Detail Information for IndEnz0002018717
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;