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: 100980711 100981368 103784926
GGO: 101139668 101145787
PON: 100453403(ACE) 100453767
NLE: 100592115 100602761(ACE)
MCC: 100428661(ACE)
MCF: 102127700 102128376(ACE)
CSAB: 103243232 103243233
RRO: 104675473 104675505
CJC: 100408147(ACE)
SBQ: 101052117(ACE)
MMU: 11421(Ace) 217246(Ace3)
RNO: 24310(Ace) 498012(Ace3)
CGE: 100753209(Ace3) 103158533(Ace)
HGL: 101701835(Ace) 101703133
OCU: 100009274(ACE) 103351595
CFA: 100856208 610668(ACE)
FCA: 101083124 101094061(ACE)
BTA: 100295485(ACE3) 509484(ACE)
CHX: 102171917(ACE) 106503207
OAS: 105613829 554335(ACE)
SSC: 100515049 613133(ACE)
LVE: 103087287
ECB: 100064777 100064801(ACE)
EAI: 106835520(ACE) 106835568
MYB: 102243978(ACE)
MYD: 102756093(ACE)
HAI: 109380275 109380308(ACE)
PALE: 102880255 102890071(ACE)
MDO: 100025797(ACE)
SHR: 100932537(ACE) 100932800
GGA: 419953(ACE)
MGP: 100542100(ACE)
CJO: 107325232(ACE)
APLA: 101802065(ACE)
ACYG: 106045989(ACE)
TGU: 100217841(ACE)
GFR: 102032473(ACE)
FAB: 101819593(ACE)
PHI: 102111483(ACE)
PMAJ: 107215323(ACE)
CCW: 104698643(ACE)
FPG: 101924109(ACE)
FCH: 102048145(ACE)
CLV: 102083877(ACE)
EGZ: 104134883(ACE)
AAM: 106497416(ACE)
ASN: 102374457(ACE)
AMJ: 102573284(ACE)
PSS: 102443828(ACE)
CMY: 102933955(ACE)
CPIC: 101930790(ACE)
ACS: 100558092(ace)
PVT: 110080291(ACE)
PBI: 103067603(ACE)
GJA: 107125675(ACE)
XTR: 100144634(ace)
NPR: 108785994(ACE)
DRE: 565980(ace)
SGH: 107557358(ace) 107598651
CCAR: 109060366(ace) 109099167
IPU: 108274082(ace)
AMEX: 103040258(ace)
TRU: 101076790(ace)
LCO: 104923252(ace)
NCC: 104966409(ace)
MZE: 101470840(ace)
XMA: 102221242(ace) 102238075
PRET: 103481980(ace) 103482159
CSEM: 103382106(ace)
LCF: 108875837(ace)
HCQ: 109509686 109515983(ace)
BPEC: 110159607(ace)
ELS: 105024522(ace)
SFM: 108928079(ace)
CMK: 103187713(ace)
CIN: 100180899
DME: Dmel_CG10142(Ance-5) Dmel_CG10593(Acer) Dmel_CG16869(Ance-2) Dmel_CG17988(Ance-3) Dmel_CG8196(Ance-4) Dmel_CG8827(Ance)
DSI: Dsimw501_GD10112(Dsim_GD10112) Dsimw501_GD23554(Dsim_GD23554) Dsimw501_GD23936(Dsim_Ance) Dsimw501_GD23937(Dsim_GD23937) Dsimw501_GD23939(Dsim_GD23939) Dsimw501_GD24910(Dsim_GD24910)
TUT: 107368139
CEL: CELE_C42D8.5(acn-1)
CBR: CBG14607(Cbr-acn-1)
BMY: Bm1_31085
HMG: 100210213
XCC: XCC1116
XCB: XC_3130
XCP: XCR_1338
XCV: XCV1249
XAX: XACM_1192
XAC: XAC1217
XOO: XOO3539
XOM: XOO3345(XOO3345)
XOP: PXO_04473
XOR: XOC_1282
XAL: XALC_0887
SML: Smlt3574
SMT: Smal_2996
SMZ: SMD_3147
PSUW: WQ53_02775
PSD: DSC_06070
LAB: LA76x_3622(ace)
LCP: LC55x_3591(ace)
LEZ: GLE_1570
LEM: LEN_3391
DKO: I596_1523
SON: SO_2494
SDN: Sden_2117
SFR: Sfri_1887
SAZ: Sama_1817
SLO: Shew_2053
SSE: Ssed_2057
SPL: Spea_2340
SWD: Swoo_2544
SWP: swp_2383
SVO: SVI_2322
SPSW: Sps_01127
CPS: CPS_1585
PSEO: OM33_11595
PSPO: PSPO_a1844
PART: PARC_a2553
AMAL: I607_08070
AMAE: I876_08335
AMAO: I634_08440
AMAD: I636_08870
AMAI: I635_09140
AMAG: I533_08380
AMAC: MASE_07965
GNI: GNIT_1032
SAGA: M5M_17395
LLO: LLO_1982
KKO: Kkor_1388
KGE: TQ33_1115
ADE: Adeh_2024
MXA: MXAN_3581
HOH: Hoch_6422
CAK: Caul_0184
PZU: PHZ_c0316
PSF: PSE_0360
HNE: HNE_1947
HBA: Hbal_0598
SAL: Sala_0456
SPHP: LH20_16505
SMAZ: LH19_18700
SGI: SGRAN_3476(ace)
SPHU: SPPYR_0141
SWI: Swit_2667
SPHD: HY78_12175
SPHM: G432_00930
STAX: MC45_04745
SPHI: TS85_09285
SSAN: NX02_12980
SPKC: KC8_02095
SSY: SLG_23650
SPHR: BSY17_2968
BLAS: BSY18_285
ELI: ELI_07405
AAY: WYH_00229
ASOC: CB4_03604
GVI: gll3143
GLJ: GKIL_2224
SACI: Sinac_2369
SUS: Acid_4844
GBA: J421_0092
HSW: Hsw_1814
FBU: UJ101_00896(ACE)
CEX: CSE_15400
CABY: Cabys_1631
 » 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 85:9386-90 (1988)
DOI:10.1073/pnas.85.24.9386
  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 86:7741-5 (1989)
DOI:10.1073/pnas.86.20.7741
  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 267:13398-405 (1992)
Reference
4  [PMID:7674927]
  Authors
Corvol P, Williams TA, Soubrier F.
  Title
Peptidyl dipeptidase A: angiotensin I-converting enzyme.
  Journal
Methods Enzymol 248:283-305 (1995)
Other DBs
ExplorEnz - The Enzyme Database: 3.4.15.1
IUBMB Enzyme Nomenclature: 3.4.15.1
ExPASy - ENZYME nomenclature database: 3.4.15.1
BRENDA, the Enzyme Database: 3.4.15.1
CAS: 9015-82-1
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