECO:0000250|UniProtKB:P00727; METAL 285; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P00727; METAL 285; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P00727; METAL 301; /note=Zinc 3; via carbonyl oxygen; structural; /evidence=ECO:0000250|UniProtKB:P00727; METAL 303; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P00727; METAL 362; /note=Magnesium; catalytic; /evidence=ECO:0000250|UniProtKB:P00727; METAL 362; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P00727; METAL 364; /note=Magnesium; catalytic; /evidence=ECO:0000250|UniProtKB:P00727; METAL 364; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P00727; METAL 364; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P00727 |
| Rhea ID | RHEA:60444; RHEA:60445; RHEA:28783; RHEA:28784; RHEA:62568; RHEA:62569 |
| Cross Reference Brenda |