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Showing drug card for Lisinopril (DB00722)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:07:38
Primary Accession Number DB00722
Secondary Accession Number
  • APRD00560
Name Lisinopril
Drug Type
  • Approved
  • Investigational
  • Small Molecule
Description One of the angiotensin-converting enzyme inhibitors (ACE inhibitors), orally active, that has been used in the treatment of hypertension and congestive heart failure. [PubChem]
Synonyms
  1. lisinopril
Brand Names
  1. Acercomp
  2. Inhibril
  3. Linopril
  4. Lisinopril Dihydrate
  5. Lisipril
  6. Lysinopril
  7. Noperten
  8. Presiten
  9. Prinivil
  10. Prinzide
  11. Renacor
  12. Sinopril
  13. Zestoretic
  14. Zestril
Brand Mixtures
  1. Prinzide (Hydrochlorothiazide + Lisinopril)
  2. Zestoretic Tab 10/12.5mg (Hydrochlorothiazide + Lisinopril)
  3. Zestoretic Tab 20/12.5mg (Hydrochlorothiazide + Lisinopril)
  4. Zestoretic Tab 20/25mg (Hydrochlorothiazide + Lisinopril)
Chemical IUPAC Name (2S)-1-[(2S)-6-amino-2-[[(2S)-1-hydroxy-1-oxo-4-phenylbutan-2-yl]amino]hexanoyl]pyrrolidine-2-carboxylic acid
Chemical Formula C21H31N3O5
Chemical Structure Structure
CAS Registry Number 83915-83-7
InChI Identifier InChI=1/C21H31N3O5/c22-13-5-4-9-16(19(25)24-14-6-10-18(24)21(28)29)23-17(20(26)27)12-11-15-7-2-1-3-8-15/h1-3,7-8,16-18,23H,4-6,9-14,22H2,(H,26,27)(H,28,29)/t16-,17-,18-/m0/s1/f/h26,28H
InChI Key RLAWWYSOJDYHDC-YMXGEOMKDH
KEGG Drug D00362 Link Image
KEGG Compound Not Available
PubChem Compound 5362119 Link Image
PubChem Substance 205105 Link Image
ChEBI ID Not Available
PharmGKB ID PA450242 Link Image
HET ID LPR Link Image
GenBank ID Not Available
Drug ID Number [DIN] 02217538 Link Image
RxList Link http://www.rxlist.com/cgi/generic/lisinop.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Lisinopril Link Image
FDA Label
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference Not Available
Average Molecular Weight 405.4879
Monoisotopic Molecular Weight 405.2264
State Solid
Melting Point Not Available
Experimental Water Solubility 13 mg/L Source: PhysProp
Predicted Water Solubility 2.16e-01 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity -0.9 Source: PhysProp
Predicted LogP -1.23 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -3.27 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 NCCCC[C@H](N[C@@H](CCC1=CC=CC=C1)C(O)=O)C(=O)N1CCC[C@H]1C(O)=O
Canonical SMILES NCCCCC(NC(CCC1=CC=CC=C1)C(O)=O)C(=O)N1CCCC1C(O)=O
Drug Category
  • Angiotensin-converting Enzyme Inhibitors
  • Antihypertensive Agents
  • Cardiotonic Agents
ATC Codes
AHFS Codes
  • 24:32.04
Indication For the treatment of hypertension, heart failure and acute myocardial infarction. It may be used alone or in combination with thiazide diuretics
Pharmacology Lisinopril, an angiotensin-converting enzyme (ACE) inhibitor, is used to treat hypertension, congestive heart failure (CHF), postmyocardial infarction, and diabetic nephropathy or retinopathy. Although it is the lysine ester of enalaprilat, the active form of the prodrug enalapril, lisinopril is active unchanged.
Mechanism of Action Lisinopril competes with angiotensin I for its binding site on the angiotensin-converting enzyme (ACE), an enzyme which converts angiotensin I to angiotensin II. As angiotensin II is a vasoconstrictor and a negative feedback mediator for renin activity, lower angiotensin II plasma levels result in decreased blood pressure and increased plasma renin activity. Baroreceptor reflex mechanisms, stimulated by the fall in blood pressure, release kininase II, an enzyme identical to ACE that degrades bradykinin, a vasodilator.
Absorption Approximately 25%, but widely variable between individuals (6 to 60%)
Toxicity hypotension, LD50= 2000 mg/kg(orally in rat)
Protein Binding Lisinopril does not appear to be bound to other serum proteins
Biotransformation Lisinopril does not undergo metabolism and is excreted unchanged entirely in the urine
Half Life 12 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
Clozapine Increases the effect and toxicity of clozapine
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 excess salt/sodium unless otherwise instructed by your physician.
  • Avoid natural licorice.
  • Avoid salt substitutes containing potassium.
  • Take without regard to meals.
Pathways
Name SMPDB Link KEGG Link
Lisinopril Pathway SMP00150 Link Image
General References
  1. Patchett AA, Harris E, Tristram EW, Wyvratt MJ, Wu MT, Taub D, Peterson ER, Ikeler TJ, ten Broeke J, Payne LG, Ondeyka DL, Thorsett ED, Greenlee WJ, Lohr NS, Hoffsommer RD, Joshua H, Ruyle WV, Rothrock JW, Aster SD, Maycock AL, Robinson FM, Hirschmann R, Sweet CS, Ulm EH, Gross DM, Vassil TC, Stone CA: A new class of angiotensin-converting enzyme inhibitors. Nature. 1980 Nov 20;288(5788):280-3. [PubMed Link Image]
  2. Drugs.com Link Image
  3. Wikipedia Link Image
  4. RxList Link Image
Organisms Affected
  • Humans and other mammals
Targets
  1. Angiotensin-converting enzyme, testis-specific isoform
  2. Angiotensin-converting enzyme, somatic isoform
  3. Angiotensinogen
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. Austad SG: [Lisinopril (Zestril)--a new ACE inhibitor] Tidsskr Nor Laegeforen. 1989 Jun 20;109(17-18):1921. [PubMed Link Image]
  2. Frontera Y, Piecuch JF: Multiple episodes of angioedema associated with lisinopril, an ACE inhibitor. J Am Dent Assoc. 1995 Feb;126(2):217-20. [PubMed Link Image]
  3. Hasslacher C: Influence of the ACE inhibitor lisinopril on blood pressure, metabolism, and renal function parameter in hypertensive type II diabetic patients: a postmarketing surveillance study. J Diabetes Complications. 1996 May-Jun;10(3):136-8. [PubMed Link Image]
  4. Abdelmalek MF, Douglas DD: Lisinopril-induced isolated visceral angioedema: review of ACE-inhibitor-induced small bowel angioedema. Dig Dis Sci. 1997 Apr;42(4):847-50. [PubMed Link Image]
  5. Tellez-Sanz R, Garcia-Fuentes L, Baron C: Calorimetric analysis of lisinopril binding to angiotensin I-converting enzyme. FEBS Lett. 1998 Feb 13;423(1):75-80. [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]
Drug Target 3 [top]
Target 3 ID 1694
Target 3 Name Angiotensinogen
Target 3 Synonyms
  1. Angiotensinogen precursor
  2. Serpin A8
Target 3 Gene Name AGT
Target 3 Protein Sequence >Angiotensinogen precursor 
MRKRAPQSEMAPAGVSLRATILCLLAWAGLAAGDRVYIHPFHLVIHNESTCEQLAKANAG
KPKDPTFIPAPIQAKTSPVDEKALQDQLVLVAAKLDTEDKLRAAMVGMLANFLGFRIYGM
HSELWGVVHGATVLSPTAVFGTLASLYLGALDHTADRLQAILGVPWKDKNCTSRLDAHKV
LSALQAVQGLLVAQGRADSQAQLLLSTVVGVFTAPGLHLKQPFVQGLALYTPVVLPRSLD
FTELDVAAEKIDRFMQAVTGWKTGCSLMGASVDSTLAFNTYVHFQGKMKGFSLLAEPQEF
WVDNSTSVSVPMLSGMGTFQHWSDIQDNFSVTQVPFTESACLLLIQPHYASDLDKVEGLT
FQQNSLNWMKKLSPRTIHLTMPQLVLQGSYDLQDLLAQAELPAILHTELNLQKLSNDRIR
VGEVLNSIFFELEADEREPTESTQQLNKPEVLEVTLNRPFLFAVYDQSATALHFLGRVAN
PLSTA
Target 3 Number of Residues 493
Target 3 Molecular Weight 53155
Target 3 Theoretical pI 6.27
Target 3 GO Classification
Function
enzyme regulator activity
enzyme inhibitor activity
protease inhibitor activity
endopeptidase inhibitor activity
serine-type endopeptidase inhibitor activity
Process
Not Available
Component
Not Available
Target 3 General Function Involved in serine-type endopeptidase inhibitor activity
Target 3 Specific Function Angiotensin-3 stimulates aldosterone release
Target 3 Pathways Not Available
Target 3 Reactions Not Available
Target 3 Pfam Domain Function
Target 3 Signals
  • 1-33
Target 3 Transmembrane Regions
  • None
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 178640 Link Image
Target 3 UniProtKB/Swiss-Prot ID P01019 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name ANGT_HUMAN Link Image
Target 3 PDB ID Not Available
Target 3 Cellular Location
  • Secreted protein
Target 3 Gene Sequence >1458 bp 
ATGCGGAAGCGAGCACCCCAGTCTGAGATGGCTCCTGCCGGTGTGAGCCTGAGGGCCACC
ATCCTCTGCCTCCTGGCCTGGGCTGGCCTGGCTGCAGGTGACCGGGTGTACATACACCCC
TTCCACCTCGTCATCCACAATGAGAGTACCTGTGAGCAGCTGGCAAAGGCCAATGCCGGG
AAGCCCAAAGACCCCACCTTCATACCTGCTCCAATTCAGGCCAAGACATCCCCTGTGGAT
GAAAAGGCCCTACAGGACCAGCTGGTGCTAGTCGCTGCAAAACTTGACACCGAAGACAAG
TTGAGGGCCGCAATGGTCGGGATGCTGGCCAACTTCTTGGGCTTCCGTATATATGGCATG
CACAGTGAGCTATGGGGCGTGGTCCATGGGGCCACCGTCCTCTCCCCAACGGCTGTCTTT
GGCACCCTGGCCTCTCTCTATCTGGGAGCCTTGGACCACACAGCTGACAGGCTACAGGCA
ATCCTGGGTGTTCCTTGGAAGGACAAGAACTGCACCTCCCGGCTGGATGCGCACAAGGTC
CTGTCTGCCCTGCAGGCTGTACAGGGCCTGCTAGTGGCCCAGGGCAGGGCTGATAGCCAG
GCCCAGCTGCTGCTGTCCACGGTGGTGGGCGTGTTCACAGCCCCAGGCCTGCACCTGAAG
CAGCCGTTTGTGCAGGGCCTGGCTCTCTATACCCCTGTGGTCCTCCCACGCTCTCTGGAC
TTCACAGAACTGGATGTTGCTGCTGAGAAGATTGACAGGTTCATGCAGGCTGTGACAGGA
TGGAAGACTGGCTGCTCCCTGATGGGAGCCAGTGTGGACAGCACCCTGGCTTTCAACACC
TACGTCCACTTCCAAGGGAAGATGAAGGGCTTCTCCCTGCTGGCCGAGCCCCAGGAGTTC
TGGGTGGACAACAGCACCTCAGTGTCTGTTCCCATGCTCTCTGGCATGGGCACCTTCCAG
CACTGGAGTGACATCCAGGACAACTTCTCGGTGACTCAAGTGCCCTTCACTGAGAGCGCC
TGCCTGCTGCTGATCCAGCCTCACTATGCCTCTGACCTGGACAAGGTGGAGGGTCTCACT
TTCCAGCAAAACTCCCTCAACTGGATGAAGAAACTGTCTCCCCGGACCATCCACCTGACC
ATGCCCCAACTGGTGCTGCAAGGATCTTATGACCTGCAGGACCTGCTCGCCCAGGCTGAG
CTGCCCGCCATTCTGCACACCGAGCTGAACCTGCAAAAATTGAGCAATGACCGCATCAGG
GTGGGGGAGGTGCTGAACAGCATTTTTTTTGAGCTTGAAGCGGATGAGAGAGAGCCCACA
GAGTCTACCCAACAGCTTAACAAGCCTGAGGTCTTGGAGGTGACCCTGAACCGCCCATTC
CTGTTTGCTGTGTATGATCAAAGCGCCACTGCCCTGCACTTCCTGGGCCGCGTGGCCAAC
CCGCTGAGCACAGCATGA
Target 3 GenBank Gene ID
Target 3 GeneCard ID AGT Link Image
Target 3 GenAtlas ID AGT Link Image
Target 3 HGNC ID HGNC:333 Link Image
Target 3 Chromosome Location 1
Target 3 Locus 1q42-q43
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Goodfriend TL, Peach MJ: Angiotensin III: (DES-Aspartic Acid-1)-Angiotensin II. Evidence and speculation for its role as an important agonist in the renin - angiotensin system. Circ Res. 1975 Jun;36(6 Suppl 1):38-48. [PubMed Link Image]
  2. Jeunemaitre X, Soubrier F, Kotelevtsev YV, Lifton RP, Williams CS, Charru A, Hunt SC, Hopkins PN, Williams RR, Lalouel JM, et al.: Molecular basis of human hypertension: role of angiotensinogen. Cell. 1992 Oct 2;71(1):169-80. [PubMed Link Image]
  3. Fukamizu A, Takahashi S, Seo MS, Tada M, Tanimoto K, Uehara S, Murakami K: Structure and expression of the human angiotensinogen gene. Identification of a unique and highly active promoter. J Biol Chem. 1990 May 5;265(13):7576-82. [PubMed Link Image]
  4. Kunapuli SP, Kumar A: Molecular cloning of human angiotensinogen cDNA and evidence for the presence of its mRNA in rat heart. Circ Res. 1987 May;60(5):786-90. [PubMed Link Image]
  5. Gaillard I, Clauser E, Corvol P: Structure of human angiotensinogen gene. DNA. 1989 Mar;8(2):87-99. [PubMed Link Image]
  6. Kunapuli SP, Benedict CR, Kumar A: Tissue specific hormonal regulation of the rat angiotensinogen gene expression. Arch Biochem Biophys. 1987 May 1;254(2):642-6. [PubMed Link Image]
  7. Campbell DJ, Bouhnik J, Coezy E, Menard J, Corvol P: Processing of rat and human angiotensinogen precursors by microsomal membranes. Mol Cell Endocrinol. 1985 Nov;43(1):31-40. [PubMed Link Image]
  8. Arakawa K, Minohara A, Yamada J, Nakamura M: Enzymatic degradation and electrophoresis of human angiotensin I. Biochim Biophys Acta. 1968 Sep 10;168(1):106-12. [PubMed Link Image]
  9. Kageyama R, Ohkubo H, Nakanishi S: Primary structure of human preangiotensinogen deduced from the cloned cDNA sequence. Biochemistry. 1984 Jul 31;23(16):3603-9. [PubMed Link Image]
  10. Tewksbury DA, Dart RA, Travis J: The amino terminal amino acid sequence of human angiotensinogen. Biochem Biophys Res Commun. 1981 Apr 30;99(4):1311-5. [PubMed Link Image]
  11. 7539791 Oxvig C, Haaning J, Kristensen L, Wagner JM, Rubin I, Stigbrand T, Gleich GJ, Sottrup-Jensen L: Identification of angiotensinogen and complement C3dg as novel proteins binding the proform of eosinophil major basic protein in human pregnancy serum and plasma. J Biol Chem. 1995 Jun 9;270(23):13645-51.
  12. 7607642 Hixson JE, Powers PK: Detection and characterization of new mutations in the human angiotensinogen gene (AGT). Hum Genet. 1995 Jul;96(1):110-2.
  13. 7744780 Inoue I, Rohrwasser A, Helin C, Jeunemaitre X, Crain P, Bohlender J, Lifton RP, Corvol P, Ward K, Lalouel JM: A mutation of angiotensinogen in a patient with preeclampsia leads to altered kinetics of the renin-angiotensin system. J Biol Chem. 1995 May 12;270(19):11430-6.
  14. 8513325 Ward K, Hata A, Jeunemaitre X, Helin C, Nelson L, Namikawa C, Farrington PF, Ogasawara M, Suzumori K, Tomoda S, et al.: A molecular variant of angiotensinogen associated with preeclampsia. Nat Genet. 1993 May;4(1):59-61.
  15. 8621667 Gimenez-Roqueplo AP, Leconte I, Cohen P, Simon D, Guyene TT, Celerier J, Pau B, Corvol P, Clauser E, Jeunemaitre X: The natural mutation Y248C of human angiotensinogen leads to abnormal glycosylation and altered immunological recognition of the protein. J Biol Chem. 1996 Apr 19;271(16):9838-44.
  16. 9492317 Carpenter KA, Wilkes BC, Schiller PW: The octapeptide angiotensin II adopts a well-defined structure in a phospholipid environment. Eur J Biochem. 1998 Jan 15;251(1-2):448-53.
Target 3 Drug References
  1. Bernier NJ, Kaiya H, Takei Y, Perry SF: Mediation of humoral catecholamine secretion by the renin-angiotensin system in hypotensive rainbow trout (Oncorhynchus mykiss). J Endocrinol. 1999 Mar;160(3):351-63. [PubMed Link Image]
  2. Wang R, Zagariya A, Ibarra-Sunga O, Gidea C, Ang E, Deshmukh S, Chaudhary G, Baraboutis J, Filippatos G, Uhal BD: Angiotensin II induces apoptosis in human and rat alveolar epithelial cells. Am J Physiol. 1999 May;276(5 Pt 1):L885-9. [PubMed Link Image]
  3. Takai S, Jin D, Sakaguchi M, Miyazaki M: Chymase-dependent angiotensin II formation in human vascular tissue. Circulation. 1999 Aug 10;100(6):654-8. [PubMed Link Image]
  4. Bernier NJ, Gilmour KM, Takei Y, Perry SF: Cardiovascular control via angiotensin II and circulating catecholamines in the spiny dogfish, Squalus acanthias. J Comp Physiol [B]. 1999 Jul;169(4-5):237-48. [PubMed Link Image]
  5. Takai S, Sakaguchi M, Jin D, Yamada M, Kirimura K, Miyazaki M: Different angiotensin II-forming pathways in human and rat vascular tissues. Clin Chim Acta. 2001 Mar;305(1-2):191-5. [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.