Detail Information for IndEnz0002016756
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