| IED ID | IndEnz0002016527 |
| Enzyme Type ID | protease016527 |
| Protein Name |
Angiotensin-converting enzyme EC 3.4.15.1 Dipeptidyl carboxypeptidase I Kininase II |
| Gene Name | Ance Race CG8827 |
| 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 | MRLFLLALLATLAVTQALVKEEIQAKEYLENLNKELAKRTNVETEAAWAYGSNITDENEKKKNEISAELAKFMKEVASDTTKFQWRSYQSEDLKRQFKALTKLGYAALPEDDYAELLDTLSAMESNFAKVKVCDYKDSTKCDLALDPEIEEVISKSRDHEELAYYWREFYDKAGTAVRSQFERYVELNTKAAKLNNFTSGAEAWLDEYEDDTFEQQLEDIFADIRPLYQQIHGYVRFRLRKHYGDAVVSETGPIPMHLLGNMWAQQWSEIADIVSPFPEKPLVDVSAEMEKQGYTPLKMFQMGDDFFTSMNLTKLPQDFWDKSIIEKPTDGRDLVCHASAWDFYLTDDVRIKQCTRVTQDQLFTVHHELGHIQYFLQYQHQPFVYRTGANPGFHEAVGDVLSLSVSTPKHLEKIGLLKDYVRDDEARINQLFLTALDKIVFLPFAFTMDKYRWSLFRGEVDKANWNCAFWKLRDEYSGIEPPVVRSEKDFDAPAKYHISADVEYLRYLVSFIIQFQFYKSACIKAGQYDPDNVELPLDNCDIYGSAAAGAAFHNMLSMGASKPWPDALEAFNGERIMSGKAIAEYFEPLRVWLEAENIKNNVHIGWTTSNKCVSS |
| Enzyme Length | 615 |
| Uniprot Accession Number | Q10714 |
| Absorption | |
| Active Site | ACT_SITE 368 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by captopril and, to a lesser extent, by lisinopril, trandolaprilat, fosinoprilat and enalaprilat. {ECO:0000269|PubMed:7775412, ECO:0000269|PubMed:8761461}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of a C-terminal dipeptide, oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II.; EC=3.4.15.1; Evidence={ECO:0000269|PubMed:7775412}; |
| DNA Binding | |
| EC Number | 3.4.15.1 |
| Enzyme Function | FUNCTION: May be involved in the specific maturation or degradation of a number of bioactive peptides. May play a role in the contractions of the heart, gut and testes, and in spermatid differentiation. {ECO:0000269|PubMed:12591244}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (10); Chain (1); Disulfide bond (4); Glycosylation (3); Helix (35); Metal binding (3); Sequence conflict (13); Signal peptide (1); Turn (6) |
| Keywords | 3D-structure;Carboxypeptidase;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Zinc |
| Interact With | P01019; P01042 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space. |
| Modified Residue | |
| Post Translational Modification | PTM: Glycosylated. {ECO:0000269|PubMed:8761461}. |
| Signal Peptide | SIGNAL 1..17 |
| Structure 3D | X-ray crystallography (22) |
| Cross Reference PDB | 1J36; 1J37; 1J38; 2X8Y; 2X8Z; 2X90; 2X91; 2X92; 2X93; 2X94; 2X95; 2X96; 2X97; 2XHM; 3ZQZ; 4AA1; 4AA2; 4ASQ; 4ASR; 4CA7; 4CA8; 5A2R; |
| Mapped Pubmed ID | 10201373; 10498935; 10581287; 10769238; 10779495; 10887086; 10913309; 10961940; 10961941; 11102838; 11260716; 11585808; 11677596; 11703947; 11731450; 11897392; 12093364; 12135929; 12239569; 12431739; 12431741; 12464180; 12505997; 12524369; 12783790; 14568549; 14605208; 14642751; 14691551; 15020468; 15082551; 15341741; 15527959; 15579698; 15603586; 15680371; 15716118; 15728670; 15788537; 15797386; 15834142; 15935780; 16198288; 16391236; 16403023; 16410409; 16880385; 17055976; 17092951; 17921161; 17969149; 18171476; 18403407; 18701888; 18794353; 19171888; 19504457; 20220848; 20371351; 20488190; 20599761; 20813047; 20951134; 21074052; 2121594; 21245164; 21480662; 21810173; 22028675; 22145623; 22510984; 22513375; 22595244; 22733779; 22737084; 23071443; 23082758; 23658762; 23699410; 24092876; 24289879; 24398368; 24680699; 24813173; 24979807; 25154396; 25294943; 25642644; 25687947; 25824290; 25848931; 26293305; 26321638; 26380810; 26656654; 26801178; 26872827; 26896327; 27230753; 27397649; 27727275; 27794539; 27911728; 28195208; 29030610; 29935791; 30018084; 30383747; 30562515; 31138608; 31197356; 31722958; 32339165; 32487456; 32900993; 33563972; 33748138; 33795866; 6816674; 7479892; 7513799; 8625823; 8918893; 9026285; 9053307; 9275195; 9381174; 9461491; 9518620; |
| Motif | |
| Gene Encoded By | |
| Mass | 70,914 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=33.5 uM for angiotensin I {ECO:0000269|PubMed:7775412, ECO:0000269|PubMed:8761461, ECO:0000269|PubMed:9839949}; KM=53.4 uM for N-acetyl-Ser-Asp-Lys-Pro {ECO:0000269|PubMed:7775412, ECO:0000269|PubMed:8761461, ECO:0000269|PubMed:9839949}; KM=2.59 mM for Hip-His-Leu {ECO:0000269|PubMed:7775412, ECO:0000269|PubMed:8761461, ECO:0000269|PubMed:9839949}; KM=10.26 mM for Hip-His-Leu-NH(2) {ECO:0000269|PubMed:7775412, ECO:0000269|PubMed:8761461, ECO:0000269|PubMed:9839949}; KM=372 uM for (Leu5)enkephalin {ECO:0000269|PubMed:7775412, ECO:0000269|PubMed:8761461, ECO:0000269|PubMed:9839949}; KM=1.88 mM for (Leu5)enkephalinamide {ECO:0000269|PubMed:7775412, ECO:0000269|PubMed:8761461, ECO:0000269|PubMed:9839949}; |
| Metal Binding | METAL 367; /note=Zinc; catalytic; METAL 371; /note=Zinc; catalytic; METAL 395; /note=Zinc; catalytic |
| Rhea ID | |
| Cross Reference Brenda | 3.4.15.1; |