| IED ID | IndEnz0002001020 |
| Enzyme Type ID | protease001020 |
| Protein Name |
Subtilisin Carlsberg EC 3.4.21.62 |
| Gene Name | subC apr |
| Organism | Bacillus licheniformis |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus licheniformis |
| Enzyme Sequence | MMRKKSFWLGMLTAFMLVFTMAFSDSASAAQPAKNVEKDYIVGFKSGVKTASVKKDIIKESGGKVDKQFRIINAAKAKLDKEALKEVKNDPDVAYVEEDHVAHALAQTVPYGIPLIKADKVQAQGFKGANVKVAVLDTGIQASHPDLNVVGGASFVAGEAYNTDGNGHGTHVAGTVAALDNTTGVLGVAPSVSLYAVKVLNSSGSGSYSGIVSGIEWATTNGMDVINMSLGGASGSTAMKQAVDNAYAKGVVVVAAAGNSGSSGNTNTIGYPAKYDSVIAVGAVDSNSNRASFSSVGAELEVMAPGAGVYSTYPTNTYATLNGTSMASPHVAGAAALILSKHPNLSASQVRNRLSSTATYLGSSFYYGKGLINVEAAAQ |
| Enzyme Length | 379 |
| Uniprot Accession Number | P00780 |
| Absorption | |
| Active Site | ACT_SITE 137; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 168; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 325; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by p-chlorophenyl and 1-naphthyl boronic acid derivatives. {ECO:0000269|PubMed:9425066}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.; EC=3.4.21.62; Evidence={ECO:0000269|PubMed:11109488, ECO:0000269|Ref.4}; |
| DNA Binding | |
| EC Number | 3.4.21.62 |
| Enzyme Function | FUNCTION: Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides (Ref.4, PubMed:11109488). Shows high specificity for aromatic and hydrophobic amino acids in the P1 substrate position (PubMed:11109488). May play an important role in the degradation of feather keratin (PubMed:11109488). {ECO:0000269|PubMed:11109488, ECO:0000269|Ref.4}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (15); Chain (1); Domain (2); Helix (9); Metal binding (9); Propeptide (1); Sequence conflict (6); Signal peptide (1); Turn (2) |
| Keywords | 3D-structure;Calcium;Direct protein sequencing;Hydrolase;Metal-binding;Protease;Secreted;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11109488}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..29; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (27) |
| Cross Reference PDB | 1AF4; 1AV7; 1AVT; 1BE6; 1BE8; 1BFK; 1BFU; 1C3L; 1CSE; 1OYV; 1R0R; 1SBC; 1SCA; 1SCB; 1SCD; 1SCN; 1SEL; 1VSB; 1YU6; 2SEC; 2WUV; 2WUW; 3UNX; 3VSB; 4C3U; 4C3V; 6DWQ; |
| Mapped Pubmed ID | 12684499; 12888355; 15858268; 20099851; 22331906; 22751665; 23075397; 3064813; 3150541; 3301348; 8068694; 8297378; 8378343; 9113975; 9443341; 9675126; 9789015; |
| Motif | |
| Gene Encoded By | |
| Mass | 38,867 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.2 mM for Suc-Ala(2)-Ala-pNA {ECO:0000269|Ref.4}; KM=0.79 mM for Suc-Ala(2)-Phe-pNA {ECO:0000269|Ref.4}; KM=0.851 mM for Suc-Ala(2)-Phe-pNA {ECO:0000269|PubMed:11109488}; KM=0.22 mM for MeO-Suc-Ala(2)-Phe-pNA {ECO:0000269|Ref.4}; KM=5.6 mM for Suc-Gly(2)-Phe-pNA {ECO:0000269|PubMed:11109488}; KM=0.334 mM for Suc-Ala(2)-Pro-Phe-pNA {ECO:0000269|PubMed:11109488}; KM=0.062 mM for Suc-Ala(2)-Pro-Leu-pNA {ECO:0000269|PubMed:11109488}; KM=0.422 mM for Suc-Ala(2)-Pro-Arg-pNA {ECO:0000269|PubMed:11109488}; KM=0.245 mM for Suc-Ala(2)-Pro-Glu-pNA {ECO:0000269|PubMed:11109488}; KM=0.042 mM for Suc-Ala-Glu-Pro-Phe-pNA {ECO:0000269|PubMed:11109488}; Note=kcat is 1.6 sec(-1) with Suc-Ala(2)-Ala-pNA as substrate. kcat is 57 sec(-1) with Suc-Ala(2)-Phe-pNA as substrate. kcat is 97 sec(-1) with MeO-Suc-Ala(2)-Phe-pNA as substrate (Ref.4). kcat is 0.990 sec(-1) with Suc-Gly(2)-Phe-pNA as substrate. kcat is 20.3 sec(-1) with Suc-Ala(2)-Phe-pNA as substrate. kcat is 646 sec(-1) with Suc-Ala(2)-Pro-Phe-pNA as substrate. kcat is 137 sec(-1) with Suc-Ala(2)-Pro-Leu-pNA as substrate. kcat is 5.31 sec(-1) with Suc-Ala(2)-Pro-Arg-pNA as substrate. kcat is 1.92 sec(-1) with Suc-Ala(2)-Pro-Glu-pNA as substrate. kcat is 375 sec(-1) with Suc-Ala-Glu-Pro-Phe-pNA as substrate (PubMed:11109488). {ECO:0000269|PubMed:11109488, ECO:0000269|Ref.4}; |
| Metal Binding | METAL 107; /note=Calcium 1; /evidence=ECO:0000269|PubMed:8512925; METAL 146; /note=Calcium 1; /evidence=ECO:0000269|PubMed:8512925; METAL 179; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:8512925; METAL 181; /note=Calcium 1; /evidence=ECO:0000269|PubMed:8512925; METAL 183; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:8512925; METAL 185; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:8512925; METAL 273; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:8512925; METAL 275; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:8512925; METAL 278; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:8512925 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.62; |