| IED ID | IndEnz0002010000 |
| Enzyme Type ID | protease010000 |
| Protein Name |
Phenoloxidase-activating enzyme EC 3.4.21.- Prophenoloxidase-activating enzyme Cleaved into: Phenoloxidase-activating enzyme light chain; Phenoloxidase-activating enzyme heavy chain |
| Gene Name | PPAE |
| Organism | Bombyx mori (Silk moth) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Amphiesmenoptera Lepidoptera (butterflies and moths) Glossata Neolepidoptera Heteroneura Ditrysia Obtectomera Bombycoidea (hawk-moths) Bombycidae (silkworm moths) Bombycinae Bombyx Bombyx mori (Silk moth) |
| Enzyme Sequence | MFLIWTFIVAVLAIQTKSVVAQSCRTPNGLNGNCVSVYECQALLAILNNQRRTQQDEKFLRDSQCGTKNSVPAVCCPCNAADGQQGNCVNINSCPYVLQLLKNPNEANLNYVRGSVCQGSEQQSICCVTAPQSTAVTTTPRPKRVHACQSEMTATPPNPEGKCCGRDIAVGDKIVGGAPASIDSYPWLVVIEYVRLERTMLLCGGALISGKYVLTAGHCVKGAILDVGTPKTVRLGEYNTTNPGRDCVSVSAGGTDCTDPLVKIGIEKTIPHPDYQPYHFLRKHDIGLIRLQSIAPFTDFIRPICLPSTDYTVNPPSKFALTVAGWGRYLQFDNGTVRSSKIKLHVTLPFVQRDVCEANQKPLRNGQRITLWKGQMCAGGEAGKDSCKGDSGGPLMYEHSKKYEAVGIVSFGPEKCGQIDIPGVYTNVYEYLPWIQNTIEP |
| Enzyme Length | 441 |
| Uniprot Accession Number | Q9XXV0 |
| Absorption | |
| Active Site | ACT_SITE 218; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 285; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 391; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274 |
| Activity Regulation | ACTIVITY REGULATION: Stabilized by calcium (PubMed:4197814). Inhibited by di-isopropyl phosphorofluoridate (DFP), phenylmethanesulfonylfluoride (PMSF), p-nitrophenyl-p'-guanidinobenzonate (p-NPGB), p-chloromercuribenzoate (PCMB), ethylenediaminetetraacetic acid (EDTA), urea and CI-13c (PubMed:4197814, PubMed:4197815, PubMed:7981662). {ECO:0000269|PubMed:4197814, ECO:0000269|PubMed:4197815, ECO:0000269|PubMed:7981662}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Endopeptidase with selective post-Arg cleavage site (PubMed:4197814, PubMed:4197815, PubMed:10066809, PubMed:7981662). Activates prophenoloxidase (PubMed:4197814, PubMed:4197815). Has a probable role in the melanization process as part of the innate immune response (Probable). {ECO:0000269|PubMed:10066809, ECO:0000269|PubMed:4197814, ECO:0000269|PubMed:4197815, ECO:0000269|PubMed:7981662, ECO:0000305}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 0-25 degrees Celsius. {ECO:0000269|PubMed:10066809}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0-8.5. {ECO:0000269|PubMed:10066809}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (2); Disulfide bond (10); Domain (3); Glycosylation (2); Metal binding (4); Modified residue (1); Sequence conflict (1); Signal peptide (1); Site (1) |
| Keywords | Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Protease;Pyrrolidone carboxylic acid;Reference proteome;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 22; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:10066809 |
| Post Translational Modification | PTM: Proteolytically cleaved for activation (PubMed:10066809). Cleavage produces a light chain and a catalytic heavy chain which remains covalently associated probably through an interchain disulfide bond (Probable). {ECO:0000269|PubMed:10066809, ECO:0000305|PubMed:10066809}.; PTM: Glycosylated. {ECO:0000269|PubMed:10066809}. |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000269|PubMed:10066809 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 47,985 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.2 uM for prophenoloxidase (at pH 7.6 and 0 degrees Celsius) {ECO:0000269|PubMed:4197814, ECO:0000269|PubMed:4197815}; KM=1.43 mM for N-benzoyl-L-arginine ethyl ester hydrochloride (BAEE) (in the absence of KCl) {ECO:0000269|PubMed:4197815}; KM=0.77 mM for N-benzoyl-L-arginine ethyl ester hydrochloride (BAEE) (in the presence of 0.025 M KCl) {ECO:0000269|PubMed:4197815}; KM=1.2 mM for N-benzoyl-L-arginine ethyl ester hydrochloride (BAEE) (in the presence of 0.004 M KCl) {ECO:0000269|PubMed:10066809}; KM=0.35 mM for N-benzoyl-L-arginine ethyl ester hydrochloride (BAEE) (in the presence of 0.5 M KCl) {ECO:0000269|PubMed:10066809}; KM=0.145 mM for N-benzoyl-L-arginine ethyl ester hydrochloride (BAEE) (in the presence of 0.5 M KCl) {ECO:0000269|PubMed:4197815}; KM=0.709 mM for N-p-tosyl-L-arginine methyl ester hydrochloride (TAME) (in the presence of 0.5 M KCl) {ECO:0000269|PubMed:4197815}; |
| Metal Binding | METAL 237; /note=Calcium; /evidence=ECO:0000250|UniProtKB:O97366; METAL 239; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:O97366; METAL 242; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:O97366; METAL 246; /note=Calcium; /evidence=ECO:0000250|UniProtKB:O97366 |
| Rhea ID | |
| Cross Reference Brenda |