| Entry |
|
| Name |
peptidyl-dipeptidase A;
dipeptidyl carboxypeptidase I;
peptidase P;
dipeptide hydrolase (ambiguous);
peptidyl dipeptidase;
angiotensin converting enzyme;
kininase II;
angiotensin I-converting enzyme;
carboxycathepsin;
dipeptidyl carboxypeptidase;
peptidyl dipeptidase I;
peptidyl-dipeptide hydrolase;
peptidyldipeptide hydrolase;
endothelial cell peptidyl dipeptidase;
ACE;
peptidyl dipeptidase-4;
PDH;
peptidyl dipeptide hydrolase;
DCP
|
| Class |
Hydrolases;
Acting on peptide bonds (peptidases);
Peptidyl-dipeptidases
 |
| Reaction(IUBMB) |
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
|
| Comment |
A Cl--dependent, zinc glycoprotein that is generally membrane-bound. A potent inhibitor is captopril. Important in elevation of blood pressure, through formation of angiotensin II (vasoconstrictor) and destruction of bradykinin (vasodilator). Two molecular forms exist in mammalian tissues, a widely-distributed somatic form of 150- to 180-kDa that contains two non-identical catalytic sites, and a testicular form of 90- to 100-kDa that contains only a single catalytic site. Type example of peptidase family M2
|
| Orthology |
|
| Genes |
HSA: | | PTR: | | PPS: | | GGO: | | PON: | | MCC: | | MMU: | | RNO: | | CFA: | | AML: | | FCA: | | BTA: | | SSC: | | ECB: | | MDO: | | SHR: | | GGA: | | MGP: | | TGU: | | ACS: | | XTR: | | DRE: | | TRU: | | OLA: | | BFO: | | CIN: | | SPU: | | DME: | | DPO: | | DAN: | | DER: | | DPE: | | DSE: | | DSI: | | DWI: | | DYA: | | DGR: | | DMO: | | DVI: | | AGA: | | AAG: | | CQU: | | AME: | | NVI: | | TCA: | | API: | | PHU: | | ISC: | | CEL: | | CBR: | | BMY: | | TSP: | | NVE: | | HMG: | | TAD: | | XCC: | | XCB: | | XCA: | | XCV: | | XCP: | | XAC: | | XAX: | | XAO: | | XOO: | | XOM: | | XOP: | | XOR: | | XAL: | | XCI: | | SML: | | SMT: | | BUJ: | | SMZ: | | PSU: | | PSD: | | SON: | | SDN: | | SFR: | | SAZ: | | SBL: | | SBM: | | SBN: | | SBP: | | SBT: | | SBS: | | SBB: | | SLO: | | SSE: | | SPL: | | SHE: | | SHM: | | SHN: | | SWD: | | SWP: | | SVO: | | CPS: | | AMC: | | AMAC: | | AMB: | | AMG: | | AMK: | | AMAA: | | ALT: | | GAG: | | GNI: | | TTU: | | LLO: | | KKO: | | SAGA: | | ADE: | | ACP: | | AFW: | | ANK: | | MXA: | | MFU: | | MSD: | | CCX: | | SUR: | | SCL: | | HOH: | | CAK: | | PZU: | | AEX: | | PSF: | | MMR: | | HNE: | | HBA: | | NPP: | | SAL: | | SWI: | | SPHM: | | SSY: | | ELI: | | ABA: | | TSA: | | TRS: | | SUS: | | OHO: | | SACI: | | GVI: | | CEX: | | » show all
 |
| Reference |
|
| Authors |
Soubrier F, Alhenc-Gelas F, Hubert C, Allegrini J, John M, Tregear G, Corvol P. |
| Title |
Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning. |
| Journal |
Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 9386-90. |
| Organism |
|
| Reference |
|
| Authors |
Ehlers MR, Fox EA, Strydom DJ, Riordan JF. |
| Title |
Molecular cloning of human testicular angiotensin-converting enzyme: the testis isozyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme. |
| Journal |
Proc. Natl. Acad. Sci. U. S. A. 86 (1989) 7741-5. |
| Organism |
|
| Reference |
|
| Authors |
Wei L, Clauser E, Alhenc-Gelas F, Corvol P. |
| Title |
The two homologous domains of human angiotensin I-converting enzyme interact differently with competitive inhibitors. |
| Journal |
J. Biol. Chem. 267 (1992) 13398-405. |
| Organism |
|
| Reference |
|
| Authors |
Corvol P, Williams TA, Soubrier F. |
| Title |
Peptidyl dipeptidase A: angiotensin I-converting enzyme. |
| Journal |
Methods. Enzymol. 248 (1995) 283-305. |
| Other DBs |
ExplorEnz - The Enzyme Database: IUBMB Enzyme Nomenclature: ExPASy - ENZYME nomenclature database: BRENDA, the Enzyme Database: CAS: 9015-82-1 |