Detail Information for IndEnz0002018768
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;