Detail Information for IndEnz0002011232
IED ID IndEnz0002011232
Enzyme Type ID protease011232
Protein Name Scytalidopepsin B
SLB
EC 3.4.23.32
Acid protease B
Gene Name
Organism Scytalidium lignicola (Hyphomycete)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Leotiomycetes Leotiomycetes incertae sedis Scytalidium Scytalidium lignicola (Hyphomycete)
Enzyme Sequence MKFTTAAVLSALVSAEIAFAAPGGNGFARRQARRQARAAGLKASPFRQVNAKEATVESNWGGAILIGSDFDTVSATANVPSASGGSSAAGTAWVGIDGDTCQTAILQTGFDWYGDGTYDAWYEWYPEVSDDFSGITISEGDSIQMSVTATSDTSGSATLENLTTGQKVSKSFSNESSGSLCRTNAEFIIEDFEECNSNGSDCEFVPFASFSPAVEFTDCSVTSDGESVSLDDAQITQVIINNQDVTDCSVSGTTVSCSYV
Enzyme Length 260
Uniprot Accession Number P15369
Absorption
Active Site ACT_SITE 190; /note=Proton acceptor; /evidence=ECO:0000269|PubMed:14993599
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity, cleaving 24-Phe-|-Phe-25, but not 15-Leu-|-Tyr-16 and 25-Phe-|-Tyr-26 in the B chain of insulin.; EC=3.4.23.32;
DNA Binding
EC Number 3.4.23.32
Enzyme Function
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Beta strand (20); Chain (1); Disulfide bond (3); Helix (1); Propeptide (1); Sequence conflict (4); Signal peptide (1); Site (1); Turn (2)
Keywords 3D-structure;Aspartyl protease;Direct protein sequencing;Disulfide bond;Hydrolase;Protease;Signal;Zymogen
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..20; /evidence=ECO:0000255
Structure 3D X-ray crystallography (4)
Cross Reference PDB 1S2B; 1S2K; 2IFR; 2IFW;
Mapped Pubmed ID 17069854;
Motif
Gene Encoded By
Mass 27,165
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.23.32;