IED ID | IndEnz0002019052 |
Enzyme Type ID | protease019052 |
Protein Name |
Alkaline proteinase ALP EC 3.4.21.- Fragments |
Gene Name | |
Organism | Fusarium culmorum |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Nectriaceae Fusarium Fusarium sambucinum species complex Fusarium culmorum |
Enzyme Sequence | GSTSYIYDTSAGSGTYAYIVDTGIITSHNGFNWAANDIISKSYSNYGTVLDIFAPGTSVLSS |
Enzyme Length | 62 |
Uniprot Accession Number | P83610 |
Absorption | |
Active Site | ACT_SITE 21; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10080 |
Activity Regulation | ACTIVITY REGULATION: Inhibited by phenylmethanesulfonyl fluoride (PMSF) and chymostatin (CST), but not by Bowman-Birk type trypsin-chymotrypsin inhibitor (BBI). {ECO:0000269|PubMed:11846781}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.21.- |
Enzyme Function | FUNCTION: Serine protease. May be involved in the invasion of grains and hydrolyzation of grain proteins. {ECO:0000269|PubMed:11846781}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius.; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.3-9.6.; |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Domain (1); Non-adjacent residues (2); Non-terminal residue (2) |
Keywords | Direct protein sequencing;Hydrolase;Protease;Secreted;Serine protease |
Interact With | |
Induction | INDUCTION: By gluten. {ECO:0000269|PubMed:11846781}. |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 6,493 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.1 mM for N-succinyl-Ala-Ala-Pro-Phe p-nitroanilide (at pH 6.0 with dimethylsulfoxide); KM=2.3 mM for N-succinyl-Ala-Ala-Pro-Phe p-nitroanilide (at pH 9.0 with dimethylsulfoxide); KM=1.1 mM for N-succinyl-Ala-Ala-Pro-Phe p-nitroanilide (at pH 9.0 without dimethylsulfoxide); |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |