| IED ID | IndEnz0002018768 |
| Enzyme Type ID | protease018768 |
| Protein Name |
Aminopeptidase S EC 3.4.11.24 API SGAP |
| Gene Name | SGR_5809 |
| Organism | Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptomycetales Streptomycetaceae Streptomyces Streptomyces griseus group Streptomyces griseus subgroup Streptomyces griseus Streptomyces griseus subsp. griseus Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350) |
| Enzyme Sequence | MRPNRFSLRRSPTAVAAVALAAVLAAGAPAAQAAGAAAPTAAAAAAPDIPLANVKAHLTQLSTIAANNGGNRAHGRPGYKASVDYVKAKLDAAGYTTTLQQFTSGGATGYNLIADWPGGDPNKVLMAGAHLDSVSSGAGINDNGSGSAAVLETALAVSRAGYQPDKHLRFAWWGAEELGLIGSKYYVNNLPSADRSKLAGYLNFDMIGSPNPGYFVYDDDPVIEKTFKDYFAGLNVPTEIETEGDGRSDHAPFKNVGVPVGGLFTGAGYTKSAAQAQKWGGTAGQAFDRCYHSSCDSLSNINDTALDRNSDAAAHAIWTLSSGTGEPPTGEGVFSNTTDVAIPDAGAAVTSSVAVTGRTGNAPAALQVGVDIKHTYRGDLVVDLLAPDGTAYRLKNSSSGDSADNVIATYTVNASSEVANGSWKLRVQDIARQDTGYIDSWKLTF |
| Enzyme Length | 445 |
| Uniprot Accession Number | P80561 |
| Absorption | |
| Active Site | ACT_SITE 176; /note="Proton acceptor"; /evidence="ECO:0000303|PubMed:15280041, ECO:0000303|PubMed:17608735" |
| Activity Regulation | ACTIVITY REGULATION: Calcium activates the enzyme, inhibited by 1,10-phenanthroline, EDTA and EGTA (PubMed:2503378). End-product inhibited by L-amino acids (PubMed:15388919). Non-competitively inhibited by NaF and NaH(2)PO(4) (PubMed:17608735). {ECO:0000269|PubMed:15388919, ECO:0000269|PubMed:17608735, ECO:0000269|PubMed:2503378, ECO:0000269|PubMed:8444149}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues.; EC=3.4.11.24; Evidence={ECO:0000269|PubMed:8444149}; |
| DNA Binding | |
| EC Number | 3.4.11.24 |
| Enzyme Function | FUNCTION: An exopeptidase specific for larger hydrophobic amino acids (especially leucine), no cleavage occurs if the next residue is proline (PubMed:8444149). {ECO:0000269|PubMed:2503378, ECO:0000269|PubMed:8444149, ECO:0000269|PubMed:8665903}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Stable after heating at 69 degrees Celsius for 5 hours. {ECO:0000269|PubMed:2503378}; |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (10); Chain (1); Disulfide bond (1); Domain (1); Helix (10); Metal binding (10); Mutagenesis (3); Propeptide (1); Sequence conflict (2); Signal peptide (1); Site (1); Turn (3) |
| Keywords | 3D-structure;Aminopeptidase;Calcium;Direct protein sequencing;Disulfide bond;Hydrolase;Metal-binding;Protease;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2503378, ECO:0000269|PubMed:8665903}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..45; /evidence="ECO:0000269|PubMed:2503378, ECO:0000269|PubMed:8665903" |
| Structure 3D | X-ray crystallography (11) |
| Cross Reference PDB | 1CP7; 1F2O; 1F2P; 1QQ9; 1TF8; 1TF9; 1TKF; 1TKH; 1TKJ; 1XBU; 1XJO; |
| Mapped Pubmed ID | 10771423; 11484227; |
| Motif | |
| Gene Encoded By | |
| Mass | 45,940 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.59 mM for Leu-NH-Np (with zinc as cofactor) {ECO:0000269|PubMed:8444149}; KM=0.13 mM for Leu-NH-Np (with manganese as cofactor) {ECO:0000269|PubMed:8444149}; KM=0.046 mM for Leu-NH-Np (with cobalt as cofactor) {ECO:0000269|PubMed:8444149}; KM=4.1 mM for Ala-NH-Np (with zinc as cofactor) {ECO:0000269|PubMed:8444149}; KM=1.74 mM for Ala-NH-Np (with cobalt as cofactor) {ECO:0000269|PubMed:8444149}; KM=0.57 mM for Leu-pNA (with zinc as cofactor) {ECO:0000269|PubMed:15280041}; Note=kcat is 390 sec(-1) with Leu-pNA. {ECO:0000269|PubMed:15280041}; |
| Metal Binding | METAL 48; /note="Calcium"; /evidence="ECO:0000269|PubMed:15388919, ECO:0000269|PubMed:9048953"; METAL 49; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:15388919, ECO:0000269|PubMed:9048953"; METAL 130; /note="Zinc 1; catalytic"; /evidence="ECO:0000269|PubMed:15388919, ECO:0000269|PubMed:9048953"; METAL 142; /note="Zinc 1; catalytic"; /evidence="ECO:0000269|PubMed:15388919, ECO:0000269|PubMed:9048953"; METAL 142; /note="Zinc 2; catalytic"; /evidence="ECO:0000269|PubMed:15388919, ECO:0000269|PubMed:9048953"; METAL 177; /note="Zinc 2; catalytic"; /evidence="ECO:0000269|PubMed:15388919, ECO:0000269|PubMed:9048953"; METAL 205; /note="Zinc 1; catalytic"; /evidence="ECO:0000269|PubMed:15388919, ECO:0000269|PubMed:9048953"; METAL 292; /note="Zinc 2; catalytic"; /evidence="ECO:0000269|PubMed:15388919, ECO:0000269|PubMed:9048953"; METAL 307; /note="Calcium"; /evidence="ECO:0000269|PubMed:15388919, ECO:0000269|PubMed:9048953"; METAL 311; /note="Calcium"; /evidence="ECO:0000269|PubMed:15388919, ECO:0000269|PubMed:9048953" |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.24; |