|Gene:||katE||Accession Numbers: EG10509 (EcoCyc), b1732, ECK1730|
Synonyms: catalase HPII, HPII, hydroperoxidase II, HPIII
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].
Gene Citations: [vonOssowski91]
|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]
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
|Biological Process:||GO:0006972 - hyperosmotic response
GO:0006974 - cellular response to DNA damage stimulus [Khil02]
GO:0006979 - response to oxidative stress [GOA01, Loewen84a]
GO:0042744 - hydrogen peroxide catabolic process [UniProtGOA11, Loewen84a]
GO:0055114 - oxidation-reduction process [UniProtGOA11, GOA01]
|Molecular Function:||GO:0004096 - catalase activity
[Li07b, GOA01a, GOA01, Loewen86, Loewen84a]
GO:0005506 - iron ion binding [Bravo95]
GO:0020037 - heme binding [GOA01, Bravo95]
GO:0042802 - identical protein binding [Rajagopala14, Lasserre06, Bravo95]
GO:0004601 - peroxidase activity [UniProtGOA11]
GO:0016491 - oxidoreductase activity [UniProtGOA11]
GO:0046872 - metal ion binding [UniProtGOA11]
|Cellular Component:||GO:0005737 - cytoplasm
[UniProtGOA11a, UniProtGOA11, Heimberger88]
GO:0005829 - cytosol [DiazMejia09, Lasserre06]
|MultiFun Terms:||cell processes → protection → detoxification|
|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]
Enzymatic reaction of: catalase
Synonyms: hydroperoxidase, hydrogen peroxide:hydrogen peroxide oxidoreductase
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].
Cofactor Binding Comment: contains one cis-heme d isomer per subunit [Loewen93]
pH(opt): 4-11 [Loewen86]
Enzymatic reaction of: heme d synthase (catalase II)
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.
10/20/97 Gene b1732 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10509; confirmed by SwissProt match.
Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554
Bravo97: Bravo J, Fita I, Ferrer JC, Ens W, Hillar A, Switala J, Loewen PC (1997). "Identification of a novel bond between a histidine and the essential tyrosine in catalase HPII of Escherichia coli." Protein Sci 6(5);1016-23. PMID: 9144772
Chelikani03a: Chelikani P, Donald LJ, Duckworth HW, Loewen PC (2003). "Hydroperoxidase II of Escherichia coli exhibits enhanced resistance to proteolytic cleavage compared to other catalases." Biochemistry 42(19);5729-35. PMID: 12741830
Chelikani05: Chelikani P, Carpena X, Perez-Luque R, Donald LJ, Duckworth HW, Switala J, Fita I, Loewen PC (2005). "Characterization of a large subunit catalase truncated by proteolytic cleavage." Biochemistry 44(15);5597-605. PMID: 15823018
Dawson91: Dawson JH, Bracete AM, Huff AM, Kadkhodayan S, Zeitler CM, Sono M, Chang CK, Loewen PC (1991). "The active site structure of E. coli HPII catalase. Evidence favoring coordination of a tyrosinate proximal ligand to the chlorin iron." FEBS Lett 295(1-3);123-6. PMID: 1662642
DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114
Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909
Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938
Greenberg88: Greenberg JT, Demple B (1988). "Overproduction of peroxide-scavenging enzymes in Escherichia coli suppresses spontaneous mutagenesis and sensitivity to redox-cycling agents in oxyR-mutants." EMBO J 7(8);2611-7. PMID: 2847922
Hoerter05a: Hoerter JD, Arnold AA, Kuczynska DA, Shibuya A, Ward CS, Sauer MG, Gizachew A, Hotchkiss TM, Fleming TJ, Johnson S (2005). "Effects of sublethal UVA irradiation on activity levels of oxidative defense enzymes and protein oxidation in Escherichia coli." J Photochem Photobiol B 81(3);171-80. PMID: 16183297
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
Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394
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
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
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
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
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
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
Nies84: Nies D, Schlegel HG (1984). "Use of catalase from Escherichia coli in model experiments for oxygen supply of microorganisms with hydrogen peroxide." Biotechnol Bioeng 26(7);737-41. PMID: 18553439
Obinger97: Obinger C, Maj M, Nicholls P, Loewen P (1997). "Activity, peroxide compound formation, and heme d synthesis in Escherichia coli HPII catalase." Arch Biochem Biophys 342(1);58-67. PMID: 9185614
Park05: Park S, You X, Imlay JA (2005). "Substantial DNA damage from submicromolar intracellular hydrogen peroxide detected in Hpx- mutants of Escherichia coli." Proc Natl Acad Sci U S A 102(26);9317-22. PMID: 15967999
Park07a: Park C, Zhou S, Gilmore J, Marqusee S (2007). "Energetics-based protein profiling on a proteomic scale: identification of proteins resistant to proteolysis." J Mol Biol 368(5);1426-37. PMID: 17400245
Peng92: Peng Q, Timkovich R, Loewen PC, Peterson J (1992). "Identification of heme macrocycle type by near-infrared magnetic circular dichroism spectroscopy at cryogenic temperatures." FEBS Lett 309(2);157-60. PMID: 1324193
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
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
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
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
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
Hoerter05: 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
Tanaka93: Tanaka K, Takayanagi Y, Fujita N, Ishihama A, Takahashi H (1993). "Heterogeneity of the principal sigma factor in Escherichia coli: the rpoS gene product, sigma 38, is a second principal sigma factor of RNA polymerase in stationary-phase Escherichia coli." Proc Natl Acad Sci U S A 90(8);3511-5. PMID: 8475100
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