Detail Information for IndEnz0002004647
IED ID IndEnz0002004647
Enzyme Type ID protease004647
Protein Name Insulin-degrading enzyme
EC 3.4.24.56
Insulin protease
Insulinase
Insulysin
Gene Name Ide CG5517
Organism Drosophila melanogaster (Fruit fly)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora melanogaster group melanogaster subgroup Drosophila melanogaster (Fruit fly)
Enzyme Sequence MTIAESSQKSATRKPDSMEPILRLNNIEKSLQDTRDYRGLQLENGLKVLLISDPNTDVSAAALSVQVGHMSDPTNLPGLAHFCEHMLFLGTEKYPHENGYTTYLSQSGGSSNAATYPLMTKYHFHVAPDKLDGALDRFAQFFIAPLFTPSATEREINAVNSEHEKNLPSDLWRIKQVNRHLAKPDHAYSKFGSGNKTTLSEIPKSKNIDVRDELLKFHKQWYSANIMCLAVIGKESLDELEGMVLEKFSEIENKNVKVPGWPRHPYAEERYGQKVKIVPIKDIRSLTISFTTDDLTQFYKSGPDNYLTHLIGHEGKGSILSELRRLGWCNDLMAGHQNTQNGFGFFDIVVDLTQEGLEHVDDIVKIVFQYLEMLRKEGPKKWIFDECVKLNEMRFRFKEKEQPENLVTHAVSSMQIFPLEEVLIAPYLSNEWRPDLIKGLLDELVPSKSRIVIVSQSFEPDCDLAEPYYKTKYGITRVAKDTVQSWENCELNENLKLALPNSFIPTNFDISDVPADAPKHPTIILDTPILRVWHKQDNQFNKPKACMTFDMSNPIAYLDPLNCNLNHMMVMLLKDQLNEYLYDAELASLKLSVMGKSCGIDFTIRGFSDKQVVLLEKLLDHLFDFSIDEKRFDILKEEYVRSLKNFKAEQPYQHSIYYLALLLTENAWANMELLDAMELVTYDRVLNFAKEFFQRLHTECFIFGNVTKQQATDIAGRVNTRLEATNASKLPILARQMLKKREYKLLAGDSYLFEKENEFHKSSCAQLYLQCGAQTDHTNIMVNLVSQVLSEPCYDCLRTKEQLGYIVFSGVRKVNGANGIRIIVQSAKHPSYVEDRIENFLQTYLQVIEDMPLDEFERHKEALAVKKLEKPKTIFQQFSQFYGEIAMQTYHFEREEAEVAILRKISKADFVDYFKKFIAKDGEERRVLSVHIVSQQTDENATSEAEPVEITNMERHKPISDIVTFKSCKELYPIALPFLDIKAKGARSKL
Enzyme Length 990
Uniprot Accession Number P22817
Absorption
Active Site ACT_SITE 84; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10096
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Degradation of insulin, glucagon and other polypeptides. No action on proteins.; EC=3.4.24.56;
DNA Binding
EC Number 3.4.24.56
Enzyme Function FUNCTION: Can cleave insulin and TGF-alpha. {ECO:0000269|PubMed:3139025}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:3139025};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-8. {ECO:0000269|PubMed:3139025};
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Erroneous initiation (3); Initiator methionine (1); Metal binding (3); Sequence conflict (6)
Keywords Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc
Interact With
Induction INDUCTION: Inhibited by bacitracin and sulfhydryl-specific reagents. {ECO:0000269|PubMed:3139025}.
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10924473; 12865422; 15234342; 15834148; 16107220; 18245849; 18690061; 19520911; 20220848; 20371351; 20493190; 21074052; 21212741; 21917925; 22758915; 23071443; 23445342; 23827522; 24430872; 25096240; 25294943; 25312911; 25740935; 26472340; 26526100; 2659071; 26865094; 26870755; 27172210; 27444168; 27794539; 28633019; 29523653; 30378026; 30541713; 30652125; 31208963; 32019113; 32984330; 33143302; 7610476; 8099278; 9128138;
Motif
Gene Encoded By
Mass 113,684
Kinetics
Metal Binding METAL 81; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU10096; METAL 85; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU10096; METAL 162; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU10096
Rhea ID
Cross Reference Brenda 3.4.24.56;