| IED ID | IndEnz0002018717 |
| Enzyme Type ID | protease018717 |
| Protein Name |
Procardosin-B EC 3.4.23.- Cleaved into: Cardosin-B heavy chain Cardosin-B 34 kDa subunit ; Cardosin-B light chain Cardosin-B 14 kDa subunit |
| Gene Name | cardB |
| Organism | Cynara cardunculus (Cardoon) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae asterids campanulids Asterales Asteraceae Carduoideae Cardueae Carduinae Cynara Cynara cardunculus (Cardoon) |
| Enzyme Sequence | MGTPIKASLLALFLFFLLSPTAFSVSNGGLLRVGLKKRKVDRLDQLRAHGVHMLGNARKDFGFRRTLSDSGSGIVALTNDRDTAYYGEIGIGTPPQNFAVIFDTGSSDLWVPSTKCDTSLACVIHPRYDSGDSSTYKGNGTTASIQYGTGAIVGFYSQDSVEVGDLVVEHQDFIETTEEDDTVFLKSEFDGILGLGFQEISAGKAVPVWYNMVNQGLVEEAVFSFWLNRNVDEEEGGELVFGGVDPNHFRGNHTYVPVTRKGYWQFEMGDVLIGDKSSGFCAGGCAAIADSGTSFFAGPTAIITQINQAIGAKGVLNQQCKTLVGQYGKNMIQMLTSEVQPDKICSHMKLCTFDGAHDVRSMIESVVDKNNDKSSGGEICTFCEMALVRMQNEIKRNETEDNIINHVNEVCDQLPTSSAESIVDCNGISSMPNIAFTIGSKLFEVTPEQYIYKVGEGEAATCISGFTALDIMSPQGPIWILGDMFMGPYHTVFDYGKLRVGFAEAV |
| Enzyme Length | 506 |
| Uniprot Accession Number | Q9XFX4 |
| Absorption | |
| Active Site | ACT_SITE 103; /evidence="ECO:0000250|UniProtKB:P42210, ECO:0000255|PROSITE-ProRule:PRU10094"; ACT_SITE 290; /evidence="ECO:0000250|UniProtKB:P42210, ECO:0000255|PROSITE-ProRule:PRU10094" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by the specific aspartic proteinase inhibitors diazoacetyl-noleucine methyl ester and pepstatin. {ECO:0000269|PubMed:8654427}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.23.- |
| Enzyme Function | FUNCTION: Aspartic protease. Cleaves alpha-lactalbumin but not beta-lactoglobulin. {ECO:0000269|PubMed:16428617, ECO:0000269|PubMed:8654427}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Stable at temperatures of up to 60 degrees Celsius. {ECO:0000269|PubMed:8654427}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0. Active from pH 2.0-7.0. {ECO:0000269|PubMed:8654427}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (22); Chain (3); Disulfide bond (6); Domain (2); Glycosylation (3); Helix (10); Propeptide (1); Sequence conflict (7); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;Aspartyl protease;Cell wall;Direct protein sequencing;Disulfide bond;Endoplasmic reticulum;Extracellular matrix;Glycoprotein;Hydrolase;Membrane;Microsome;Protease;Secreted;Signal;Vacuole;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:Q9XFX3}. Protein storage vacuole {ECO:0000250|UniProtKB:Q9XFX3}. Secreted, cell wall {ECO:0000269|PubMed:11414612}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:11414612}. Note=Procardosin-B is associated with the microsomal membranes, the mature form is secreted. {ECO:0000250|UniProtKB:Q9XFX3, ECO:0000269|PubMed:11414612}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 5NFG; |
| Mapped Pubmed ID | 28770303; |
| Motif | |
| Gene Encoded By | |
| Mass | 54,951 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.081 mM for Leu-Ser-Phe(NO2)-Ahx-Ala-Leu {ECO:0000269|PubMed:8654427}; KM=0.11 mM for Lys-Pro-Ala-Glu-Phe-Phe(NO2)-Ala-Leu {ECO:0000269|PubMed:8654427}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.23.40; |