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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:06:46
Primary Accession Number DB00492
Secondary Accession Number
  • APRD00526
Name Fosinopril
Drug Type
  • Approved
  • Small Molecule
Description A phosphinic acid-containing angiotensin-converting enzyme inhibitor that is effective in the treatment of hypertension. It is a prodrug that is converted to its active metabolite fosinoprilat. [PubChem]
Synonyms
  1. Fosinopril Sodium
Brand Names
  1. Acecor
  2. Monopril
  3. Secorvas
  4. Staril
Brand Mixtures Not Available
Chemical IUPAC Name (2S,4S)-4-cyclohexyl-1-[2-[(2-methyl-1-propanoyloxypropoxy)-(4-phenylbutyl)phosphoryl]acetyl]pyrrolidine-2-carboxylic acid
Chemical Formula C30H46NO7P
Chemical Structure Structure
CAS Registry Number 98048-97-6
InChI Identifier InChI=1/C30H46NO7P/c1-4-28(33)37-30(22(2)3)38-39(36,18-12-11-15-23-13-7-5-8-14-23)21-27(32)31-20-25(19-26(31)29(34)35)24-16-9-6-10-17-24/h5,7-8,13-14,22,24-26,30H,4,6,9-12,15-21H2,1-3H3,(H,34,35)/t25-,26+,30?,39?/m1/s1/f/h34H
InChI Key BIDNLKIUORFRQP-AIINYXMPDF
KEGG Drug D00622 Link Image
KEGG Compound C07016 Link Image
PubChem Compound 55891 Link Image
PubChem Substance 194429 Link Image
ChEBI ID Not Available
PharmGKB ID PA449710 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 02262428 Link Image
RxList Link http://www.rxlist.com/cgi/generic/fosinop.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Fosinopril Link Image
FDA Label
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference E. W. Petrillo, Jr., U.S. Pat. 4,337,201 (1982)
Average Molecular Weight 563.6625
Monoisotopic Molecular Weight 563.3012
State Solid
Melting Point 149-153 oC
Experimental Water Solubility Insoluble Source: PhysProp
Predicted Water Solubility 1.01e-03 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 6.3 Source: PhysProp
Predicted LogP 4.71 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -5.75 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 CCC(=O)O[C@@H](O[P@@](=O)(CCCCC1=CC=CC=C1)CC(=O)N1C[C@@H](C[C@H]1C(O)=O)C1CCCCC1)C(C)C
Canonical SMILES CCC(=O)OC(OP(=O)(CCCCC1=CC=CC=C1)CC(=O)N1CC(CC1C(O)=O)C1CCCCC1)C(C)C
Drug Category
  • Angiotensin-converting Enzyme Inhibitors
  • Antihypertensive Agents
ATC Codes
AHFS Codes
  • 24:32.04
Indication For the treatment of hypertension. It may be used alone or in combination with thiazide diuretics. It is also indicated in the management of heart failure.
Pharmacology Fosinopril is an angiotensin-converting enzyme (ACE) inhibitor. ACE is a peptidyl dipeptidase that catalyzes the conversion of angiotensin I to the vasoconstrictor substance, angiotensin II. By blocking ACE, Fosinopril decreases angiotensin II which is a vasoconstrictor. Fosinopril 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. Angiotensin II also stimulates aldosterone secretion by the adrenal cortex.
Mechanism of Action Fosinoprilat, the active metabolite of fosinopril, competes with angiotensin I for binding at the angiotensin-converting enzyme, blocking the conversion of angiotensin I to angiotensin II. Inhibition of ACE results in decreased plasma 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 stimulation of baroreceptor reflex mechanisms, which leads to decreased vasopressor activity and to decreased aldosterone secretion. Fosinoprilat may also act on kininase II, an enzyme identical to ACE that degrades the vasodilator bradykinin.
Absorption Bioavailability is approximately 36% following oral administration.
Toxicity Human overdoses of fosinopril have not been reported, but the most common manifestation of human fosinopril overdosage is likely to be hypotension. Oral doses of fosinopril at 2600 mg/kg in rats were associated with significant lethality.
Protein Binding 87%
Biotransformation Since fosinoprilat is not biotransformed after intravenous administration, fosinopril, not fosinoprilat, appears to be the precursor for the glucuronide and p-hydroxy metabolites.
Half Life 12 hours
Dosage Forms
Form Route
Tablet Oral
Tablet Oral
Patient Information Not Available
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
  • Avoid alcohol.
  • Avoid natural licorice.
  • Avoid salt substitutes containing potassium.
  • Do not take calcium, aluminum, magnesium or Iron supplements within 2 hours of taking this medication.
  • Take without regard to meals.
Pathways
Name SMPDB Link KEGG Link
Fosinopril Pathway SMP00149 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. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
  3. Kowala MC, Grove RI, Aberg G: Inhibitors of angiotensin converting enzyme decrease early atherosclerosis in hyperlipidemic hamsters. Fosinopril reduces plasma cholesterol and captopril inhibits macrophage-foam cell accumulation independently of blood pressure and plasma lipids. Atherosclerosis. 1994 Jul;108(1):61-72. [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. Sharma S, Deitchman D, Eni JS, Gelperin K, Ilgenfritz JP, Blumenthal M: The hemodynamic effects of long-term ACE inhibition with fosinopril in patients with heart failure. Fosinopril Hemodynamics Study Group. Am J Ther. 1999 Jul;6(4):181-9. [PubMed Link Image]
  2. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [PubMed Link Image]
  3. David D, Jallad N, Germino FW, Willett MS, de Silva J, Weidner SM, Mills DJ: A Comparison of the Cough Profile of Fosinopril and Enalapril in Hypertensive Patients with a History of ACE Inhibitor-Associated Cough. Am J Ther. 1995 Oct;2(10):806-813. [PubMed Link Image]
  4. Vershinina AM, Gapon LI, Veber EE, Popova SN, Pliusnin AV: [Effects of ACE inhibitor fosinopril on a 24-h profile of arterial pressure in hypertensive patients with obesity and hypercholesterolemia] Ter Arkh. 2005;77(4):55-8. [PubMed Link Image]
  5. : [Microalbuminuria--an independent indication for administration of ACE inhibitors: role of fosinopril (PREVEND IT trial)] Ter Arkh. 2005;77(9):84-8. [PubMed Link Image]
  6. : Fosinopril (Staril)--another ACE inhibitor. Drug Ther Bull. 1991 Jun 10;29(12):48. [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.