Escherichia coli K-12 substr. MG1655 Enzyme: catalase II

Gene: katE Accession Numbers: EG10509 (EcoCyc), b1732, ECK1730

Synonyms: catalase HPII, HPII, hydroperoxidase II, HPIII

Regulation Summary Diagram: ?

Regulation summary diagram for katE

Subunit composition of catalase II = [KatE]4
         catalase II = KatE

There are two distinct catalases in E. coli. The KatE enzyme is the monofunctional catalase HPII. A bifunctional catalase, HPI, is encoded by katG [Loewen86]. Aerobically grown E. coli produce sufficient endogenous H2O2 to cause toxic levels of DNA damage via the Fenton reaction [Park05]; endogenously produced H2O2 is primarily scavenged by a third enzyme, alkyl hydroperoxide reductase, while catalase is the primary scavenger at high H2O2 concentrations [Seaver01a, Seaver01].

While most heme proteins contain ferroheme b as the prosthetic group, HPII contains a unique cofactor, heme d. It has been suggested that heme d is formed in a reaction catalyzed by HPII itself. Based on this model, HPII first binds protoheme, which is subsequently hydroxylated by HPII utilizing one of the first H2O2 substrate molecules [Timkovich90]. Later work has supported this theory. While HPII from aerobically grown E. coli contains heme d, HPII purified from microaerobic or anaerobic cultures contains a mixture of heme d and ferroheme b. The protoheme of HPII obtained from such cells can be converted into heme d by treatment of the purified enzyme with hydrogen peroxide. The His128 residue of HPII is required for this conversion [Loewen93].

A number of crystal structures of wild type and mutant forms of KatE have been reported [Tormo90, Bravo95, Murshudov96, Bravo97, Bravo99, Sevinc99, MelikAdamyan01, Chelikani03, Chelikani05, Jha11, Jha12]. The apparent hexameric structure of HPII was noted to be unusual [Loewen86]; however, crystal structures show a homotetrameric enzyme, each subunit containing a cis-heme d group [Bravo95]. The heme d group is rotated 180° with the respect to the orientation found for protoheme IX in beef liver catalase [Murshudov96, Bravo99]. The Ile274 residue influences heme orientation [Jha11]. The proximal ligand for the heme group is Tyr415 [Dawson91, Bravo99]. His392 and Tyr415 are linked by a bond between the Nδ of His and the Cβ of Tyr. Although the bond was initially only apparent in subunits that contained a heme d group [Bravo97], it was later found that His-Tyr bond formation and heme oxidation can be uncoupled [MelikAdamyan01]. The catalytic activity of various site-directed mutants in active site residues N201 and H128 has been analyzed. Formation of heme d from protoheme may occur via a protoheme compound I [Obinger97]. The S234 and E530 residues also appear to have a role in the oxidation of the heme b to heme d [Jha12a].

The active site heme groups are deeply buried within the enzyme, requiring substrates and products to move through channels within the enzyme. Various mutants have been constructed, and activity measurements and crystal structures of the resulting enzymes have elucidated the structure and function of those channels [Sevinc99, Mate99, MelikAdamyan01, Chelikani03, Chelikani05, Jha11, Jha12a].

Compared to some other catalases, HPII contains both N- and C-terminal extensions. Both domains are required for accumulation of active enzyme [Sevinc98]. Approximately 90 residues of the N-terminus of each subunit are inserted into a loop on the adjacent subunit. This interwoven structure was thought to contribute to the exceptional thermal stability of the enzyme [Switala99], but a later study showed that C-terminal truncation had a larger effect on stability [Chelikani03a]. The C-terminal domain is a divergent member of the type I glutamine amidotransferase (GAT) superfamily; it lacks the catalytic triad and thus also enzymatic activity [Horvath01]. A proteolytically truncated form of HPII that lacks 36% of its sequence has been analyzed [Chelikani05].

KatE production is increased in stationary phase [Loewen85, Schellhorn88] and by hyperosmotic stress [Weber06] and is four-fold higher under aerobic compared to anaerobic growth conditions [Schellhorn88]. Expression is dependent on σS (KatF) [Schellhorn88, Sak89, Tanaka97]. Overexpression of katE suppresses H2O2 sensitivity of an oxyR mutant strain [Greenberg88]. A katE mutant is more sensitive to chromate than wild type [Ackerley06].

Reviews: [Schellhorn95, Loewen96, Mishra12]

Citations: [Loewen84, Mulvey88, Mulvey90, Schellhorn92, Peng92, Smirnova00, Oktyabrsky01, Smirnova, Jung03, Semchyshyn, Benov03, Semchyshyna, Hoerter05, Park07]

Gene Citations: [vonOssowski91]

Locations: cytosol

Map Position: [1,811,891 -> 1,814,152] (39.05 centisomes, 141°)
Length: 2262 bp / 753 aa

Molecular Weight of Polypeptide: 84.162 kD (from nucleotide sequence), 92.0 kD (experimental) [Loewen86 ]

Molecular Weight of Multimer: 532.0 kD (experimental) [Loewen86]

pI: 5.87

Unification Links: ASAP:ABE-0005780 , CGSC:593 , DIP:DIP-10052N , EchoBASE:EB0504 , EcoGene:EG10509 , EcoliWiki:b1732 , Mint:MINT-1247982 , ModBase:P21179 , OU-Microarray:b1732 , PortEco:katE , PR:PRO_000023042 , Pride:P21179 , Protein Model Portal:P21179 , RefSeq:YP_025308 , RegulonDB:EG10509 , SMR:P21179 , String:511145.b1732 , UniProt:P21179

Relationship Links: InterPro:IN-FAMILY:IPR002226 , InterPro:IN-FAMILY:IPR010582 , InterPro:IN-FAMILY:IPR011614 , InterPro:IN-FAMILY:IPR018028 , InterPro:IN-FAMILY:IPR020835 , InterPro:IN-FAMILY:IPR024708 , InterPro:IN-FAMILY:IPR024712 , InterPro:IN-FAMILY:IPR029062 , Panther:IN-FAMILY:PTHR11465 , PDB:Structure:1CF9 , PDB:Structure:1GG9 , PDB:Structure:1GGE , PDB:Structure:1GGF , PDB:Structure:1GGH , PDB:Structure:1GGJ , PDB:Structure:1GGK , PDB:Structure:1IPH , PDB:Structure:1P7Y , PDB:Structure:1P7Z , PDB:Structure:1P80 , PDB:Structure:1P81 , PDB:Structure:1QF7 , PDB:Structure:1QWS , PDB:Structure:1YE9 , PDB:Structure:3P9P , PDB:Structure:3P9Q , PDB:Structure:3P9R , PDB:Structure:3P9S , PDB:Structure:3PQ2 , PDB:Structure:3PQ3 , PDB:Structure:3PQ4 , PDB:Structure:3PQ5 , PDB:Structure:3PQ6 , PDB:Structure:3PQ7 , PDB:Structure:3PQ8 , PDB:Structure:3TTT , PDB:Structure:3TTU , PDB:Structure:3TTV , PDB:Structure:3TTW , PDB:Structure:3TTX , PDB:Structure:3VU3 , PDB:Structure:4BFL , PDB:Structure:4ENP , PDB:Structure:4ENQ , PDB:Structure:4ENR , PDB:Structure:4ENS , PDB:Structure:4ENT , PDB:Structure:4ENU , PDB:Structure:4ENV , PDB:Structure:4ENW , Pfam:IN-FAMILY:PF00199 , Pfam:IN-FAMILY:PF06628 , Prints:IN-FAMILY:PR00067 , Prosite:IN-FAMILY:PS00437 , Prosite:IN-FAMILY:PS00438 , Prosite:IN-FAMILY:PS51402 , Smart:IN-FAMILY:SM01060

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Genetic Regulation Schematic: ?

Genetic regulation schematic for katE

GO Terms:

Biological Process: GO:0006972 - hyperosmotic response Inferred from experiment [Weber06]
GO:0006974 - cellular response to DNA damage stimulus Inferred from experiment [Khil02]
GO:0006979 - response to oxidative stress Inferred from experiment Inferred by computational analysis [GOA01a, Loewen84a]
GO:0042744 - hydrogen peroxide catabolic process Inferred from experiment Inferred by computational analysis [UniProtGOA11, Loewen84a]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11, GOA01a]
Molecular Function: GO:0004096 - catalase activity Inferred from experiment Inferred by computational analysis [GOA01, GOA01a, Loewen86, Loewen84a]
GO:0005506 - iron ion binding Inferred from experiment [Bravo95]
GO:0020037 - heme binding Inferred from experiment Inferred by computational analysis [GOA01a, Bravo95]
GO:0042802 - identical protein binding Inferred from experiment [Rajagopala14, Lasserre06, Bravo95]
GO:0004601 - peroxidase activity Inferred by computational analysis [UniProtGOA11]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005737 - cytoplasm Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, Heimberger88]
GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Lasserre06]

MultiFun Terms: cell processes protection detoxification

Essentiality data for katE knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Last-Curated ? 03-Dec-2012 by Keseler I , SRI International

Enzymatic reaction of: catalase

Synonyms: hydroperoxidase, hydrogen peroxide:hydrogen peroxide oxidoreductase

EC Number:

2 hydrogen peroxide <=> 2 H2O + oxygen

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

In Pathways: superoxide radicals degradation

The enzyme was first purified from E. coli B [Claiborne79].

Cofactors or Prosthetic Groups: heme d [Loewen86]

Cofactor Binding Comment: contains one cis-heme d isomer per subunit [Loewen93]

Inhibitors (Unknown Mechanism): cyanide [Maj96]

Kinetic Parameters:

Km (μM)
Specific Activity (U/mg)
hydrogen peroxide

pH(opt): 4-11 [Loewen86]

Enzymatic reaction of: heme d synthase (catalase II)

heme b + hydrogen peroxide <=> heme d

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

Reversibility of this reaction is unspecified.

Citations: [Timkovich90]

Sequence Features

Protein sequence of catalase II with features indicated

Feature Class Location Citations Comment
Active-Site 128
UniProt: Non-Experimental Qualifier: by similarity;
Active-Site 201
UniProt: Non-Experimental Qualifier: by similarity;
Crosslink-Site 392, 415
UniProt: 3'-histidyl-3-tyrosine (His-Tyr).
Metal-Binding-Site 415
UniProt: Iron (heme axial ligand).

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


10/20/97 Gene b1732 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10509; confirmed by SwissProt match.


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Horvath01: Horvath MM, Grishin NV (2001). "The C-terminal domain of HPII catalase is a member of the type I glutamine amidotransferase superfamily." Proteins 42(2);230-6. PMID: 11119647

Jha11: Jha V, Louis S, Chelikani P, Carpena X, Donald LJ, Fita I, Loewen PC (2011). "Modulation of heme orientation and binding by a single residue in catalase HPII of Escherichia coli." Biochemistry 50(12);2101-10. PMID: 21332158

Jha12: Jha V, Donald LJ, Loewen PC (2012). "Mutation of Phe413 to Tyr in catalase KatE from Escherichia coli leads to side chain damage and main chain cleavage." Arch Biochem Biophys 525(2);207-14. PMID: 22172685

Jha12a: Jha V, Chelikani P, Carpena X, Fita I, Loewen PC (2012). "Influence of main channel structure on H(2)O(2) access to the heme cavity of catalase KatE of Escherichia coli." Arch Biochem Biophys 526(1);54-9. PMID: 22820098

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Jung03: Jung IL, Kim IG (2003). "Transcription of ahpC, katG, and katE genes in Escherichia coli is regulated by polyamines: polyamine-deficient mutant sensitive to H2O2-induced oxidative damage." Biochem Biophys Res Commun 301(4);915-22. PMID: 12589799

Khil02: Khil PP, Camerini-Otero RD (2002). "Over 1000 genes are involved in the DNA damage response of Escherichia coli." Mol Microbiol 44(1);89-105. PMID: 11967071

Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726

Loewen84: Loewen PC, Triggs BL (1984). "Genetic mapping of katF, a locus that with katE affects the synthesis of a second catalase species in Escherichia coli." J Bacteriol 160(2);668-75. PMID: 6094482

Loewen84a: Loewen PC (1984). "Isolation of catalase-deficient Escherichia coli mutants and genetic mapping of katE, a locus that affects catalase activity." J Bacteriol 157(2);622-6. PMID: 6319370

Loewen85: Loewen PC, Switala J, Triggs-Raine BL (1985). "Catalases HPI and HPII in Escherichia coli are induced independently." Arch Biochem Biophys 1985;243(1);144-9. PMID: 3904630

Loewen86: Loewen PC, Switala J (1986). "Purification and characterization of catalase HPII from Escherichia coli K12." Biochem Cell Biol 1986;64(7);638-46. PMID: 3019370

Loewen93: Loewen PC, Switala J, von Ossowski I, Hillar A, Christie A, Tattrie B, Nicholls P (1993). "Catalase HPII of Escherichia coli catalyzes the conversion of protoheme to cis-heme d." Biochemistry 1993;32(38);10159-64. PMID: 8399141

Loewen96: Loewen P (1996). "Probing the structure of catalase HPII of Escherichia coli--a review." Gene 179(1);39-44. PMID: 8955627

Maj96: Maj M, Nicholls P, Obinger C, Hillar A, Loewen PC (1996). "Reaction of E. coli catalase HPII with cyanide as ligand and as inhibitor." Biochim Biophys Acta 1298(2);241-9. PMID: 8980649

Maj98: Maj M, Loewen P, Nicholls P (1998). "E. coli HPII catalase interaction with high spin ligands: formate and fluoride as active site probes." Biochim Biophys Acta 1384(2);209-22. PMID: 9659382

Mate99: Mate MJ, Sevinc MS, Hu B, Bujons J, Bravo J, Switala J, Ens W, Loewen PC, Fita I (1999). "Mutants that alter the covalent structure of catalase hydroperoxidase II from Escherichia coli." J Biol Chem 274(39);27717-25. PMID: 10488114

MelikAdamyan01: Melik-Adamyan W, Bravo J, Carpena X, Switala J, Mate MJ, Fita I, Loewen PC (2001). "Substrate flow in catalases deduced from the crystal structures of active site variants of HPII from Escherichia coli." Proteins 44(3);270-81. PMID: 11455600

Mishra12: Mishra S, Imlay J (2012). "Why do bacteria use so many enzymes to scavenge hydrogen peroxide?." Arch Biochem Biophys 525(2);145-60. PMID: 22609271

Mulvey88: Mulvey MR, Sorby PA, Triggs-Raine BL, Loewen PC (1988). "Cloning and physical characterization of katE and katF required for catalase HPII expression in Escherichia coli." Gene 73(2);337-45. PMID: 2977357

Mulvey90: Mulvey MR, Switala J, Borys A, Loewen PC (1990). "Regulation of transcription of katE and katF in Escherichia coli." J Bacteriol 172(12);6713-20. PMID: 2254248

Murshudov96: Murshudov GN, Grebenko AI, Barynin V, Dauter Z, Wilson KS, Vainshtein BK, Melik-Adamyan W, Bravo J, Ferran JM, Ferrer JC, Switala J, Loewen PC, Fita I (1996). "Structure of the heme d of Penicillium vitale and Escherichia coli catalases." J Biol Chem 271(15);8863-8. PMID: 8621527

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Oktyabrsky01: Oktyabrsky ON, Smirnovam GV, Muzyka NG (2001). "Role of glutathione in regulation of hydroperoxidase I in growing Escherichia coli." Free Radic Biol Med 31(2);250-5. PMID: 11440837

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Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554

Sak89: Sak BD, Eisenstark A, Touati D (1989). "Exonuclease III and the catalase hydroperoxidase II in Escherichia coli are both regulated by the katF gene product." Proc Natl Acad Sci U S A 86(9);3271-5. PMID: 2541439

Schellhorn88: Schellhorn HE, Hassan HM (1988). "Transcriptional regulation of katE in Escherichia coli K-12." J Bacteriol 170(9);4286-92. PMID: 3045091

Schellhorn92: Schellhorn HE, Stones VL (1992). "Regulation of katF and katE in Escherichia coli K-12 by weak acids." J Bacteriol 174(14);4769-76. PMID: 1385595

Schellhorn95: Schellhorn HE (1995). "Regulation of hydroperoxidase (catalase) expression in Escherichia coli." FEMS Microbiol Lett 131(2);113-9. PMID: 7557318

Seaver01: Seaver LC, Imlay JA (2001). "Hydrogen peroxide fluxes and compartmentalization inside growing Escherichia coli." J Bacteriol 183(24);7182-9. PMID: 11717277

Seaver01a: Seaver LC, Imlay JA (2001). "Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli." J Bacteriol 183(24);7173-81. PMID: 11717276

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Semchyshyna: Semchyshyn HM, Lushchak VI "[Oxidative stress and control of catalase activity in Escherichia coli]." Ukr Biokhim Zh 76(2);31-42. PMID: 15915708

Sevinc95: Sevinc MS, Ens W, Loewen PC (1995). "The cysteines of catalase HPII of Escherichia coli, including Cys438 which is blocked, do not have a catalytic role." Eur J Biochem 230(1);127-32. PMID: 7601091

Sevinc98: Sevinc MS, Switala J, Bravo J, Fita I, Loewen PC (1998). "Truncation and heme pocket mutations reduce production of functional catalase HPII in Escherichia coli." Protein Eng 11(7);549-55. PMID: 9740372

Sevinc99: Sevinc MS, Mate MJ, Switala J, Fita I, Loewen PC (1999). "Role of the lateral channel in catalase HPII of Escherichia coli." Protein Sci 8(3);490-8. PMID: 10091651

Smirnova: Smirnova GV, Zakirova ON, Oktiabr'skii ON "[The role of antioxidant systems in response of bacteria Escherichia coli to heat shock]." Mikrobiologiia 70(5);595-601. PMID: 11763776

Smirnova00: Smirnova GV, Muzyka NG, Oktyabrsky ON (2000). "The role of antioxidant enzymes in response of Escherichia coli to osmotic upshift." FEMS Microbiol Lett 186(2);209-13. PMID: 10802173

Switala99: Switala J, O'Neil JO, Loewen PC (1999). "Catalase HPII from Escherichia coli exhibits enhanced resistance to denaturation." Biochemistry 38(13);3895-901. PMID: 10194300

Tanaka97: Tanaka K, Handel K, Loewen PC, Takahashi H (1997). "Identification and analysis of the rpoS-dependent promoter of katE, encoding catalase HPII in Escherichia coli." Biochim Biophys Acta 1352(2);161-6. PMID: 9199247

Timkovich90: Timkovich R, Bondoc LL (1990). "Diversity in the Structure of Hemes." Adv. in Biophysics, vol. 1, C.A. Bush, ed., Jai Press, 203-247.

Tormo90: Tormo J, Fita I, Switala J, Loewen PC (1990). "Crystallization and preliminary X-ray diffraction analysis of catalase HPII from Escherichia coli." J Mol Biol 213(2);219-20. PMID: 2187997

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt15: UniProt Consortium (2015). "UniProt version 2015-01 released on 2015-01-16 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

vonOssowski91: von Ossowski I, Mulvey MR, Leco PA, Borys A, Loewen PC (1991). "Nucleotide sequence of Escherichia coli katE, which encodes catalase HPII." J Bacteriol 1991;173(2);514-20. PMID: 1987146

Weber06: Weber A, Kogl SA, Jung K (2006). "Time-dependent proteome alterations under osmotic stress during aerobic and anaerobic growth in Escherichia coli." J Bacteriol 188(20);7165-75. PMID: 17015655

Other References Related to Gene Regulation

Bradley07: Bradley MD, Beach MB, de Koning AP, Pratt TS, Osuna R (2007). "Effects of Fis on Escherichia coli gene expression during different growth stages." Microbiology 153(Pt 9);2922-40. PMID: 17768236

Hoerter05a: Hoerter JD, Arnold AA, Ward CS, Sauer M, Johnson S, Fleming T, Eisenstark A (2005). "Reduced hydroperoxidase (HPI and HPII) activity in the Deltafur mutant contributes to increased sensitivity to UVA radiation in Escherichia coli." J Photochem Photobiol B 79(2);151-7. PMID: 15878120

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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