KEGG   ENZYME: 3.4.15.1Help
Entry
EC 3.4.15.1                 Enzyme                                 

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
BRITE hierarchy
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
History
EC 3.4.15.1 created 1972, modified 1981, modified 1989, modified 1996, modified 2011
Orthology
K01283  
peptidyl-dipeptidase A
Genes
HSA: 
1636(ACE)
PTR: 
449567(ACE)
PPS: 
GGO: 
PON: 
MCC: 
MCF: 
MMU: 
11421(Ace) 217246(Ace3)
RNO: 
24310(Ace) 498012(Ace3)
CGE: 
HGL: 
TUP: 
CFA: 
AML: 
FCA: 
BTA: 
100295485(ACE3) 509484(ACE)
BOM: 
PHD: 
CHX: 
OAS: 
554335(ACE)
SSC: 
CFR: 
BACU: 
LVE: 
ECB: 
MYB: 
MYD: 
PALE: 
SHR: 
OAA: 
GGA: 
419953(ACE)
MGP: 
TGU: 
FAB: 
PHI: 
APLA: 
FPG: 
FCH: 
CLV: 
ASN: 
AMJ: 
PSS: 
CMY: 
ACS: 
PBI: 
XTR: 
DRE: 
565980(ace)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
CMK: 
BFO: 
CIN: 
SPU: 
DME: 
Dmel_CG10142(Ance-5) Dmel_CG10593(Acer) Dmel_CG16869(Ance-2) Dmel_CG17988(Ance-3) Dmel_CG8196(Ance-4) Dmel_CG8827(Ance)
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
AGA: 
AAG: 
CQU: 
AME: 
408536(GB16675)
NVI: 
TCA: 
BMOR: 
API: 
PHU: 
ISC: 
CEL: 
CBR: 
CBG14607(Cbr-acn-1)
BMY: 
LOA: 
TSP: 
NVE: 
HMG: 
TAD: 
XCC: 
XCB: 
XCA: 
XCP: 
XCV: 
XAC: 
XCI: 
XAX: 
XAO: 
XOO: 
XOM: 
XOP: 
XOR: 
XAL: 
XFU: 
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: 
AMAL: 
AMAE: 
AMAO: 
AMAD: 
AMAI: 
AMAG: 
ALT: 
GAG: 
GNI: 
TTU: 
LLO: 
KKO: 
SAGA: 
ADE: 
ACP: 
AFW: 
ANK: 
MXA: 
MFU: 
MSD: 
CCX: 
SUR: 
SCL: 
SCU: 
HOH: 
CAK: 
PZU: 
AEX: 
PSF: 
MMR: 
HNE: 
HBA: 
NPP: 
SAL: 
SWI: 
SPHM: 
SSY: 
ELI: 
BIF: 
RRD: 
ABA: 
TSA: 
TRS: 
SUS: 
GBA: 
SACI: 
GVI: 
GLJ: 
BACC: 
HSW: 
HYM: 
OHO: 
CCZ: 
CEX: 
 » show all
Taxonomy
Reference
1  [PMID:2849100]
  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.
  Sequence
[hsa:1636]
Reference
2  [PMID:2554286]
  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.
  Sequence
[hsa:1636]
Reference
3  [PMID:1320019]
  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.
Reference
4  [PMID:7674927]
  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

DBGET integrated database retrieval system