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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:07:57
Primary Accession Number DB00881
Secondary Accession Number
  • APRD00523
Name Quinapril
Drug Type
  • Approved
  • Investigational
  • Small Molecule
Description Quinapril is used in the treatment of hypertension and congestive heart failure. Quinapril is actually a prodrug. It is converted to its active metabolite, quinaprilat, in the liver. Quinapril inhibits angiotensin converting enzyme, an enzyme which catalyses the formation of angiotensin II from its precursor, angiotensin I. Angiotensin II is a powerful vasoconstrictor and increases blood pressure through a variety of mechanisms.
Synonyms
  1. Quinapril Hcl
  2. Quinapril Hydrochloride
  3. Quinaprilum [Latin]
Brand Names
  1. Accupril
  2. Accuprin
  3. Accupro
  4. Acequin
  5. Acuitel
  6. Korec
  7. Quinazil
Brand Mixtures Not Available
Chemical IUPAC Name (3S)-2-[(2S)-2-[[(2S)-1-ethoxy-1-oxo-4-phenylbutan-2-yl]amino]propanoyl]-3,4-dihydro-1H-isoquinoline-3-carboxylic acid
Chemical Formula C25H30N2O5
Chemical Structure Structure
CAS Registry Number 85441-61-8
InChI Identifier InChI=1/C25H30N2O5/c1-3-32-25(31)21(14-13-18-9-5-4-6-10-18)26-17(2)23(28)27-16-20-12-8-7-11-19(20)15-22(27)24(29)30/h4-12,17,21-22,26H,3,13-16H2,1-2H3,(H,29,30)/t17-,21-,22-/m0/s1/f/h29H
InChI Key JSDRRTOADPPCHY-YHZYPMOJDP
KEGG Drug D03752 Link Image
KEGG Compound C07398 Link Image
PubChem Compound 54892 Link Image
PubChem Substance 9602 Link Image
ChEBI ID 8713 Link Image
PharmGKB ID PA451205 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 01947672 Link Image
RxList Link http://www.rxlist.com/cgi/generic/quinap.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Quinapril Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference M. L. Hoefle, S. Klutchko, U.S. Pat. 4,344,949 (1982)
Average Molecular Weight 438.5161
Monoisotopic Molecular Weight 438.2155
State Solid
Melting Point 120-130oC
Experimental Water Solubility 1 mg/L Source: PhysProp
Predicted Water Solubility 8.50e-03 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 3.2 Source: PhysProp
Predicted LogP 1.40 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -4.71 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)N1CC2=CC=CC=C2C[C@H]1C(O)=O
Canonical SMILES CCOC(=O)C(CCC1=CC=CC=C1)NC(C)C(=O)N1CC2=CC=CC=C2CC1C(O)=O
Drug Category
  • Angiotensin-converting Enzyme Inhibitors
  • Antihypertensive Agents
ATC Codes
AHFS Codes
  • 24:32.04
Indication For the treatment of hypertension and chronic heart failure.
Pharmacology Quinapril, an angiotensin-converting enzyme (ACE) inhibitor, is used to treat hypertension and heart failure. Like ramipril, quinapril is a prodrug that, upon deesterification, is converted to the active metabolite quinaprilat. The effect of quinapril in hypertension and in congestive heart failure (CHF) appears to result primarily from the inhibition of circulating and tissue ACE activity, thereby reducing angiotensin II formation.
Mechanism of Action Quinaprilat 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 stimulation of baroreceptor reflex mechanisms. Quinaprilat may also act on kininase II, an enzyme identical to ACE that degrades the vasodilator bradykinin.
Absorption Following oral administration, peak plasma quinapril concentrations are observed within one hour. Based on recovery of quinapril and its metabolites in urine, the extent of absorption is at least 60%. The rate and extent of quinapril absorption are diminished moderately (approximately 25-30%) when ACCUPRIL tablets are administered during a high-fat meal.
Toxicity Overdose may lead to severe hypotension. LD50=1739mg/kg (orally in mice).
Protein Binding 97%
Biotransformation Hepatic.
Half Life 2 hours
Dosage Forms
Form Route
Tablet 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
Tetracycline Quinapril can reduce the absorption of tetracycline
Tizanidine Tizanidine increases the risk of hypotension with the ACE inhibitor
Triamterene Increased risk of hyperkaliemia
Food Interactions
  • Do not take with a high-fat meal.
  • Magnesium, potassium and zinc needs increased.
Pathways
Name SMPDB Link KEGG Link
Quinapril Pathway SMP00153 Link Image
General References
  1. Drugs.com Link Image
  2. Wikipedia Link Image
  3. RxList Link Image
Organisms Affected
  • Humans and other mammals
Phase 1 Metabolizing Enzymes
  1. Cytochrome P450 3A4 (CYP3A4)
Targets
  1. Angiotensin-converting enzyme, testis-specific isoform
  2. Angiotensin-converting enzyme, somatic isoform
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Cytochrome P450 3A4 (CYP3A4)
Enzyme 1 Gene Name CYP3A4
Enzyme 1 SwissProt ID P08684 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >sp|P08684|CP3A4_HUMAN Cytochrome P450 3A4 (EC 1.14.13.67) 
ALIPDLAMETWLLLAVSLVLLYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFD
MECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISIA
EDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYSM
DVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVF
PREVTNFLRKSVKRMKESRLEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSII
FIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVLQMEYLDMVVN
ETLRLFPIAMRLERVCKKDVEINGMFIPKGWVVMIPSYALHRDPKYWTEPEKFLPERFSK
KNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGG
LLQPEKPVVLKVESRDGTVSGA
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. Pitt B, O'Neill B, Feldman R, Ferrari R, Schwartz L, Mudra H, Bass T, Pepine C, Texter M, Haber H, Uprichard A, Cashin-Hemphill L, Lees RS: The QUinapril Ischemic Event Trial (QUIET): evaluation of chronic ACE inhibitor therapy in patients with ischemic heart disease and preserved left ventricular function. Am J Cardiol. 2001 May 1;87(9):1058-63. [PubMed Link Image]
  2. Khan BV, Sola S, Lauten WB, Natarajan R, Hooper WC, Menon RG, Lerakis S, Helmy T: Quinapril, an ACE inhibitor, reduces markers of oxidative stress in the metabolic syndrome. Diabetes Care. 2004 Jul;27(7):1712-5. [PubMed Link Image]
  3. Voors AA, van Geel PP, Oosterga M, Buikema H, van Veldhuisen DJ, van Gilst WH: Vascular effects of quinapril completely depend on ACE insertion/deletion polymorphism. J Renin Angiotensin Aldosterone Syst. 2004 Sep;5(3):130-4. [PubMed Link Image]
  4. Skvortsov AA, Nasonova SN, Sychev AV, Arbolishvili GN, Baklanova NA, Mareev VIu, Belenkov IuN: [Combined therapy with quinapril, an ACE inhibitor, and valsartan, a type 1 angiotensin II receptors blocker, for moderate chronic cardiac failure may raise the degree of neurohormonal block and improve 24-h heart rate variability compared to the effect of monotherapy (data from the trial SADKO-CHF)] Ter Arkh. 2005;77(8):34-43. [PubMed Link Image]
  5. Valles Prats M, Matas Serra M, Bronsoms Artero J, Mate Benito G, Torguet Escuder P, Mauri Nicolas JM: Quinapril ACE-inhibition effects on adrenergic parameters in moderate essential hypertension. Kidney Int Suppl. 1996 Jun;55:S104-6. [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.