Catalase-peroxidase

Details

Name
Catalase-peroxidase
Synonyms
  • 1.11.1.21
  • CP
  • Peroxidase/catalase
Gene Name
katG
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Amino acid sequence
>lcl|BSEQ0051179|Catalase-peroxidase
MPEQHPPITETTTGAASNGCPVVGHMKYPVEGGGNQDWWPNRLNLKVLHQNPAVADPMGA
AFDYAAEVATIDVDALTRDIEEVMTTSQPWWPADYGHYGPLFIRMAWHAAGTYRIHDGRG
GAGGGMQRFAPLNSWPDNASLDKARRLLWPVKKKYGKKLSWADLIVFAGNCALESMGFKT
FGFGFGRVDQWEPDEVYWGKEATWLGDERYSGKRDLENPLAAVQMGLIYVNPEGPNGNPD
PMAAAVDIRETFRRMAMNDVETAALIVGGHTFGKTHGAGPADLVGPEPEAAPLEQMGLGW
KSSYGTGTGKDAITSGIEVVWTNTPTKWDNSFLEILYGYEWELTKSPAGAWQYTAKDGAG
AGTIPDPFGGPGRSPTMLATDLSLRVDPIYERITRRWLEHPEELADEFAKAWYKLIHRDM
GPVARYLGPLVPKQTLLWQDPVPAVSHDLVGEAEIASLKSQIRASGLTVSQLVSTAWAAA
SSFRGSDKRGGANGGRIRLQPQVGWEVNDPDGDLRKVIRTLEEIQESFNSAAPGNIKVSF
ADLVVLGGCAAIEKAAKAAGHNITVPFTPGRTDASQEQTDVESFAVLEPKADGFRNYLGK
GNPLPAEYMLLDKANLLTLSAPEMTVLVGGLRVLGANYKRLPLGVFTEASESLTNDFFVN
LLDMGITWEPSPADDGTYQGKDGSGKVKWTGSRVDLVFGSNSELRALVEVYGADDAQPKF
VQDFVAAWDKVMNLDRFDVR
Number of residues
740
Molecular Weight
80604.275
Theoretical pI
Not Available
GO Classification
Functions
catalase activity / heme binding / metal ion binding / NADH binding / NADPH binding / oxidoreductase activity, acting on a heme group of donors, nitrogenous group as acceptor / peroxidase activity
Processes
cellular response to hydrogen peroxide / evasion or tolerance by symbiont of host-produced reactive oxygen species / hydrogen peroxide catabolic process / pathogenesis / positive regulation of DNA repair / response to antibiotic / response to oxidative stress
Components
cell wall / cytosol / extracellular region / plasma membrane
General Function
Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity, oxidizing various electron donors including NADP(H) (PubMed:9006925, PubMed:18178143). Protects M.tuberculosis against toxic reactive oxygen species (ROS) including hydrogen peroxide as well as organic peroxides and thus contributes to its survival within host macrophages by countering the phagocyte oxidative burst (PubMed:8658136, PubMed:15165233). Also displays efficient peroxynitritase activity, which may help the bacterium to persist in macrophages (PubMed:10080924).
Specific Function
Catalase activity
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0051180|Catalase-peroxidase (katG)
GTGCCCGAGCAACACCCACCCATTACAGAAACCACCACCGGAGCCGCTAGCAACGGCTGT
CCCGTCGTGGGTCATATGAAATACCCCGTCGAGGGCGGCGGAAACCAGGACTGGTGGCCC
AACCGGCTCAATCTGAAGGTACTGCACCAAAACCCGGCCGTCGCTGACCCGATGGGTGCG
GCGTTCGACTATGCCGCGGAGGTCGCGACCATCGACGTTGACGCCCTGACGCGGGACATC
GAGGAAGTGATGACCACCTCGCAGCCGTGGTGGCCCGCCGACTACGGCCACTACGGGCCG
CTGTTTATCCGGATGGCGTGGCACGCTGCCGGCACCTACCGCATCCACGACGGCCGCGGC
GGCGCCGGGGGCGGCATGCAGCGGTTCGCGCCGCTTAACAGCTGGCCCGACAACGCCAGC
TTGGACAAGGCGCGCCGGCTGCTGTGGCCGGTCAAGAAGAAGTACGGCAAGAAGCTCTCA
TGGGCGGACCTGATTGTTTTCGCCGGCAACTGCGCGCTGGAATCGATGGGCTTCAAGACG
TTCGGGTTCGGCTTCGGCCGGGTCGACCAGTGGGAGCCCGATGAGGTCTATTGGGGCAAG
GAAGCCACCTGGCTCGGCGATGAGCGTTACAGCGGTAAGCGGGATCTGGAGAACCCGCTG
GCCGCGGTGCAGATGGGGCTGATCTACGTGAACCCGGAGGGGCCGAACGGCAACCCGGAC
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
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP9WIE5
UniProtKB Entry NameKATG_MYCTU
General References
  1. 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. [Article]
  2. Cockerill FR 3rd, Uhl JR, Temesgen Z, Zhang Y, Stockman L, Roberts GD, Williams DL, Kline BC: Rapid identification of a point mutation of the Mycobacterium tuberculosis catalase-peroxidase (katG) gene associated with isoniazid resistance. J Infect Dis. 1995 Jan;171(1):240-5. [Article]
  3. Daum LT, Rodriguez JD, Worthy SA, Ismail NA, Omar SV, Dreyer AW, Fourie PB, Hoosen AA, Chambers JP, Fischer GW: Next-generation ion torrent sequencing of drug resistance mutations in Mycobacterium tuberculosis strains. J Clin Microbiol. 2012 Dec;50(12):3831-7. doi: 10.1128/JCM.01893-12. Epub 2012 Sep 12. [Article]
  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. [Article]
  5. 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. [Article]
  6. Mulder MA, Nair S, Abratt VR, Zappe H, Steyn LM: Involvement of the N- and C-terminal domains of Mycobacterium tuberculosis KatG in the protection of mutant Escherichia coli against DNA-damaging agents. Microbiology. 1999 Aug;145 ( Pt 8):2011-21. [Article]
  7. Sherman DR, Mdluli K, Hickey MJ, Arain TM, Morris SL, Barry CE 3rd, Stover CK: Compensatory ahpC gene expression in isoniazid-resistant Mycobacterium tuberculosis. Science. 1996 Jun 14;272(5268):1641-3. [Article]
  8. Johnsson K, Froland WA, Schultz PG: Overexpression, purification, and characterization of the catalase-peroxidase KatG from Mycobacterium tuberculosis. J Biol Chem. 1997 Jan 31;272(5):2834-40. [Article]
  9. Wengenack NL, Jensen MP, Rusnak F, Stern MK: Mycobacterium tuberculosis KatG is a peroxynitritase. Biochem Biophys Res Commun. 1999 Mar 24;256(3):485-7. [Article]
  10. 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. [Article]
  11. Ng VH, Cox JS, Sousa AO, MacMicking JD, McKinney JD: Role of KatG catalase-peroxidase in mycobacterial pathogenesis: countering the phagocyte oxidative burst. Mol Microbiol. 2004 Jun;52(5):1291-302. [Article]
  12. Ghiladi RA, Knudsen GM, Medzihradszky KF, Ortiz de Montellano PR: The Met-Tyr-Trp cross-link in Mycobacterium tuberculosis catalase-peroxidase (KatG): autocatalytic formation and effect on enzyme catalysis and spectroscopic properties. J Biol Chem. 2005 Jun 17;280(24):22651-63. Epub 2005 Apr 18. [Article]
  13. Jakopitsch C, Vlasits J, Wiseman B, Loewen PC, Obinger C: Redox intermediates in the catalase cycle of catalase-peroxidases from Synechocystis PCC 6803, Burkholderia pseudomallei, and Mycobacterium tuberculosis. Biochemistry. 2007 Feb 6;46(5):1183-93. [Article]
  14. Singh R, Switala J, Loewen PC, Ivancich A: Two [Fe(IV)=O Trp*] intermediates in M. tuberculosis catalase-peroxidase discriminated by multifrequency (9-285 GHz) EPR spectroscopy: reactivity toward isoniazid. J Am Chem Soc. 2007 Dec 26;129(51):15954-63. Epub 2007 Dec 4. [Article]
  15. Singh R, Wiseman B, Deemagarn T, Jha V, Switala J, Loewen PC: Comparative study of catalase-peroxidases (KatGs). Arch Biochem Biophys. 2008 Mar 15;471(2):207-14. doi: 10.1016/j.abb.2007.12.008. Epub 2007 Dec 23. [Article]
  16. Raman K, Yeturu K, Chandra N: targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis. BMC Syst Biol. 2008 Dec 19;2:109. doi: 10.1186/1752-0509-2-109. [Article]
  17. Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A: Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3. [Article]
  18. Ando H, Kitao T, Miyoshi-Akiyama T, Kato S, Mori T, Kirikae T: Downregulation of katG expression is associated with isoniazid resistance in Mycobacterium tuberculosis. Mol Microbiol. 2011 Mar;79(6):1615-28. doi: 10.1111/j.1365-2958.2011.07547.x. Epub 2011 Feb 10. [Article]
  19. Bertrand T, Eady NA, Jones JN, Jesmin, Nagy JM, Jamart-Gregoire B, Raven EL, Brown KA: Crystal structure of Mycobacterium tuberculosis catalase-peroxidase. J Biol Chem. 2004 Sep 10;279(37):38991-9. Epub 2004 Jul 1. [Article]
  20. Zhao X, Yu H, Yu S, Wang F, Sacchettini JC, Magliozzo RS: Hydrogen peroxide-mediated isoniazid activation catalyzed by Mycobacterium tuberculosis catalase-peroxidase (KatG) and its S315T mutant. Biochemistry. 2006 Apr 4;45(13):4131-40. [Article]
  21. Zhao X, Hersleth HP, Zhu J, Andersson KK, Magliozzo RS: Access channel residues Ser315 and Asp137 in Mycobacterium tuberculosis catalase-peroxidase (KatG) control peroxidatic activation of the pro-drug isoniazid. Chem Commun (Camb). 2013 Dec 25;49(99):11650-2. doi: 10.1039/c3cc47022a. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00609Ethionamideapprovedunknownother/unknownDetails
DB00951Isoniazidapproved, investigationalyesother/unknownDetails