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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:07:45
Primary Accession Number DB00178
Secondary Accession Number
  • APRD00009
Name Ramipril
Drug Type
  • Approved
  • Small Molecule
Description A long-acting angiotensin-converting enzyme inhibitor. It is a prodrug that is transformed in the liver to its active metabolite ramiprilat. [PubChem]
Synonyms
  1. Ramiprilum [Latin]
Brand Names
  1. Acovil
  2. Altace
  3. Carasel
  4. Cardace
  5. Delix
  6. Hytren
  7. Lostapres
  8. Pramace
  9. Quark
  10. Ramace
  11. Triatec
  12. Tritace
  13. Unipril
  14. Vesdil
Brand Mixtures Not Available
Chemical IUPAC Name (2S,3aS,6aS)-1-[(2S)-2-[[(2S)-1-ethoxy-1-oxo-4-phenylbutan-2-yl]amino]propanoyl]-3,3a,4,5,6,6a-hexahydro-2H-cyclopenta[d]pyrrole-2-carboxylic acid
Chemical Formula C23H32N2O5
Chemical Structure Structure
CAS Registry Number 87333-19-5
InChI Identifier InChI=1/C23H32N2O5/c1-3-30-23(29)18(13-12-16-8-5-4-6-9-16)24-15(2)21(26)25-19-11-7-10-17(19)14-20(25)22(27)28/h4-6,8-9,15,17-20,24H,3,7,10-14H2,1-2H3,(H,27,28)/t15-,17-,18-,19-,20-/m0/s1/f/h27H
InChI Key HDACQVRGBOVJII-ZUWNEQGUDP
KEGG Drug D00421 Link Image
KEGG Compound Not Available
PubChem Compound 5362129 Link Image
PubChem Substance 193088 Link Image
ChEBI ID Not Available
PharmGKB ID Not Available
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 02221829 Link Image
RxList Link http://www.rxlist.com/cgi/generic/ramipril.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Ramipril Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS)
Synthesis Reference E. H. Gold et al., U.S. Pat. 4,587,258 (1967).
Average Molecular Weight 416.5106
Monoisotopic Molecular Weight 416.2311
State Solid
Melting Point 109 oC
Experimental Water Solubility 3.5mg/L Source: PhysProp
Predicted Water Solubility 3.90e-02 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 2.9 Source: PhysProp
Predicted LogP 0.92 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -4.03 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point Not Available
Mass Spectrum Not Available
MOL File Show Link Image | Download Link Image
SDF File Show Link Image | Download Link Image
PDB File Show Link Image | Download Link Image
2D Structure
3D Structure
Experimental PDB ID 1UZF Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES CCOC(=O)[C@H](CCC1=CC=CC=C1)N[C@@H](C)C(=O)N1[C@H]2CCC[C@H]2C[C@H]1C(O)=O
Canonical SMILES CCOC(=O)C(CCC1=CC=CC=C1)NC(C)C(=O)N1C2CCCC2CC1C(O)=O
Drug Category
  • Angiotensin-converting Enzyme Inhibitors
  • Antihypertensive Agents
ATC Codes
AHFS Codes
  • 24:32.04
Indication For diuretics and digitalis in congestive heart failure as adjunctive therapy and for use in prophylaxis in post MI.
Pharmacology Ramipril is an angiotensin-converting enzyme (ACE) inhibitor similar to benazepril, fosinopril, and quinapril. An inactive prodrug, ramipril is converted to ramiprilat in the liver and is used to treat hypertension and heart failure, to reduce proteinuria and renal disease in patients with nephropathies, and to prevent stroke, myocardial infarction, and cardiac death in high-risk patients.
Mechanism of Action Ramiprilat, the active metabolite, competes with angiotensin I for binding at the angiotensin-converting enzyme, blocking the conversion of angiotensin I to angiotensin II. As angiotensin II is a vasoconstrictor and a negative-feedback mediator for renin activity, lower concentrations result in a decrease in blood pressure and an increase in plasma renin. Ramiprilat may also act on kininase II, an enzyme identical to ACE that degrades the vasodilator bradykinin.
Absorption The extent of absorption is at least 50-60% and is not significantly influenced by the presence of food in the GI tract, although the rate of absorption is reduced.
Toxicity The most likely clinical manifestations would be symptoms attributable to hypotension. LD50 = 10933 mg/kg (orally in mice).
Protein Binding Protein binding of ramipril is about 73% and that of ramiprilat about 56%. The absolute bioavailabilities of ramipril and ramiprilat were 28% and 44%, respectively.
Biotransformation Hepatic. Ramipril is a prodrug and is converted to the active metabolite ramiprilat by liver esterase enzymes.
Half Life 2-4 hours
Dosage Forms
Form Route
Capsule Oral
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Amiloride Increased risk of hyperkaliemia
Drospirenone Increased risk of hyperkaliemia
Lithium The ACE inhibitor increases serum levels of lithium
Potassium Increased risk of hyperkaliemia
Spironolactone Increased risk of hyperkaliemia
Tizanidine Tizanidine increases the risk of hypotension with the ACE inhibitor
Triamterene Increased risk of hyperkaliemia
Food Interactions
  • Take without regard to meals. Avoid alcohol.
Pathways
Name SMPDB Link KEGG Link
Ramipril Pathway SMP00154 Link Image
General References
  1. Drugs.com Link Image
  2. Wikipedia Link Image
  3. RxList Link Image
Organisms Affected
  • Humans and other mammals
Targets
  1. Angiotensin-converting enzyme, testis-specific isoform
  2. Angiotensin-converting enzyme, somatic isoform
Drug Target 1 [top]
Target 1 ID 143
Target 1 Name Angiotensin-converting enzyme, testis-specific isoform
Target 1 Synonyms
  1. ACE-T
  2. Angiotensin-converting enzyme, testis-specific isoform precursor
  3. Dipeptidyl carboxypeptidase I
  4. EC 3.2.1.-
  5. EC 3.4.15.1
  6. Kininase II
Target 1 Gene Name ACE
Target 1 Protein Sequence >Angiotensin-converting enzyme, testis-specific isoform precursor 
MGQGWATAGLPSLLFLLLCYGHPLLVPSQEASQQVTVTHGTSSQATTSSQTTTHQATAHQ
TSAQSPNLVTDEAEASKFVEEYDRTSQVVWNEYAEANWNYNTNITTETSKILLQKNMQIA
NHTLKYGTQARKFDVNQLQNTTIKRIIKKVQDLERAALPAQELEEYNKILLDMETTYSVA
TVCHPNGSCLQLEPDLTNVMATSRKYEDLLWAWEGWRDKAGRAILQFYPKYVELINQAAR
LNGYVDAGDSWRSMYETPSLEQDLERLFQELQPLYLNLHAYVRRALHRHYGAQHINLEGP
IPAHLLGNMWAQTWSNIYDLVVPFPSAPSMDTTEAMLKQGWTPRRMFKEADDFFTSLGLL
PVPPEFWNKSMLEKPTDGREVVCHASAWDFYNGKDFRIKQCTTVNLEDLVVAHHEMGHIQ
YFMQYKDLPVALREGANPGFHEAIGDVLALSVSTPKHLHSLNLLSSEGGSDEHDINFLMK
MALDKIAFIPFSYLVDQWRWRVFDGSITKENYNQEWWSLRLKYQGLCPPVPRTQGDFDPG
AKFHIPSSVPYIRYFVSFIIQFQFHEALCQAAGHTGPLHKCDIYQSKEAGQRLATAMKLG
FSRPWPEAMQLITGQPNMSASAMLSYFKPLLDWLRTENELHGEKLGWPQYNWTPNSARSE
GPLPDSGRVSFLGLDLDAQQARVGQWLLLFLGIALLVATLGLSQRLFSIRHRSLHRHSHG
PQFGSEVELRHS
Target 1 Number of Residues 744
Target 1 Molecular Weight 83331
Target 1 Theoretical pI 6.60
Target 1 GO Classification
Function
peptidyl-dipeptidase A activity
binding
ion binding
cation binding
transition metal ion binding
zinc ion binding
catalytic activity
hydrolase activity
peptidase activity
metallopeptidase activity
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
cellular protein metabolism
proteolysis
Component
cell
membrane
Target 1 General Function Involved in metallopeptidase activity
Target 1 Specific Function Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety
Target 1 Pathways Not Available
Target 1 Reactions
  • 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 COFACTOR Zinc INHIBITOR (S)-N-[3-(3,4-Methylenedioxyphenyl)-2-(mercaptomethyl)-1-oxoprolyl]g lycine; (S)-N-[3-(3,4-Methylenedioxyphenyl)-2-(mercaptomethyl)-1-oxoprolyl]- (S)-alanine; (S)-N-[3-(3,4-Methylenedioxyphenyl)-2-(acetylthio)methyl-1-oxoprolyl ]glycine benzyl ester; (S)-N-[3-(3,4-Methylenedioxyphenyl)-2-(acetylthio)methyl-1-oxoprolyl ]-(S)-alanine benzyl ester EFFECTOR Chloride
Target 1 Pfam Domain Function
Target 1 Signals
  • 1-31
Target 1 Transmembrane Regions
  • 685-701
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 338667 Link Image
Target 1 UniProtKB/Swiss-Prot ID P22966 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name ACET_HUMAN Link Image
Target 1 PDB ID 1UZF Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location
  • Cell membrane
  • single-pass type I membrane protein. Processed form:Secreted protein. A soluble form
Target 1 Gene Sequence >2199 bp 
ATGGGCCAGGGTTGGGCTACTGCAGGACTTCCCAGCCTCCTCTTCCTGCTGCTCTGCTAC
GGGCACCCTCTGCTGGTCCCCAGCCAGGAGGCATCCCAACAGGTGACAGTCACCCATGGG
ACAAGCAGCCAGGCAACAACCAGCAGCCAGACAACCACCCACCAGGCGACGGCCCACCAG
ACATCAGCCCAGAGCCCAAACCTGGTGACTGATGAGGCTGAGGCCAGCAAGTTTGTGGAG
GAATATGACCGGACATCCCAGGTGGTGTGGAACGAGTATGCCGAGGCCAACTGGAACTAC
AACACCAACATCACCACAGAGACCAGCAAGATTCTGCTGCAGAAGAACATGCAAATAGCC
AACCACACCCTGAAGTACGGCACCCAGGCCAGGAAGTTTGATGTGAACCAGTTGCAGAAC
ACCACTATCAAGCGGATCATAAAGAAGGTTCAGGACCTAGAACGGGCAGCGCTGCCTGCC
CAGGAGCTGGAGGAGTACAACAAGATCCTGTTGGATATGGAAACCACCTACAGCGTGGCC
ACTGTGTGCCACCCGAATGGCAGCTGCCTGCAGCTCGAGCCAGATCTGACGAATGTGATG
GCCACATCCCGGAAATATGAAGACCTGTTATGGGCATGGGAGGGCTGGCGAGACAAGGCG
GGGAGAGCCATCCTCCAGTTTTACCCGAAATACGTGGAACTCATCAACCAGGCTGCCCGG
CTCAATGGCTATGTAGATGCAGGGGACTCGTGGAGGTCTATGTACGAGACACCATCCCTG
GAGCAAGACCTGGAGCGGCTCTTCCAGGAGCTGCAGCCACTCTACCTCAACCTGCATGCC
TACGTGCGCCGGGCCCTGCACCGTCACTACGGGGCCCAGCACATCAACCTGGAGGGGCCC
ATTCCTGCTCACCTGCTGGGGAACATGTGGGCGCAGACCTGGTCCAACATCTATGACTTG
GTGGTGCCCTTCCCTTCAGCCCCCTCGATGGACACCACAGAGGCTATGCTAAAGCAGGGC
TGGACGCCCAGGAGGATGTTTAAGGAGGCTGATGATTTCTTCACCTCCCTGGGGCTGCTG
CCCGTGCCTCCTGAGTTCTGGAACAAGTCGATGCTGGAGAAGCCAACCGACGGGCGGGAG
GTGGTCTGCCACGCCTCGGCCTGGGACTTCTACAACGGCAAGGACTTCCGGATCAAGCAG
TGCACCACCGTGAACTTGGAGGACCTGGTGGTGGCCCACCACGAAATGGGCCACATCCAG
TATTTCATGCAGTACAAAGACTTACCTGTGGCCTTGAGGGAGGGTGCCAACCCCGGCTTC
CATGAGGCCATTGGGGACGTGCTAGCCCTCTCAGTGTCTACGCCCAAGCACCTGCACAGT
CTCAACCTGCTGAGCAGTGAGGGTGGCAGCGACGAGCATGACATCAACTTTCTGATGAAG
ATGGCCCTTGACAAGATCGCCTTTATCCCCTTCAGCTACCTCGTCGATCAGTGGCGCTGG
AGGGTATTTGATGGAAGCATCACCAAGGAGAACTATAACCAGGAGTGGTGGAGCCTCAGG
CTGAAGTACCAGGGCCTCTGCCCCCCAGTGCCCAGGACTCAAGGTGACTTTGACCCAGGG
GCCAAGTTCCACATTCCTTCTAGCGTGCCTTACATCAGGTACTTCGTCAGCTTCATCATC
CAGTTCCAGTTCCACGAGGCACTGTGCCAGGCAGCTGGCCACACGGGCCCCCTGCACAAG
TGTGACATCTACCAGTCCAAGGAGGCCGGGCAGCGCCTGGCGACCGCCATGAAGCTGGGC
TTCAGTAGGCCGTGGCCGGAAGCCATGCAGCTGATCACGGGCCAGCCCAACATGAGCGCC
TCGGCCATGTTGAGCTACTTCAAGCCGCTGCTGGACTGGCTCCGCACGGAGAACGAGCTG
CATGGGGAGAAGCTGGGCTGGCCGCAGTACAACTGGACGCCGAACTCCGCTCGCTCAGAA
GGGCCCCTCCCAGACAGCGGCCGCGTCAGCTTCCTGGGCCTGGACCTGGATGCGCAGCAG
GCCCGCGTGGGCCAGTGGCTGCTGCTCTTCCTGGGCATCGCCCTGCTGGTAGCCACCCTG
GGCCTCAGCCAGCGGCTCTTCAGCATCCGCCACCGCAGCCTCCACCGGCACTCCCACGGG
CCCCAGTTCGGCTCCGAGGTGGAGCTGAGACACTCCTGA
Target 1 GenBank Gene ID
Target 1 GeneCard ID ACE Link Image
Target 1 GenAtlas ID ACE Link Image
Target 1 HGNC ID HGNC:2707 Link Image
Target 1 Chromosome Location 17
Target 1 Locus 17q23.3
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Rieder MJ, Taylor SL, Clark AG, Nickerson DA: Sequence variation in the human angiotensin converting enzyme. Nat Genet. 1999 May;22(1):59-62. [PubMed Link Image]
  2. Harmer D, Gilbert M, Borman R, Clark KL: Quantitative mRNA expression profiling of ACE 2, a novel homologue of angiotensin converting enzyme. FEBS Lett. 2002 Dec 4;532(1-2):107-10. [PubMed Link Image]
  3. Ehlers MR, Riordan JF: Angiotensin-converting enzyme: zinc- and inhibitor-binding stoichiometries of the somatic and testis isozymes. Biochemistry. 1991 Jul 23;30(29):7118-26. [PubMed Link Image]
  4. Lattion AL, Soubrier F, Allegrini J, Hubert C, Corvol P, Alhenc-Gelas F: The testicular transcript of the angiotensin I-converting enzyme encodes for the ancestral, non-duplicated form of the enzyme. FEBS Lett. 1989 Jul 31;252(1-2):99-104. [PubMed Link Image]
  5. Ehlers MR, Fox EA, Strydom DJ, Riordan JF: Molecular cloning of human testicular angiotensin-converting enzyme: the testis isozyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme. Proc Natl Acad Sci U S A. 1989 Oct;86(20):7741-5. [PubMed Link Image]
  6. Sturrock ED, Yu XC, Wu Z, Biemann K, Riordan JF: Assignment of free and disulfide-bonded cysteine residues in testis angiotensin-converting enzyme: functional implications. Biochemistry. 1996 Jul 23;35(29):9560-6. [PubMed Link Image]
Target 1 Drug References
  1. Kleinert S: HOPE for cardiovascular disease prevention with ACE-inhibitor ramipril. Heart Outcomes Prevention Evaluation. Lancet. 1999 Sep 4;354(9181):841. [PubMed Link Image]
  2. Teo K, Yusuf S, Sleight P, Anderson C, Mookadam F, Ramos B, Hilbrich L, Pogue J, Schumacher H: Rationale, design, and baseline characteristics of 2 large, simple, randomized trials evaluating telmisartan, ramipril, and their combination in high-risk patients: the Ongoing Telmisartan Alone and in Combination with Ramipril Global Endpoint Trial/Telmisartan Randomized Assessment Study in ACE Intolerant Subjects with Cardiovascular Disease (ONTARGET/TRANSCEND) trials. Am Heart J. 2004 Jul;148(1):52-61. [PubMed Link Image]
  3. Levitt DG, Schoemaker RC: Human physiologically based pharmacokinetic model for ACE inhibitors: ramipril and ramiprilat. BMC Clin Pharmacol. 2006 Jan 6;6:1. [PubMed Link Image]
  4. Cacciapuoti F, Capasso A, Mirra G, De Nicola A, Minicucci F, Gentile S: Prevention of left ventricular hypertrophy by ACE-inhibitor, ramipril in comparison with calcium-channel antagonist, felodipine. Int J Cardiol. 1998 Jan 31;63(2):175-8. [PubMed Link Image]
  5. Kalinowski M, Tepe G, Schieber A, Bruck B, Claussen CD, Duda SH: [Intra-arterial application of the ACE inhibitor ramipril using a microperforated catheter for the prevention of neointimal proliferation after angioplasty in an animal model] Rofo. 1998 Nov;169(5):532-6. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 244
Target 2 Name Angiotensin-converting enzyme, somatic isoform
Target 2 Synonyms
  1. Angiotensin-converting enzyme, somatic isoform precursor
  2. CD143 antigen
  3. Dipeptidyl carboxypeptidase I
  4. EC 3.4.15.1
  5. Kininase II
Target 2 Gene Name ACE
Target 2 Protein Sequence >Angiotensin-converting enzyme, somatic isoform precursor 
MGAASGRRGPGLLLPLPLLLLLPPQPALALDPGLQPGNFSADEAGAQLFAQSYNSSAEQV
LFQSVAASWAHDTNITAENARRQEEAALLSQEFAEAWGQKAKELYEPIWQNFTDPQLRRI
IGAVRTLGSANLPLAKRQQYNALLSNMSRIYSTAKVCLPNKTATCWSLDPDLTNILASSR
SYAMLLFAWEGWHNAAGIPLKPLYEDFTALSNEAYKQDGFTDTGAYWRSWYNSPTFEDDL
EHLYQQLEPLYLNLHAFVRRALHRRYGDRYINLRGPIPAHLLGDMWAQSWENIYDMVVPF
PDKPNLDVTSTMLQQGWNATHMFRVAEEFFTSLELSPMPPEFWEGSMLEKPADGREVVCH
ASAWDFYNRKDFRIKQCTRVTMDQLSTVHHEMGHIQYYLQYKDLPVSLRRGANPGFHEAI
GDVLALSVSTPEHLHKIGLLDRVTNDTESDINYLLKMALEKIAFLPFGYLVDQWRWGVFS
GRTPPSRYNFDWWYLRTKYQGICPPVTRNETHFDAGAKFHVPNVTPYIRYFVSFVLQFQF
HEALCKEAGYEGPLHQCDIYRSTKAGAKLRKVLQAGSSRPWQEVLKDMVGLDALDAQPLL
KYFQPVTQWLQEQNQQNGEVLGWPEYQWHPPLPDNYPEGIDLVTDEAEASKFVEEYDRTS
QVVWNEYAEANWNYNTNITTETSKILLQKNMQIANHTLKYGTQARKFDVNQLQNTTIKRI
IKKVQDLERAALPAQELEEYNKILLDMETTYSVATVCHPNGSCLQLEPDLTNVMATSRKY
EDLLWAWEGWRDKAGRAILQFYPKYVELINQAARLNGYVDAGDSWRSMYETPSLEQDLER
LFQELQPLYLNLHAYVRRALHRHYGAQHINLEGPIPAHLLGNMWAQTWSNIYDLVVPFPS
APSMDTTEAMLKQGWTPRRMFKEADDFFTSLGLLPVPPEFWNKSMLEKPTDGREVVCHAS
AWDFYNGKDFRIKQCTTVNLEDLVVAHHEMGHIQYFMQYKDLPVALREGANPGFHEAIGD
VLALSVSTPKHLHSLNLLSSEGGSDEHDINFLMKMALDKIAFIPFSYLVDQWRWRVFDGS
ITKENYNQEWWSLRLKYQGLCPPVPRTQGDFDPGAKFHIPSSVPYIRYFVSFIIQFQFHE
ALCQAAGHTGPLHKCDIYQSKEAGQRLATAMKLGFSRPWPEAMQLITGQPNMSASAMLSY
FKPLLDWLRTENELHGEKLGWPQYNWTPNSARSEGPLPDSGRVSFLGLDLDAQQARVGQW
LLLFLGIALLVATLGLSQRLFSIRHRSLHRHSHGPQFGSEVELRHS
Target 2 Number of Residues 1327
Target 2 Molecular Weight 149716
Target 2 Theoretical pI 6.36
Target 2 GO Classification
Function
peptidyl-dipeptidase A activity
binding
ion binding
cation binding
transition metal ion binding
zinc ion binding
catalytic activity
hydrolase activity
peptidase activity
metallopeptidase activity
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
cellular protein metabolism
proteolysis
Component
cell
membrane
Target 2 General Function Involved in metallopeptidase activity
Target 2 Specific Function Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator
Target 2 Pathways Not Available
Target 2 Reactions
  • 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 COFACTOR Zinc INHIBITOR (S)-N-[3-(3,4-Methylenedioxyphenyl)-2-(mercaptomethyl)-1-oxoprolyl]g lycine; (S)-N-[3-(3,4-Methylenedioxyphenyl)-2-(mercaptomethyl)-1-oxoprolyl]- (S)-alanine; (S)-N-[3-(3,4-Methylenedioxyphenyl)-2-(acetylthio)methyl-1-oxoprolyl ]glycine benzyl ester; (S)-N-[3-(3,4-Methylenedioxyphenyl)-2-(acetylthio)methyl-1-oxoprolyl ]-(S)-alanine benzyl ester EFFECTOR Chloride
Target 2 Pfam Domain Function
Target 2 Signals
  • 1-29
Target 2 Transmembrane Regions
  • 1260-1276
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 178286 Link Image
Target 2 UniProtKB/Swiss-Prot ID P12821 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name ACE_HUMAN Link Image
Target 2 PDB ID 1UZF Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location
  • Cell membrane
  • single-pass type I membrane protein. Processed form:Secreted protein. A soluble form
Target 2 Gene Sequence >3921 bp 
ATGGGGGCCGCCTCGGGCCGCCGGGGGCCGGGGCTGCTGCTGCCGCTGCCGCTGCTGTTG
CTGCTGCCGCCGCAGCCCGCCCTGGCGTTGGACCCCGGGCTGCAGCCCGGCAACTTTTCT
GCTGACGAGGCCGGGGCGCAGCTCTTCGCGCAGAGCTACAACTCCAGCGCCGAACAGGTG
CTGTTCCAGAGCGTGGCCGCCAGCTGGGCGCACGACACCAACATCACCGCGGAGAATGCA
AGGCGCCAGGAGGAAGCAGCCCTGCTCAGCCAGGAGTTTGCGGAGGCCTGGGGCCAGAAG
GCCAAGGAGCTGTATGAACCGATCTGGCAGAACTTCACGGACCCGCAGCTGCGCAGGATC
ATCGGAGCTGTGCGAACCCTGGGCTCTGCCAACCTGCCCCTGGCTAAGCGGCAGCAGTAC
AACGCCCTGCTAAGCAACATGAGCAGGATCTACTCCACCGCCAAGGTCTGCCTCCCCAAC
AAGACTGCCACCTGCTGGTCCCTGGACCCAGATCTCACCAACATCCTGGCTTCCTCGCGA
AGCTACGCCATGCTCCTGTTTGCCTGGGAGGGCTGGCACAACGCTGCGGGCATCCCGCTG
AAACCGCTGTACGAGGATTTCACTGCCCTCAGCAATGAAGCCTACAAGCAGGACGGCTTC
ACAGACACGGGGGCCTACTGGCGCTCCTGGTACAACTCCCCCACCTTCGAGGACGATCTG
GAACACCTCTACCAACAGCTAGAGCCCCTCTACCTGAACCTCCATGCCTTCGTCCGCCGC
GCACTGCATCGCCGATACGGAGACAGATACATCAACCTCAGGGGACCCATCCCTGCTCAT
CTGCTGGGAGACATGTGGGCCCAGAGCTGGGAAAACATCTACGACATGGTGGTGCCTTTC
CCAGACAAGCCCAACCTCGATGTCACCAGTACTATGCTGCAGCAGGGCTGGAACGCCACG
CACATGTTCCGGGTGGCAGAGGAGTTCTTCACCTCCCTGGAGCTCTCCCCCATGCCTCCC
GAGTTCTGGGAAGGGTCGATGCTGGAGAAGCCGGCCGACGGGCGGGAAGTGGTGTGCCAC
GCCTCGGCTTGGGACTTCTACAACAGGAAAGACTTCAGGATCAAGCAGTGCACACGGGTC
ACGATGGACCAGCTCTCCACAGTGCACCATGAGATGGGCCATATACAGTACTACCTGCAG
TACAAGGATCTGCCCGTCTCCCTGCGTCGGGGGGCCAACCCCGGCTTCCATGAGGCCATT
GGGGACGTGCTGGCGCTCTCGGTCTCCACTCCTGAACATCTGCACAAAATCGGCCTGCTG
GACCGTGTCACCAATGACACGGAAAGTGACATCAATTACTTGCTAAAAATGGCACTGGAA
AAAATTGCCTTCCTGCCCTTTGGCTACTTGGTGGACCAGTGGCGCTGGGGGGTCTTTAGT
GGGCGTACCCCCCCTTCCCGCTACAACTTCGACTGGTGGTATCTTCGAACCAAGTATCAG
GGGATCTGTCCTCCTGTTACCCGAAACGAAACCCACTTTGATGCTGGAGCTAAGTTTCAT
GTTCCAAATGTGACACCATACATCAGGTACTTTGTGAGTTTTGTCCTGCAGTTCCAGTTC
CATGAAGCCCTGTGCAAGGAGGCAGGCTATGAGGGCCCACTGCACCAGTGTGACATCTAC
CGGTCCACCAAGGCAGGGGCCAAGCTCCGGAAGGTGCTGCAGGCTGGCTCCTCCAGGCCC
TGGCAGGAGGTGCTGAAGGACATGGTCGGCTTAGATGCCCTGGATGCCCAGCCGCTGCTC
AAGTACTTCCAGCCAGTCACCCAGTGGCTGCAGGAGCAGAACCAGCAGAACGGCGAGGTC
CTGGGCTGGCCCGAGTACCAGTGGCACCCGCCGTTGCCTGACAACTACCCGGAGGGCATA
GACCTGGTGACTGATGAGGCTGAGGCCAGCAAGTTTGTGGAGGAATATGACCGGACATCC
CAGGTGGTGTGGAACGAGTATGCCGAGGCCAACTGGAACTACAACACCAACATCACCACA
GAGACCAGCAAGATTCTGCTGCAGAAGAACATGCAAATAGCCAACCACACCCTGAAGTAC
GGCACCCAGGCCAGGAAGTTTGATGTGAACCAGTTGCAGAACACCACTATCAAGCGGATC
ATAAAGAAGGTTCAGGACCTAGAACGGGCAGCGCTGCCTGCCCAGGAGCTGGAGGAGTAC
AACAAGATCCTGTTGGATATGGAAACCACCTACAGCGTGGCCACTGTGTGCCACCCGAAT
GGCAGCTGCCTGCAGCTCGAGCCAGATCTGACGAATGTGATGGCCACATCCCGGAAATAT
GAAGACCTGTTATGGGCATGGGAGGGCTGGCGAGACAAGGCGGGGAGAGCCATCCTCCAG
TTTTACCCGAAATACGTGGAACTCATCAACCAGGCTGCCCGGCTCAATGGCTATGTAGAT
GCAGGGGACTCGTGGAGGTCTATGTACGAGACACCATCCCTGGAGCAAGACCTGGAGCGG
CTCTTCCAGGAGCTGCAGCCACTCTACCTCAACCTGCATGCCTACGTGCGCCGGGCCCTG
CACCGTCACTACGGGGCCCAGCACATCAACCTGGAGGGGCCCATTCCTGCTCACCTGCTG
GGGAACATGTGGGCGCAGACCTGGTCCAACATCTATGACTTGGTGGTGCCCTTCCCTTCA
GCCCCCTCGATGGACACCACAGAGGCTATGCTAAAGCAGGGCTGGACGCCCAGGAGGATG
TTTAAGGAGGCTGATGATTTCTTCACCTCCCTGGGGCTGCTGCCCGTGCCTCCTGAGTTC
TGGAACAAGTCGATGCTGGAGAAGCCAACCGACGGGCGGGAGGTGGTCTGCCACGCCTCG
GCCTGGGACTTCTACAACGGCAAGGACTTCCGGATCAAGCAGTGCACCACCGTGAACTTG
GAGGACCTGGTGGTGGCCCACCACGAAATGGGCCACATCCAGTATTTCATGCAGTACAAA
GACTTACCTGTGGCCTTGAGGGAGGGTGCCAACCCCGGCTTCCATGAGGCCATTGGGGAC
GTGCTAGCCCTCTCAGTGTCTACGCCCAAGCACCTGCACAGTCTCAACCTGCTGAGCAGT
GAGGGTGGCAGCGACGAGCATGACATCAACTTTCTGATGAAGATGGCCCTTGACAAGATC
GCCTTTATCCCCTTCAGCTACCTCGTCGATCAGTGGCGCTGGAGGGTATTTGATGGAAGC
ATCACCAAGGAGAACTATAACCAGGAGTGGTGGAGCCTCAGGCTGAAGTACCAGGGCCTC
TGCCCCCCAGTGCCCAGGACTCAAGGTGACTTTGACCCAGGGGCCAAGTTCCACATTCCT
TCTAGCGTGCCTTACATCAGGTACTTTGTCAGCTTCATCATCCAGTTCCAGTTCCACGAG
GCACTGTGCCAGGCAGCTGGCCACACGGGCCCCCTGCACAAGTGTGACATCTACCAGTCC
AAGGAGGCCGGGCAGCGCCTGGCGACCGCCATGAAGCTGGGCTTCAGTAGGCCGTGGCCG
GAAGCCATGCAGCTGATCACGGGCCAGCCCAACATGAGCGCCTCGGCCATGTTGAGCTAC
TTCAAGCCGCTGCTGGACTGGCTCCGCACGGAGAACGAGCTGCATGGGGAGAAGCTGGGC
TGGCCGCAGTACAACTGGACGCCGAACTCCGCTCGCTCAGAAGGGCCCCTCCCAGACAGC
GGCCGCGTCAGCTTCCTGGGCCTGGACCTGGATGCGCAGCAGGCCCGCGTGGGCCAGTGG
CTGCTGCTCTTCCTGGGCATCGCCCTGCTGGTAGCCACCCTGGGCCTCAGCCAGCGGCTC
TTCAGCATCCGCCACCGCAGCCTCCACCGGCACTCCCACGGGCCCCAGTTCGGCTCCGAG
GTGGAGCTGAGACACTCCTGA
Target 2 GenBank Gene ID
Target 2 GeneCard ID ACE Link Image
Target 2 GenAtlas ID ACE Link Image
Target 2 HGNC ID HGNC:2707 Link Image
Target 2 Chromosome Location 17
Target 2 Locus 17q23.3
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Rieder MJ, Taylor SL, Clark AG, Nickerson DA: Sequence variation in the human angiotensin converting enzyme. Nat Genet. 1999 May;22(1):59-62. [PubMed Link Image]
  2. Halushka MK, Fan JB, Bentley K, Hsie L, Shen N, Weder A, Cooper R, Lipshutz R, Chakravarti A: Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis. Nat Genet. 1999 Jul;22(3):239-47. [PubMed Link Image]
  3. Tipnis SR, Hooper NM, Hyde R, Karran E, Christie G, Turner AJ: A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase. J Biol Chem. 2000 Oct 27;275(43):33238-43. [PubMed Link Image]
  4. Donoghue M, Hsieh F, Baronas E, Godbout K, Gosselin M, Stagliano N, Donovan M, Woolf B, Robison K, Jeyaseelan R, Breitbart RE, Acton S: A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9. Circ Res. 2000 Sep 1;87(5):E1-9. [PubMed Link Image]
  5. Harmer D, Gilbert M, Borman R, Clark KL: Quantitative mRNA expression profiling of ACE 2, a novel homologue of angiotensin converting enzyme. FEBS Lett. 2002 Dec 4;532(1-2):107-10. [PubMed Link Image]
  6. Ehlers MR, Riordan JF: Angiotensin-converting enzyme: zinc- and inhibitor-binding stoichiometries of the somatic and testis isozymes. Biochemistry. 1991 Jul 23;30(29):7118-26. [PubMed Link Image]
  7. Takeuchi K, Shimizu T, Ohishi N, Seyama Y, Takaku F, Yotsumoto H: Purification of human lung angiotensin-converting enzyme by high-performance liquid chromatography: properties and N-terminal amino acid sequence. J Biochem (Tokyo). 1989 Sep;106(3):442-5. [PubMed Link Image]
  8. Soubrier F, Alhenc-Gelas F, Hubert C, Allegrini J, John M, Tregear G, Corvol P: Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning. Proc Natl Acad Sci U S A. 1988 Dec;85(24):9386-90. [PubMed Link Image]
Target 2 Drug References
  1. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [PubMed Link Image]

This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.