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Showing drug card for Isoniazid (DB00951)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-02-19 16:04:57
Primary Accession Number DB00951
Secondary Accession Number
  • APRD01055
  • EXPT01940
Name Isoniazid
Drug Type
  • Approved
  • Small Molecule
Description Antibacterial agent used primarily as a tuberculostatic. It remains the treatment of choice for tuberculosis. [PubChem]
Synonyms
  1. HIA
  2. Hydrazid
  3. Hydrazide
  4. INH
  5. Isohydrazide
  6. Isonicotinhydrazid
  7. Isonicotinic acid hydrazide
  8. Isonicotinic hydrazide
  9. Isonicotinohydrazide
  10. Isonicotinoyl hydrazide
  11. Isonicotinyl hydrazide
  12. Isonicotinyl hydrazine
  13. Isonicotinylhydrazine
Brand Names
  1. Andrazide
  2. Antimicina
  3. Antituberkulosum
  4. Armacide
  5. Armazid
  6. Armazide
  7. Atcotibine
  8. Azuren
  9. Bacillin
  10. Cedin
  11. Cemidon
  12. Chemiazid
  13. Chemidon
  14. Cortinazine
  15. Cotinazin
  16. Cotinizin
  17. Defonin
  18. Dibutin
  19. Diforin
  20. Dinacrin
  21. Ditubin
  22. Ebidene
  23. Eralon
  24. Ertuban
  25. Eutizon
  26. Evalon
  27. FSR 3
  28. Fimalene
  29. GINK
  30. Hidranizil
  31. Hidrasonil
  32. Hidrulta
  33. Hidrun
  34. Hycozid
  35. Hyozid
  36. Hyzyd
  37. Ido-tebin
  38. Idrazil
  39. Inah
  40. Inizid
  41. Iscotin
  42. Isidrina
  43. Ismazide
  44. Isobicina
  45. Isocid
  46. Isocidene
  47. Isocotin
  48. Isolyn
  49. Isonerit
  50. Isonex
  51. Isoniacid
  52. Isoniazid SA
  53. Isoniazide
  54. Isonicazide
  55. Isonicid
  56. Isonico
  57. Isonicotan
  58. Isonicotil
  59. Isonide
  60. Isonidrin
  61. Isonikazid
  62. Isonilex
  63. Isonin
  64. Isonindon
  65. Isonirit
  66. Isoniton
  67. Isonizide
  68. Isopyrin
  69. Isotamine
  70. Isotebe
  71. Isotebezid
  72. Isotinyl
  73. Isozide
  74. Isozyd
  75. Laniazid
  76. Laniozid
  77. Mybasan
  78. Neo-Tizide
  79. Neoteben
  80. Neoxin
  81. Neumandin
  82. Nevin
  83. Niadrin
  84. Nicazide
  85. Nicetal
  86. Nicizina
  87. Niconyl
  88. Nicotibina
  89. Nicotibine
  90. Nicotisan
  91. Nicozide
  92. Nidaton
  93. Nidrazid
  94. Nikozid
  95. Niplen
  96. Nitadon
  97. Nydrazid
  98. Nyscozid
  99. Pelazid
  100. Percin
  101. Phthisen
  102. Pycazide
  103. Pyreazid
  104. Pyricidin
  105. Pyridicin
  106. Pyrizidin
  107. Raumanon
  108. Razide
  109. Retozide
  110. Rifamate
  111. Rimicid
  112. Rimifon
  113. Rimiphone
  114. Rimitsid
  115. Robiselin
  116. Robisellin
  117. Roxifen
  118. Sanohidrazina
  119. Sauterazid
  120. Sauterzid
  121. Stanozide
  122. TB-Phlogin
  123. TB-Razide
  124. TB-Vis
  125. Tebecid
  126. Tebenic
  127. Tebexin
  128. Tebilon
  129. Tebos
  130. Teebaconin
  131. Tekazin
  132. Tibazide
  133. Tibemid
  134. Tibison
  135. Tibivis
  136. Tibusan
  137. Tubazid
  138. Tubazide
  139. Tubeco
  140. Tubecotubercid
  141. Tuberian
  142. Tubicon
  143. Tubilysin
  144. Tubomel
  145. Tyvid
  146. Unicocyde
  147. Unicozyde
  148. Vazadrine
  149. Vederon
  150. Zidafimia
  151. Zinadon
  152. Zonazide
Brand Mixtures
  1. Isotamine B 300 (Isoniazid + Pyridoxine Hydrochloride)
  2. Rifater (Isoniazid + Pyrazinamide + Rifampin)
Chemical IUPAC Name pyridine-4-carbohydrazide
Chemical Formula C6H7N3O
Chemical Structure Structure
CAS Registry Number 54-85-3
InChI Identifier InChI=1/C6H7N3O/c7-9-6(10)5-1-3-8-4-2-5/h1-4H,7H2,(H,9,10)/f/h9H
InChI Key QRXWMOHMRWLFEY-BGGKNDAXCZ
KEGG Drug D00346 Link Image
KEGG Compound C07054 Link Image
PubChem Compound 3767 Link Image
PubChem Substance 9266 Link Image
ChEBI ID 6030 Link Image
PharmGKB ID PA450112 Link Image
HET ID ISZ Link Image
GenBank ID Not Available
Drug ID Number [DIN] 00577782 Link Image
RxList Link http://www.rxlist.com/cgi/generic2/isoniaz.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Isoniazid Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 137.1393
Monoisotopic Molecular Weight 137.0589
State Solid
Melting Point 171.4 oC
Experimental Water Solubility 140 mg/mL Source: PhysProp
Predicted Water Solubility 3.49e+01 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity -0.8 Source: PhysProp
Predicted LogP -0.71 Calculated using ALOGPS
Experimental LogS 0.01 [ADME Research, USCD]
Predicted LogS -0.59 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point 1.82
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 Not Available
Isomeric SMILES NNC(=O)C1=CC=NC=C1
Canonical SMILES NNC(=O)C1=CC=NC=C1
Drug Category
  • Antitubercular Agents
  • Fatty Acid Synthesis Inhibitors
ATC Codes
AHFS Codes
  • 08:16.04
Indication For the treatment of all forms of tuberculosis in which organisms are susceptible.
Pharmacology Isoniazid is a bactericidal agent active against organisms of the genus Mycobacterium, specifically M. tuberculosis, M. bovis and M. kansasii. It is a highly specific agent, ineffective against other microorganisms. Isoniazid is bactericidal to rapidly-dividing mycobacteria, but is bacteriostatic if the mycobacterium is slow-growing.
Mechanism of Action Isoniazid is a prodrug and must be activated by bacterial catalase. Specficially, activation is associated with reduction of the mycobacterial ferric KatG catalase-peroxidase by hydrazine and reaction with oxygen to form an oxyferrous enzyme complex. Once activated, isoniazid inhibits the synthesis of mycoloic acids, an essential component of the bacterial cell wall. At therapeutic levels isoniazid is bacteriocidal against actively growing intracellular and extracellular Mycobacterium tuberculosis organisms. Specifically isoniazid inhibits InhA, the enoyl reductase from Mycobacterium tuberculosis, by forming a covalent adduct with the NAD cofactor. It is the INH-NAD adduct that acts as a slow, tight-binding competitive inhibitor of InhA.
Absorption Readily absorbed following oral administration; however, may undergo significant first pass metabolism. Absorption and bioavailability are reduced when isoniazid is administered with food.
Toxicity LD50 100 mg/kg (Human, oral). Adverse reactions include rash, abnormal liver function tests, hepatitis, peripheral neuropathy, mild central nervous system (CNS) effects. In vivo, Isoniazid reacts with pyridoxal to form a hydrazone, and thus inhibits generation of pyridoxal phosphate. Isoniazid also combines with pyridoxal phosphate; high doses interfere with the coenzyme function of the latter.
Protein Binding Very low (0-10%)
Biotransformation Primarily hepatic. Isoniazid is acetylated by N -acetyl transferase to N -acetylisoniazid; it is then biotransformed to isonicotinic acid and monoacetylhydrazine. Monoacetylhydrazine is associated with hepatotoxicity via formation of a reactive intermediate metabolite when N-hydroxylated by the cytochrome P450 mixed oxidase system. The rate of acetylation is genetically determined. Slow acetylators are characterized by a relative lack of hepatic N -acetyltransferase.
Half Life Fast acetylators: 0.5 to 1.6 hours. Slow acetylators: 2 to 5 hours.
Dosage Forms
Form Route
Powder Oral
Syrup Oral
Tablet Oral
Patient Information Not Available
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Acenocoumarol The agent increases the effect of anticoagulant
Acetaminophen Risk of hepatotoxicity
Aminophylline Increases the effect and toxicity of theophylline
Anisindione The agent increases the effect of anticoagulant
Carbamazepine Carbamazepine effect is increased as is isoniazid toxicity
Dicumarol The agent increases the effect of anticoagulant
Disulfiram Increased risk of CNS adverse effects
Dyphylline Increases the effect and toxicity of theophylline
Ethotoin Isoniazid increases the effect of phenytoin in 20% of patients
Fosphenytoin Isoniazid increases the effect of phenytoin in 20% of patients
Ketoconazole Isoniazid decreases the effect of ketoconazole
Meperidine Possible episodes of hypotension
Mephenytoin Isoniazid increases the effect of phenytoin in 20% of patients
Oxtriphylline Increases the effect and toxicity of theophylline
Phenytoin Isoniazid increases the effect of phenytoin in 20% of patients
Theophylline Increases the effect and toxicity of theophylline
Warfarin The agent increases the effect of anticoagulant
Food Interactions
  • Avoid aged foods (cheese, red wine), pickled foods, cured foods (bacon/ham), chocolate, fava beans, beer, unless approved by your physician.
  • Avoid alcohol.
  • Do not take calcium, aluminum, magnesium or Iron supplements within 2 hours of taking this medication.
  • Increase dietary intake of magnesium, folate, vitamin B6, B12, and/or consider taking a multivitamin.
  • Take on empty stomach: 1 hour before or 2 hours after meals.
  • Take with a full glass of water.
Pathways Not Available
General References
  1. Drugs.com Link Image
  2. Wikipedia Link Image
  3. RxList Link Image
Organisms Affected
  • Mycobacteria
Phase 1 Metabolizing Enzymes
  1. Cytochrome P450 2E1 (CYP2E1)
Targets
  1. 4-aminobutyrate aminotransferase, mitochondrial
  2. Enoyl-[acyl-carrier-protein] reductase [NADH]
  3. Peroxidase/catalase T
  4. Arylamine N-acetyltransferase
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Cytochrome P450 2E1 (CYP2E1)
Enzyme 1 Gene Name CYP2E1
Enzyme 1 SwissProt ID P05181 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >sp|P05181|CP2E1_HUMAN Cytochrome P450 2E1 (EC 1.14.14.1) 
MSALGVTVALLVWAAFLLLVSMWRQVHSSWNLPPGPFPLPIIGNLFQLELKNIPKSFTRL
AQRFGPVFTLYVGSQRMVVMHGYKAVKEALLDYKDEFSGRGDLPAFHAHRDRGIIFNNGP
TWKDIRRFSLTTLRNYGMGKQGNESRIQREAHFLLEALRKTQGQPFDPTFLIGCAPCNVI
ADILFRKHFDYNDEKFLRLMYLFNENFHLLSTPWLQLYNNFPSFLHYLPGSHRKVIKNVA
EVKEYVSERVKEHHQSLDPNCPRDLTDCLLVEMEKEKHSAERLYTMDGITVTVADLFFAG
TETTSTTLRYGLLILMKYPEIEEKLHEEIDRVIGPSRIPAIKDRQEMPYMDAVVHEIQRF
ITLVPSNLPHEATRDTIFRGYLIPKGTVVVPTLDSVLYDNQEFPDPEKFKPEHFLNENGK
FKYSDYFKPFSTGKRVCAGEGLARMELFLLLCAILQHFNLKPLVDPKDIDLSPIHIGFGC
IPPRYKLCVIPRS
Drug Target 1 [top]
Target 1 ID 280
Target 1 Name 4-aminobutyrate aminotransferase, mitochondrial
Target 1 Synonyms
  1. (S)-3-amino-2-methylpropionate transaminase
  2. 4-aminobutyrate aminotransferase, mitochondrial precursor
  3. EC 2.6.1.19
  4. EC 2.6.1.22
  5. GABA aminotransferase
  6. GABA transaminase
  7. GABA-AT
  8. GABA-T
  9. Gamma-amino-N-butyrate transaminase
  10. L-AIBAT
Target 1 Gene Name ABAT
Target 1 Protein Sequence >4-aminobutyrate aminotransferase, mitochondrial precursor 
MASMLLAQRLACSFQHSYRLLVPGSRHISQAAAKVDVEFDYDGPLMKTEVPGPRSQELMK
QLNIIQNAEAVHFFCNYEESRGNYLVDVDGNRMLDLYSQISSVPIGYSHPALLKLIQQPQ
NASMFVNRPALGILPPENFVEKLRQSLLSVAPKGMSQLITMACGSCSNENALKTIFMWYR
SKERGQRGFSQEELETCMINQAPGCPDYSILSFMGAFHGRTMGCLATTHSKAIHKIDIPS
FDWPIAPFPRLKYPLEEFVKENQQEEARCLEEVEDLIVKYRKKKKTVAGIIVEPIQSEGG
DNHASDDFFRKLRDIARKHGCAFLVDEVQTGGGCTGKFWAHEHWGLDDPADVMTFSKKMM
TGGFFHKEEFRPNAPYRIFNTWLGDPSKNLLLAEVINIIKREDLLNNAAHAGKALLTGLL
DLQARYPQFISRVRGRGTFCSFDTPDDSIRNKLILIARNKGVVLGGCGDKSIRFRPTLVF
RDHHAHLFLNIFSDILADFK
Target 1 Number of Residues 508
Target 1 Molecular Weight 56440
Target 1 Theoretical pI 8.04
Target 1 GO Classification
Function
4-aminobutyrate transaminase activity
binding
vitamin binding
pyridoxal phosphate binding
catalytic activity
transferase activity
transferase activity, transferring nitrogenous groups
transaminase activity
Process
physiological process
metabolism
cellular metabolism
amino acid and derivative metabolism
amino acid derivative metabolism
gamma-aminobutyric acid metabolism
Component
Not Available
Target 1 General Function Amino acid transport and metabolism
Target 1 Specific Function Catalyzes the conversion of gamma-aminobutyrate and L- beta-aminoisobutyrate to succinate semialdehyde and methylmalonate semialdehyde, respectively. Can also convert delta-aminovalerate and beta-alanine
Target 1 Pathways
Name SMPDB Link KEGG Link
Valine, leucine and isoleucine degradation SMP00032 Link Image map00280 Link Image
Target 1 Reactions
  • 4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 602705 Link Image
Target 1 UniProtKB/Swiss-Prot ID P80404 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name GABT_HUMAN Link Image
Target 1 PDB ID 1OHY Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location
  • Mitochondrion
  • mitochondrial matrix
Target 1 Gene Sequence >1503 bp 
ATGGCCTCCATGTTGCTCGCCCAGCGGCTGGCCTGCAGCTTCCAGCACACGTACCGCCTG
CTGGTGCCTGGATCCAGACACATTAGTCAAGCTGCAGCCAAAGTCGACGTTGAATTTGAT
TATGATGGGCCTCTGATGAAGACGGAAGTCCCAGGGCCTAGATCTCAGGAGTTAATGAAA
CAGCTGAATATAATTCAGAATGCAGAGGCTGTGCATTTTTTCTGCAATTACGAAGAGAGC
CGAGGCAATTACCTGGTTGATGTGGACGGCAACCGAATGCTGGATCTTTATTCCCAGATC
TCCTCTGTTCCCATAGGTTACAGCGACCCGGCCCTCGTGAAACTCATCCAACAGCCACAA
AATGCGAGCATGTTTGTCAACAGACCCGCCCTCGAAATCCTGCCTCCGGAGAACTTTGTG
GAGAAGCTCCGGCAGTCCTTGCTCTCGGTGGCTCCCAAAGGGATGTCCCAGCTCATCACC
ATGGCCTGCGGCTCCTGCTCCAATGAAAACGCCTTAAAGACCATCTTCATGTGGTACCGG
AGCAAGGAAAGAGGGCAGAGGGGATTCTCCAAAGAGGAGCTGGAGACGTGCATGATTAAC
CAGGCCCCCTGGTGCCCCGACTACAGCATCCTCTCCTTCATGGGTTCCTTCCATGGGAGG
ACCATGGGTTGCTTAGCGACCACGCACTCTAAAGCCATTCACAAGATCGATATCCCTTCC
TTTGACTGGCCCATCGCACCGTTCCCACGGCTGAAATACCCTCTGGAAGAGTTTGTGAAA
GAGAACCAACAGGAAGAGGCCGGCTGTCTGGAAGAGGTTGAGGATCTGATTGTGAAATAT
CGAAAAAAGAAGAAGACGGTGGCCGGGATCATCGTGGAGCCCATCCAGTCCGAGGGTGGA
GACAACCATGCATCCGATGACTTCTTTCGGAAGCTGAGAGACATCGCCAGGAAGCACTGC
TGCGCCTTCTTGGTGGACGAGGTCCAGACCGGAGGAGGCTGCACGGGCAAGTTCTGGGCC
CATGAGCACTGGGGCCTGGATGACCCAGCAGACGTGATGACCTTCAGCAAGAAGATGATG
ACTGGGGGCTTCTTCCTCAAGGAGGAGTTCAGGCCTAATGCTCCCTACCGGATCTTCAAC
ACGTGGCTGGGGGACCCGTCCAAGAACCTGTTGCTGGCTGAGGTCATCAACATCATCAAG
CGGGAGGACCTGCTAAATAATGCAGCCCATGCCGGGAAGGCCCTGCTCACAGGACTGCTG
GACCTCCAGGCCCGGTACCCCCAGTTCATCAGCAGGGTGAGAGGACGAGGCACCTTTTGC
TCCTTCGATACTCCCGATGATTCCATACGGAATAAGCTCATTTTAATTGCCAGAAACAAA
GGTGTGGTGTTGGGTGGCTGTGGTGACAAATCCATTCGTTTCCGTCCCACGCTGGTGTTC
AGGGATCACCACGCTCACCTGTTCCTCAATATTTTCAGTGACATCTTAGCAGACTTCAAG
TAA
Target 1 GenBank Gene ID
Target 1 GeneCard ID ABAT Link Image
Target 1 GenAtlas ID ABAT Link Image
Target 1 HGNC ID HGNC:23 Link Image
Target 1 Chromosome Location 16
Target 1 Locus 16p13.2
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Medina-Kauwe LK, Tobin AJ, De Meirleir L, Jaeken J, Jakobs C, Nyhan WL, Gibson KM: 4-Aminobutyrate aminotransferase (GABA-transaminase) deficiency. J Inherit Metab Dis. 1999 Jun;22(4):414-27. [PubMed Link Image]
  2. Osei YD, Churchich JE: Screening and sequence determination of a cDNA encoding the human brain 4-aminobutyrate aminotransferase. Gene. 1995 Apr 3;155(2):185-7. [PubMed Link Image]
  3. De Biase D, Barra D, Simmaco M, John RA, Bossa F: Primary structure and tissue distribution of human 4-aminobutyrate aminotransferase. Eur J Biochem. 1995 Jan 15;227(1-2):476-80. [PubMed Link Image]
Target 1 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 2 [top]
Target 2 ID 368
Target 2 Name Enoyl-[acyl-carrier-protein] reductase [NADH]
Target 2 Synonyms
  1. EC 1.3.1.9
  2. NADH- dependent enoyl-ACP reductase
Target 2 Gene Name inhA
Target 2 Protein Sequence >Enoyl-[acyl-carrier-protein] reductase [NADH] 
MTGLLDGKRILVSGIITDSSIAFHIARVAQEQGAQLVLTGFDRLRLIQRITDRLPAKAPL
LELDVQNEEHLASLAGRVTEAIGAGNKLDGVVHSIGFMPQTGMGINPFFDAPYADVSKGI
HISAYSYASMAKALLPIMNPGGSIVGMDFDPSRAMPAYNWMTVAKSALESVNRFVAREAG
KYGVRSNLVAAGPIRTLAMSAIVGGALGEEAGAQIQLLEEGWDQRAPIGWNMKDATPVAK
TVCALLSDWLPATTGDIIYADGGAHTQLL
Target 2 Number of Residues 273
Target 2 Molecular Weight 28528
Target 2 Theoretical pI 6.02
Target 2 GO Classification
Function
catalytic activity
oxidoreductase activity
Process
physiological process
metabolism
Component
Not Available
Target 2 General Function Lipid transport and metabolism
Target 2 Specific Function Involved in the resistance against the antituberculosis drugs isoniazid and ethionamide
Target 2 Pathways
Name SMPDB Link KEGG Link
Fatty acid biosynthesis (path 1) map00061 Link Image
Target 2 Reactions
  • acyl-[acyl-carrier-protein] + NAD+ = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADH + H+
Target 2 Pfam Domain Function Not Available
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Essential
Target 2 GenBank ID Protein 1524230 Link Image
Target 2 UniProtKB/Swiss-Prot ID P0A5Y6 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name INHA_MYCTU Link Image
Target 2 PDB ID 1P45 Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location Not Available
Target 2 Gene Sequence >810 bp 
ATGACAGGACTGCTGGACGGCAAACGGATTCTGGTTAGCGGAATCATCACCGACTCGTCG
ATCGCGTTTCACATCGCACGGGTAGCCCAGGAGCAGGGCGCCCAGCTGGTGCTCACCGGG
TTCGACCGGCTGCGGCTGATTCAGCGCATCACCGACCGGCTGCCGGCAAAGGCCCCGCTG
CTCGAACTCGACGTGCAAAACGAGGAGCACCTGGCCAGCTTGGCCGGCCGGGTGACCGAG
GCGATCGGGGCGGGCAACAAGCTCGACGGGGTGGTGCATTCGATTGGGTTCATGCCGCAG
ACCGGGATGGGCATCAACCCGTTCTTCGACGCGCCCTACGCGGATGTGTCCAAGGGCATC
CACATCTCGGCGTATTCGTATGCTTCGATGGCCAAGGCGCTGCTGCCGATCATGAACCCC
GGAGGTTCCATCGTCGGCATGGACTTCGACCCGAGCCGGGCGATGCCGGCCTACAACTGG
ATGACGGTCGCCAAGAGCGCGTTGGAGTCGGTCAACAGGTTCGTGGCGCGCGAGGCCGGC
AAGTACGGTGTGCGTTCGAATCTCGTTGCCGCAGGCCCTATCCGGACGCTGGCGATGAGT
GCGATCGTCGGCGGTGCGCTCGGCGAGGAGGCCGGCGCCCAGATCCAGCTGCTCGAGGAG
GGCTGGGATCAGCGCGCTCCGATCGGCTGGAACATGAAGGATGCGACGCCGGTCGCCAAG
ACGGTGTGCGCGCTGCTGTCTGACTGGCTGCCGGCGACCACGGGTGACATCATCTACGCC
GACGGCGGCGCGCACACCCAATTGCTCTAG
Target 2 GenBank Gene ID
Target 2 GeneCard ID Not Available
Target 2 GenAtlas ID Not Available
Target 2 HGNC ID Not Available
Target 2 Chromosome Location Not Available
Target 2 Locus Not Available
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Rozwarski DA, Vilcheze C, Sugantino M, Bittman R, Sacchettini JC: Crystal structure of the Mycobacterium tuberculosis enoyl-ACP reductase, InhA, in complex with NAD+ and a C16 fatty acyl substrate. J Biol Chem. 1999 May 28;274(22):15582-9. [PubMed Link Image]
  2. Fleischmann RD, Alland D, Eisen JA, Carpenter L, White O, Peterson J, DeBoy R, Dodson R, Gwinn M, Haft D, Hickey E, Kolonay JF, Nelson WC, Umayam LA, Ermolaeva M, Salzberg SL, Delcher A, Utterback T, Weidman J, Khouri H, Gill J, Mikula A, Bishai W, Jacobs Jr WR Jr, Venter JC, Fraser CM: Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains. J Bacteriol. 2002 Oct;184(19):5479-90. [PubMed Link Image]
  3. Dessen A, Quemard A, Blanchard JS, Jacobs WR Jr, Sacchettini JC: Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis. Science. 1995 Mar 17;267(5204):1638-41. [PubMed Link Image]
  4. Banerjee A, Dubnau E, Quemard A, Balasubramanian V, Um KS, Wilson T, Collins D, de Lisle G, Jacobs WR Jr: inhA, a gene encoding a target for isoniazid and ethionamide in Mycobacterium tuberculosis. Science. 1994 Jan 14;263(5144):227-30. [PubMed Link Image]
  5. Rozwarski DA, Grant GA, Barton DH, Jacobs WR Jr, Sacchettini JC: Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis. Science. 1998 Jan 2;279(5347):98-102. [PubMed Link Image]
  6. Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. [PubMed Link Image]
Target 2 Drug References
  1. Broussy S, Coppel Y, Nguyen M, Bernadou J, Meunier B: 1H and 13C NMR characterization of hemiamidal isoniazid-NAD(H) adducts as possible inhibitors of InhA reductase of Mycobacterium tuberculosis. Chemistry. 2003 May 9;9(9):2034-8. [PubMed Link Image]
  2. Schroeder EK, Basso LA, Santos DS, de Souza ON: Molecular dynamics simulation studies of the wild-type, I21V, and I16T mutants of isoniazid-resistant Mycobacterium tuberculosis enoyl reductase (InhA) in complex with NADH: toward the understanding of NADH-InhA different affinities. Biophys J. 2005 Aug;89(2):876-84. Epub 2005 May 20. [PubMed Link Image]
  3. 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]
  4. 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]
  5. Wilson TM, de Lisle GW, Collins DM: Effect of inhA and katG on isoniazid resistance and virulence of Mycobacterium bovis. Mol Microbiol. 1995 Mar;15(6):1009-15. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 518
Target 3 Name Peroxidase/catalase T
Target 3 Synonyms
  1. Catalase-peroxidase T
  2. EC 1.11.1.6
Target 3 Gene Name katG
Target 3 Protein Sequence >Peroxidase/catalase T 
MPEQHPPITETTTGAASNGCPVVGHMKYPVEGGGNQDWWPNRLNLKVLHQNPAVADPMGA
AFDYAAEVATIDVDALTRDIEEVMTTSQPWWPADYGHYGPLFIRMAWHAAGTYRIHDGRG
GAGGGMQRFAPLNSWPDNASLDKARRLLWPVKKKYGKKLSWADLIVFAGNCALESMGFKT
FGFGFGRVDQWEPDEVYWGKEATWLGDERYSGKRDLENPLAAVQMGLIYVNPEGPNGNPD
PMAAAVDIRETFRRMAMNDVETAALIVGGHTFGKTHGAGPADLVGPEPEAAPLEQMGLGW
KSSYGTGTGKDAITSGIEVVWTNTPTKWDNSFLEILYGYEWELTKSPAGAWQYTAKDGAG
AGTIPDPFGGPGRSPTMLATDLSLRVDPIYERITRRWLEHPEELADEFAKAWYKLIHRDM
GPVARYLGPLVPKQTLLWQDPVPAVSHDLVGEAEIASLKSQIRASGLTVSQLVSTAWAAA
SSFRGSDKRGGANGGRIRLQPQVGWEVNDPDGDLRKVIRTLEEIQESFNSAAPGNIKVSF
ADLVVLGGCAAIEKAAKAAGHNITVPFTPGRTDASQEQTDVESFAVLEPKADGFRNYLGK
GNPLPAEYMLLDKANLLTLSAPEMTVLVGGLRVLGANYKRLPLGVFTEASESLTNDFFVN
LLDMGITWEPSPADDGTYQGKDGSGKVKWTGSRVDLVFGSNSELRALVEVYGADDAQPKF
VQDFVAAWDKVMNLDRFDVR
Target 3 Number of Residues 752
Target 3 Molecular Weight 80605
Target 3 Theoretical pI 4.87
Target 3 GO Classification
Function
antioxidant activity
peroxidase activity
catalase activity
Process
oxygen and reactive oxygen species metabolism
response to oxidative stress
physiological process
metabolism
cellular metabolism
generation of precursor metabolites and energy
electron transport
Component
Not Available
Target 3 General Function Inorganic ion transport and metabolism
Target 3 Specific Function Bifunctional, exhibiting both a catalase and broad- spectrum peroxidase activities. May play a role in the intracellular survival of mycobacteria
Target 3 Pathways
Name SMPDB Link KEGG Link
Methane metabolism map00680 Link Image
Tryptophan metabolism SMP00063 Link Image map00380 Link Image
Target 3 Reactions
  • 2 H2O2 = O2 + 2 H2O
Target 3 Pfam Domain Function
Target 3 Signals
  • None
Target 3 Transmembrane Regions
  • None
Target 3 Essentiality Essential
Target 3 GenBank ID Protein 581368 Link Image
Target 3 UniProtKB/Swiss-Prot ID Q08129 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name CATA_MYCTU Link Image
Target 3 PDB ID 1SJ2 Link Image
Target 3 PDB File Show
Target 3 3D Structure
Target 3 Cellular Location Not Available
Target 3 Gene Sequence >2223 bp 
GTGCCCGAGCAACACCCACCCATTACAGAAACCACCACCGGAGCCGCTAGCAACGGCTGT
CCCGTCGTGGGTCATATGAAATACCCCGTCGAGGGCGGCGGAAACCAGGACTGGTGGCCC
AACCGGCTCAATCTGAAGGTACTGCACCAAAACCCGGCCGTCGCTGACCCGATGGGTGCG
GCGTTCGACTATGCCGCGGAGGTCGCGACCATCGACGTTGACGCCCTGACGCGGGACATC
GAGGAAGTGATGACCACCTCGCAGCCGTGGTGGCCCGCCGACTACGGCCACTACGGGCCG
CTGTTTATCCGGATGGCGTGGCACGCTGCCGGCACCTACCGCATCCACGACGGCCGCGGC
GGCGCCGGGGGCGGCATGCAGCGGTTCGCGCCGCTTAACAGCTGGCCCGACAACGCCAGC
TTGGACAAGGCGCGCCGGCTGCTGTGGCCGGTCAAGAAGAAGTACGGCAAGAAGCTCTCA
TGGGCGGACCTGATTGTTTTCGCCGGCAACTGCGCGCTGGAATCGATGGGCTTCAAGACG
TTCGGGTTCGGCTTCGGCCGGGTCGACCAGTGGGAGCCCGATGAGGTCTATTGGGGCAAG
GAAGCCACCTGGCTCGGCGATGAGCGTTACAGCGGTAAGCGGGATCTGGAGAACCCGCTG
GCCGCGGTGCAGATGGGGCTGATCTACGTGAACCCGGAGGCGCCGAACGGCAACCCGGAC
CCCATGGCCGCGGCGGTCGACATTCGCGAGACGTTTCGGCGCATGGCCATGAACGACGTC
GAAACAGCGGCGCTGATCGTCGGCGGTCACACTTTCGGTAAGACCCATGGCGCCGGCCCG
GCCGATCTGGTCGGCCCCGAACCCGAGGCTGCTCCGCTGGAGCAGATGGGCTTGGGCTGG
AAGAGCTCGTATGGCACCGGAACCGGTAAGGACGCGATCACCAGCGGCATCGAGGTCGTA
TGGACGAACACCCCGACGAAATGGGACAACAGTTTCCTCGAGATCCTGTACGGCTACGAG
TGGGAGCTGACGAAGAGCCCTGCTGGCGCTTGGCAATACACCGCCAAGGACGGCGCCGGT
GCCGGCACCATCCCGGACCCGTTCGGCGGGCCAGGGCGCTCCCCGACGATGCTGGCCACT
GACCTCTCGCTGCGGGTGGATCCGATCTATGAGCGGATCACGCGTCGCTGGCTGGAACAC
CCCGAGGAATTGGCCGACGAGTTCGCCAAGGCCTGGTACAAGCTGATCCACCGAGACATG
GGTCCCGTTGCGAGATACCTTGGGCCGCTGGTCCCCAAGCAGACCCTGCTGTGGCAGGAT
CCGGTCCCTGCGGTCAGCCACGACCTCGTCGGCGAAGCCGAGATTGCCAGCCTTAAGAGC
CAGATCCGGGCATCGGGATTGACTGTCTCACAGCTAGTTTCGACCGCATGGGCGGCGGCG
TCGTCGTTCCGTGGTAGCGACAAGCGCGGCGGCGCCAACGGTGGTCGCATCCGCCTGCAG
CCACAAGTCGGGTGGGAGGTCAACGACCCCGACGGGGATCTGCGCAAGGTCATTCGCACC
CTGGAAGAGATCCAGGAGTCATTCAACTCCGCGGCGCCGGGGAACATCAAAGTGTCCTTC
GCCGACCTCGTCGTGCTCGGTGGCTGTGCCGCCATAGAGAAAGCAGCAAAGGCGGCTGGC
CACAACATCACGGTGCCCTTCACCCCGGGCCGCACGGATGCGTCGCAGGAACAAACCGAC
GTGGAATCCTTTGCCGTGCTGGAGCCCAAGGCAGATGGCTTCCGAAACTACCTCGGAAAG
GGCAACCCGTTGCCGGCCGAGTACATGCTGCTCGACAAGGCGAACCTGCTTACGCTCAGT
GCCCCTGAGATGACGGTGCTGGTAGGTGGCCTGCGCGTCCTCGGCGCAAACTACAAGCGC
TTACCGCTGGGCGTGTTCACCGAGGCCTCCGAGTCACTGACCAACGACTTCTTCGTGAAC
CTGCTCGACATGGGTATCACCTGGGAGCCCTCGCCAGCAGATGACGGGACCTACCAGGGC
AAGGATGGCAGTGGCAAGGTGAAGTGGACCGGCAGCCGCGTGGACCTGGTCTTCGGGTCC
AACTCGGAGTTGCGGGCGCTTGTCGAGGTCTATGGCGCCGATGACGCGCAGCCGAAGTTC
GTGCAGGACTTCGTCGCTGCCTGGGACAAGGTGATGAACCTCGACAGGTTCGACGTGCGC
TGA
Target 3 GenBank Gene ID
Target 3 GeneCard ID Not Available
Target 3 GenAtlas ID Not Available
Target 3 HGNC ID Not Available
Target 3 Chromosome Location Not Available
Target 3 Locus Not Available
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Fleischmann RD, Alland D, Eisen JA, Carpenter L, White O, Peterson J, DeBoy R, Dodson R, Gwinn M, Haft D, Hickey E, Kolonay JF, Nelson WC, Umayam LA, Ermolaeva M, Salzberg SL, Delcher A, Utterback T, Weidman J, Khouri H, Gill J, Mikula A, Bishai W, Jacobs Jr WR Jr, Venter JC, Fraser CM: Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains. J Bacteriol. 2002 Oct;184(19):5479-90. [PubMed Link Image]
  2. Zhang Y, Heym B, Allen B, Young D, Cole S: The catalase-peroxidase gene and isoniazid resistance of Mycobacterium tuberculosis. Nature. 1992 Aug 13;358(6387):591-3. [PubMed Link Image]
  3. Heym B, Zhang Y, Poulet S, Young D, Cole ST: Characterization of the katG gene encoding a catalase-peroxidase required for the isoniazid susceptibility of Mycobacterium tuberculosis. J Bacteriol. 1993 Jul;175(13):4255-9. [PubMed Link Image]
  4. Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. [PubMed Link Image]
Target 3 Drug References
  1. Pym AS, Domenech P, Honore N, Song J, Deretic V, Cole ST: Regulation of catalase-peroxidase (KatG) expression, isoniazid sensitivity and virulence by furA of Mycobacterium tuberculosis. Mol Microbiol. 2001 May;40(4):879-89. [PubMed Link Image]
  2. 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]
  3. 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]
  4. Wilson TM, de Lisle GW, Collins DM: Effect of inhA and katG on isoniazid resistance and virulence of Mycobacterium bovis. Mol Microbiol. 1995 Mar;15(6):1009-15. [PubMed Link Image]
  5. Heym B, Alzari PM, Honore N, Cole ST: Missense mutations in the catalase-peroxidase gene, katG, are associated with isoniazid resistance in Mycobacterium tuberculosis. Mol Microbiol. 1995 Jan;15(2):235-45. [PubMed Link Image]
Drug Target 4 [top]
Target 4 ID 4834
Target 4 Name Arylamine N-acetyltransferase
Target 4 Synonyms
  1. EC 2.3.1.5
Target 4 Gene Name nat
Target 4 Protein Sequence >Arylamine N-acetyltransferase 
MAMDLGGYLTRIGLDGRPRPDLGTLHAIVAAHNRSIPFENLDPLLGIPVADLSAEALFAK
LVDRRRGGYCYEHNGLLGYVLEELGFEVERLSGRVVWMRADDAPLPAQTHNVLSVAVPGA
DGRYLVDVGFGGQTLTSPIRLEAGPVQQTRHEPYRLTRHGDDHTLAAQVRGEWQPLYTFT
TEPRPRIDLEVGSWYVSTHPGSHFVTGLTVAVVTDDARYNLRGRNLAVHRSGATEHIRFD
SAAQVLDAIVNRFGIDLGDLAGRDVQARVAEVLDT
Target 4 Number of Residues 279
Target 4 Molecular Weight 30174
Target 4 Theoretical pI 6.12
Target 4 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring acyl groups
transferase activity, transferring groups other than amino-acyl groups
acyltransferase activity
acetyltransferase activity
N-acetyltransferase activity
arylamine N-acetyltransferase activity
Process
physiological process
metabolism
Component
Not Available
Target 4 General Function Involved in arylamine N-acetyltransferase activity
Target 4 Specific Function Could have a role in acetylating, and hence inactivating, the antitubercular drug isoniazid
Target 4 Pathways Not Available
Target 4 Reactions Not Available
Target 4 Pfam Domain Function
Target 4 Signals
  • None
Target 4 Transmembrane Regions
  • None
Target 4 Essentiality Essential
Target 4 GenBank ID Protein Not Available
Target 4 UniProtKB/Swiss-Prot ID O86309 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name NAT_MYCSM Link Image
Target 4 PDB ID 1W6F Link Image
Target 4 PDB File Show
Target 4 3D Structure
Target 4 Cellular Location
  • Cytoplasm
Target 4 Gene Sequence Not Available
Target 4 GenBank Gene ID
Target 4 GeneCard ID Not Available
Target 4 GenAtlas ID Not Available
Target 4 HGNC ID Not Available
Target 4 Chromosome Location Not Available
Target 4 Locus Not Available
Target 4 SNPs SNPJam Report Link Image
Target 4 General References
  1. Sandy J, Mushtaq A, Kawamura A, Sinclair J, Sim E, Noble M: The structure of arylamine N-acetyltransferase from Mycobacterium smegmatis--an enzyme which inactivates the anti-tubercular drug, isoniazid. J Mol Biol. 2002 May 10;318(4):1071-83. [PubMed Link Image]
  2. Payton M, Auty R, Delgoda R, Everett M, Sim E: Cloning and characterization of arylamine N-acetyltransferase genes from Mycobacterium smegmatis and Mycobacterium tuberculosis: increased expression results in isoniazid resistance. J Bacteriol. 1999 Feb;181(4):1343-7. [PubMed Link Image]
Target 4 Drug References Not Available

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.