View source for Catalase

{{Short description|Enzyme decomposing hydrogen peroxide}}
{{cs1 config |name-list-style=vanc |display-authors=6}}
{{Infobox protein family
| Name = Catalase
| Symbol = Catalase
| image = PDB 7cat EBI.jpg
| width =
| caption =
| Pfam= PF00199
| InterPro= IPR011614
| SMART=
| PROSITE = PDOC00395
| SCOP = 7cat
| TCDB =
| CDD = cd00328
| OPM family = 370
| OPM protein = 3e4w
| PDB =
}}
{{infobox enzyme
| Name       = Catalase
| EC_number  = 1.11.1.6
| CAS_number = 9001-05-2
| GO_code    = 0004096
| image      =
| width      = 
| caption    =  
}}
{{#invoke:Infobox_gene|getTemplateData|QID=Q14849060}}
'''Catalase''' is a common [[enzyme]] found in nearly all living organisms exposed to oxygen (such as [[bacteria]], plants, and animals) which [[catalyst|catalyzes]] the decomposition of [[hydrogen peroxide]] to [[water]] and [[oxygen]].<ref name="pmid14745498">{{cite journal | vauthors = Chelikani P, Fita I, Loewen PC | title = Diversity of structures and properties among catalases | journal = Cellular and Molecular Life Sciences | volume = 61 | issue = 2 | pages = 192–208 | date = January 2004 | pmid = 14745498 | doi = 10.1007/s00018-003-3206-5 | pmc = 11138816 | hdl-access = free | s2cid = 4411482 | hdl = 10261/111097 }}</ref> It is a very important enzyme in protecting the cell from [[oxidative stress|oxidative damage]] by [[reactive oxygen species]] (ROS). Catalase has one of the highest [[turnover number]]s of all enzymes; one catalase molecule can convert millions of hydrogen peroxide molecules to water and oxygen each second.<ref>{{cite web | title = Catalase | author = Goodsell DS | work = Molecule of the Month | publisher = RCSB Protein Data Bank | url = http://pdb101.rcsb.org/motm/57 | date = 2004-09-01 | access-date = 2016-08-23}}</ref>

Catalase is a [[Tetrameric protein|tetramer]] of four polypeptide chains, each over 500 [[amino acid]]s long.<ref name=Boon_a>{{cite web |vauthors=Boon EM, Downs A, Marcey D |title = Catalase: H<sub>2</sub>O<sub>2</sub>: H<sub>2</sub>O<sub>2</sub> Oxidoreductase | work = Catalase Structural Tutorial Text | url = http://biology.kenyon.edu/BMB/Chime/catalase/frames/cattx.htm | access-date = 2007-02-11}}</ref> It contains four iron-containing [[heme]] groups that allow the enzyme to react with hydrogen peroxide. The optimum [[pH]] for human catalase is approximately 7,<ref name="Maehly_1954">{{cite book | vauthors = Maehly AC, Chance B | chapter = The assay of catalases and peroxidases | volume = 1 | pages = 357–424 | year = 1954 | pmid = 13193536 | doi = 10.1002/9780470110171.ch14 | isbn = 978-0-470-11017-1 | title = Methods of Biochemical Analysis }}</ref> and has a fairly broad maximum: the rate of reaction does not change appreciably between pH 6.8 and 7.5.<ref name="pmid6727660">{{cite book | vauthors = Aebi H | title = Oxygen Radicals in Biological Systems | chapter = Catalase in vitro | volume = 105 | pages = [https://archive.org/details/oxygenradicalsin0000unse/page/121 121–6] | year = 1984 | pmid = 6727660 | doi = 10.1016/S0076-6879(84)05016-3 | isbn = 978-0-12-182005-3 | series = Methods in Enzymology | chapter-url = https://archive.org/details/oxygenradicalsin0000unse/page/121 }}</ref> The pH optimum for other catalases varies between 4 and 11 depending on the species.<ref name="urlEC 1.11.1.6 - catalase">{{cite web |title=EC 1.11.1.6 - catalase |url=http://www.brenda-enzymes.org/enzyme.php?ecno=1.11.1.6 |access-date=2009-05-26 |work=BRENDA: The Comprehensive Enzyme Information System |publisher=Department of Bioinformatics and Biochemistry, Technische Universität Braunschweig}}</ref> The optimum temperature also varies by species.<ref name=Bucknell>{{cite web | title = A Quantitative Enzyme Study; CATALASE |vauthors=Toner K, Sojka G, Ellis R | publisher = bucknell.edu | url = http://www.facstaff.bucknell.edu/toner/gb/lab121/labs34.html | access-date = 2007-02-11 |archive-url = https://web.archive.org/web/20000612104029/http://www.facstaff.bucknell.edu/toner/gb/lab121/labs34.html |archive-date = 2000-06-12}}</ref>

== Structure ==
Human catalase forms a [[tetramer]] composed of four [[Protein subunit|subunits]], each of which can be conceptually divided into four domains.<ref name = "Putnam_2000" >{{cite journal | vauthors = Putnam CD, Arvai AS, Bourne Y, Tainer JA | title = Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism | journal = Journal of Molecular Biology | volume = 296 | issue = 1 | pages = 295–309 | date = February 2000 | pmid = 10656833 | doi = 10.1006/jmbi.1999.3458 }}</ref> The extensive core of each subunit is generated by an eight-stranded antiparallel [[Beta barrel|β-barrel]] (β1-8), with nearest neighbor connectivity capped by β-barrel loops on one side and α9 loops on the other.<ref name = "Putnam_2000"  /> A [[Alpha helix|helical]] domain at one face of the β-barrel is composed of four C-terminal helices (α16, α17, α18, and α19) and four helices derived from residues between β4 and β5 (α4, α5, α6, and α7).<ref name = "Putnam_2000"  /> Alternative splicing may result in different protein variants.

== History ==
Catalase was first noticed in 1818 by [[Louis Jacques Thénard]], who discovered [[hydrogen peroxide]] (H<sub>2</sub>O<sub>2</sub>). Thénard suggested its breakdown was caused by an unknown substance. In 1900, [[Oscar Loew]] was the first to give it the name catalase, and found it in many plants and animals.<ref name="pmid17751716">{{cite journal | vauthors = Loew O | title = A New Enzyme of General Occurrence in Organisms | journal = Science | volume = 11 | issue = 279 | pages = 701–702 | date = May 1900 | pmid = 17751716 | doi = 10.1126/science.11.279.701 | bibcode = 1900Sci....11..701L | jstor = 1625707 | url = https://zenodo.org/record/1447826 }}</ref> In 1937 catalase from beef liver was crystallized by [[James B. Sumner]] and [[Alexander Dounce]]<ref name="pmid17776781">{{cite journal | vauthors = Sumner JB, Dounce AL | title = Crystalline Catalase | journal = Science | volume = 85 | issue = 2206 | pages = 366–367 | date = April 1937 | pmid = 17776781 | doi = 10.1126/science.85.2206.366 | bibcode = 1937Sci....85..366S }}</ref> and the molecular weight was measured in 1938.<ref name="pmid17831682">{{cite journal | vauthors = Sumner JB, Gralén N | title = The Molecular Weight of Crystalline Catalase | journal = Science | volume = 87 | issue = 2256 | page = 284 | date = March 1938 | pmid = 17831682 | doi = 10.1126/science.87.2256.284 | bibcode = 1938Sci....87..284S | s2cid = 36931581 }}</ref>

The [[amino acid]] sequence of [[bovine]] catalase was determined in 1969,<ref name="pmid4892021">{{cite journal | vauthors = Schroeder WA, Shelton JR, Shelton JB, Robberson B, Apell G | title = The amino acid sequence of bovine liver catalase: a preliminary report | journal = Archives of Biochemistry and Biophysics | volume = 131 | issue = 2 | pages = 653–655 | date = May 1969 | pmid = 4892021 | doi = 10.1016/0003-9861(69)90441-X }}</ref> and the three-dimensional structure in 1981.<ref name="pmid7328661">{{cite journal | vauthors = Murthy MR, Reid TJ, Sicignano A, Tanaka N, Rossmann MG | title = Structure of beef liver catalase | journal = Journal of Molecular Biology | volume = 152 | issue = 2 | pages = 465–499 | date = October 1981 | pmid = 7328661 | doi = 10.1016/0022-2836(81)90254-0 | bibcode = 1981JMBio.152..465M }}</ref>

== Function ==

=== Molecular mechanism ===
While the complete mechanism of catalase is not currently known,<ref name=Boon_b/> the [[chemical reaction|reaction]] is believed to occur in two stages:

: H<sub>2</sub>O<sub>2</sub> + Fe(III)-E → H<sub>2</sub>O + O=Fe(IV)-E(.+)

: H<sub>2</sub>O<sub>2</sub> + O=Fe(IV)-E(.+) → H<sub>2</sub>O + Fe(III)-E + O<sub>2</sub><ref name=Boon_b>{{cite web |vauthors=Boon EM, Downs A, Marcey D | title = Proposed Mechanism of Catalase | work = Catalase: H<sub>2</sub>O<sub>2</sub>: H<sub>2</sub>O<sub>2</sub> Oxidoreductase: Catalase Structural Tutorial | url = http://biology.kenyon.edu/BMB/Chime/catalase/frames/cattx.htm#Proposed%20Mechanism%20of%20Catalase | access-date = 2007-02-11}}</ref>

Here Fe()-E represents the [[iron]] center of the [[heme]] group attached to the enzyme. Fe(IV)-E(.+) is a mesomeric form of Fe(V)-E, meaning the iron is not completely oxidized to +V, but receives some stabilising electron density from the heme ligand, which is then shown as a radical cation (.+).

As hydrogen peroxide enters the [[active site]], it does interact with the [[amino acid]]s Asn148 ([[asparagine]] at position 148) and [[histidine|His75]], causing a [[proton]] (hydrogen [[ion]]) to transfer between the oxygen atoms. The free oxygen atom coordinates, freeing the newly formed water molecule and Fe(IV)=O. Fe(IV)=O reacts with a second hydrogen peroxide molecule to reform Fe(III)-E and produce water and oxygen.<ref name=Boon_b /> The reactivity of the iron center may be improved by the presence of the phenolate [[ligand]] of [[tyrosine|Tyr358]] in the fifth coordination position, which can assist in the [[oxidation]] of the Fe(III) to Fe(IV). The efficiency of the reaction may also be improved by the interactions of His75 and Asn148 with [[reaction intermediates]].<ref name=Boon_b /> The decomposition of hydrogen peroxide by catalase proceeds according to first-order kinetics, the rate being proportional to the hydrogen peroxide concentration.<ref>{{cite book | vauthors = Aebi H | title = Oxygen Radicals in Biological Systems | chapter = Catalase in vitro | series = Methods in Enzymology | volume = 105 | pages = 121–126 | date = 1984 | pmid = 6727660 | doi = 10.1016/S0076-6879(84)05016-3 | isbn = 978-0-12-182005-3 }}</ref>

Catalase can also catalyze the oxidation, by [[hydrogen peroxide]], of various metabolites and toxins, including [[formaldehyde]], [[formic acid]], [[phenols]], [[acetaldehyde]] and [[alcohols]]. It does so according to the following reaction:

: H<sub>2</sub>O<sub>2</sub> + H<sub>2</sub>R → 2H<sub>2</sub>O + R

The exact mechanism of this reaction is not known.

Any heavy metal ion (such as copper cations in [[copper(II) sulfate]]) can act as a [[noncompetitive inhibitor]] of catalase.  However, "Copper deficiency can lead to a reduction in catalase activity in tissues, such as heart and liver."<ref>{{cite journal | vauthors = Hordyjewska A, Popiołek Ł, Kocot J | title = The many "faces" of copper in medicine and treatment | journal = Biometals | volume = 27 | issue = 4 | pages = 611–621 | date = August 2014 | pmid = 24748564 | pmc = 4113679 | doi = 10.1007/s10534-014-9736-5 | bibcode = 2014BioMt..27..611H }}</ref> Furthermore, the poison [[cyanide]] is a noncompetitive inhibitor<ref>{{cite journal | vauthors = Kremer ML | title = Nonstationary inhibition of enzyme action. The cyanide inhibition of catalase. | journal = The Journal of Physical Chemistry | date = April 1981 | volume = 85 | issue = 7 | pages = 835–839 | doi = 10.1021/j150607a021 | bibcode = 1981JPhCh..85..835K }}</ref> of catalase at high concentrations of [[hydrogen peroxide]].<ref>{{cite journal | vauthors = Ogura Y, Yamazaki I | title = Steady-state kinetics of the catalase reaction in the presence of cyanide | journal = Journal of Biochemistry | volume = 94 | issue = 2 | pages = 403–408 | date = August 1983 | pmid = 6630165 | doi = 10.1093/oxfordjournals.jbchem.a134369 }}</ref>
[[Arsenate]] acts as an [[Enzyme activator|activator]].<ref>{{cite journal | vauthors = Kertulis-Tartar GM, Rathinasabapathi B, Ma LQ | title = Characterization of glutathione reductase and catalase in the fronds of two Pteris ferns upon arsenic exposure | journal = Plant Physiology and Biochemistry | volume = 47 | issue = 10 | pages = 960–965 | date = October 2009 | pmid = 19574057 | doi = 10.1016/j.plaphy.2009.05.009 | bibcode = 2009PlPB...47..960K }}</ref>  Three-dimensional [[protein structure]]s of the peroxidated catalase intermediates are available at the [[Protein Data Bank]].

=== Cellular role ===
Hydrogen peroxide is a harmful byproduct of many normal [[metabolism|metabolic]] processes; to prevent damage to cells and tissues, it must be quickly converted into other, less dangerous substances. To this end, catalase is frequently used by cells to rapidly catalyze the [[Chemical decomposition|decomposition]] of hydrogen peroxide into less-reactive [[gas]]eous [[oxygen]] and water molecules.<ref name=Gaetani_1996>{{cite journal | vauthors = Gaetani GF, Ferraris AM, Rolfo M, Mangerini R, Arena S, Kirkman HN | title = Predominant role of catalase in the disposal of hydrogen peroxide within human erythrocytes | journal = Blood | volume = 87 | issue = 4 | pages = 1595–1599 | date = February 1996 | pmid = 8608252 | doi = 10.1182/blood.V87.4.1595.bloodjournal8741595 | doi-access = free }}</ref>

Mice genetically engineered to lack catalase are initially phenotypically normal.<ref name=Ho_2004>{{cite journal | vauthors = Ho YS, Xiong Y, Ma W, Spector A, Ho DS | title = Mice lacking catalase develop normally but show differential sensitivity to oxidant tissue injury | journal = The Journal of Biological Chemistry | volume = 279 | issue = 31 | pages = 32804–32812 | date = July 2004 | pmid = 15178682 | doi = 10.1074/jbc.M404800200 | doi-access = free | bibcode = 2004JBiCh.27932804H }}</ref> However, catalase deficiency in mice may increase the likelihood of developing [[obesity]], fatty liver,<ref name="pmid27939935">{{cite journal | vauthors = Heit C, Marshall S, Singh S, Yu X, Charkoftaki G, Zhao H, Orlicky DJ, Fritz KS, Thompson DC, Vasiliou V | title = Catalase deletion promotes prediabetic phenotype in mice | journal = Free Radical Biology & Medicine | volume = 103 | pages = 48–56 | date = February 2017 | pmid = 27939935 | pmc = 5513671 | doi = 10.1016/j.freeradbiomed.2016.12.011 }}</ref> and [[Diabetes mellitus type 2|type 2 diabetes]].<ref name="Góth_2012">{{cite journal | vauthors = Góth L, Nagy T | title = Acatalasemia and diabetes mellitus | journal = Archives of Biochemistry and Biophysics | volume = 525 | issue = 2 | pages = 195–200 | date = September 2012 | pmid = 22365890 | doi = 10.1016/j.abb.2012.02.005 }}</ref> Some humans have very low levels of catalase ([[acatalasia]]), yet show few ill effects.

The increased [[oxidative stress]] that occurs with [[ageing|aging]] in mice is alleviated by [[gene expression|over-expression]] of catalase.<ref name="pmid27575890">{{cite journal | vauthors = Selvaratnam J, Robaire B | title = Overexpression of catalase in mice reduces age-related oxidative stress and maintains sperm production | journal = Experimental Gerontology | volume = 84 | pages = 12–20 | date = November 2016 | pmid = 27575890 | doi = 10.1016/j.exger.2016.08.012 | s2cid = 2416413 }}</ref>  Over-expressing mice do not exhibit the age-associated loss of [[spermatozoon|spermatozoa]], [[testicle|testicular]] [[germ cell|germ]] and [[Sertoli cell]]s seen in wild-type mice.  Oxidative stress in [[wild-type]] mice ordinarily induces oxidative [[DNA damage (naturally occurring)|DNA damage]] (measured as [[8-Oxo-2'-deoxyguanosine|8-oxodG]]) in [[sperm]] with aging, but these damages are significantly reduced in aged catalase over-expressing mice.<ref name="pmid27575890" />   Furthermore, these over-expressing mice show no decrease in age-dependent number of pups per litter.  Overexpression of catalase targeted to mitochondria extends the lifespan of mice.<ref name="pmid15879174">{{cite journal | vauthors = Schriner SE, Linford NJ, Martin GM, Treuting P, Ogburn CE, Emond M, Coskun PE, Ladiges W, Wolf N, Van Remmen H, Wallace DC, Rabinovitch PS | title = Extension of murine life span by overexpression of catalase targeted to mitochondria | journal = Science | volume = 308 | issue = 5730 | pages = 1909–1911 | date = June 2005 | pmid = 15879174 | doi = 10.1126/science.1106653 | s2cid = 38568666 | bibcode = 2005Sci...308.1909S }}</ref>

In [[eukaryote]]s, catalase is usually located in a cellular [[organelle]] called the [[peroxisome]].<ref name="MBOC">{{cite book |vauthors=Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P | title = Molecular Biology of the Cell | edition = 4th | publisher = Garland Science | location = New York | year = 2002 | chapter = Peroxisomes | chapter-url = https://www.ncbi.nlm.nih.gov/books/NBK26858/ | isbn = 978-0-8153-3218-3 }}</ref> Peroxisomes in plant cells are involved in [[photorespiration]] (the use of oxygen and production of carbon dioxide) and symbiotic [[nitrogen fixation]] (the breaking apart of [[diatomic]] [[nitrogen]] (N<sub>2</sub>) to reactive nitrogen atoms). Hydrogen peroxide is used as a potent antimicrobial agent when cells are infected with a pathogen. Catalase-positive pathogens, such as ''[[Mycobacterium tuberculosis]]'', ''[[Legionella pneumophila]]'', and ''[[Campylobacter jejuni]]'', make catalase to deactivate the peroxide radicals, thus allowing them to survive unharmed within the [[Host (biology)|host]].<ref name="pmid12949187">{{cite journal | vauthors = Srinivasa Rao PS, Yamada Y, Leung KY | title = A major catalase (KatB) that is required for resistance to H2O2 and phagocyte-mediated killing in Edwardsiella tarda | journal = Microbiology | volume = 149 | issue = Pt 9 | pages = 2635–2644 | date = September 2003 | pmid = 12949187 | doi = 10.1099/mic.0.26478-0 | doi-access = free }}</ref>

Like [[alcohol dehydrogenase]], catalase converts ethanol to acetaldehyde, and drop-out studies in rodents suggest that it may be responsible for the majority of this reaction in the brain.<ref name="lieb97">{{cite journal | vauthors = Lieber CS | title = Ethanol metabolism, cirrhosis and alcoholism | journal = Clinica Chimica Acta; International Journal of Clinical Chemistry | volume = 257 | issue = 1 | pages = 59–84 | date = January 1997 | pmid = 9028626 | doi = 10.1016/S0009-8981(96)06434-0 | bibcode = 1997ClChA.257...59L }}</ref><ref name="zimatkin06">{{cite journal | last1=Zimatikin |first1=Sergy |last2=Pronko |first2=Sergy |last3=Vasilou |first3=Vasilis |last4=Gonzalez |first4=Frank |last5=Richard |first5=Dietrich |title=Enzymatic Mechanisms of Ethanol Oxidation in the Brain |journal=Alcoholism Clinical & Experimental Research |volume=30 |issue=9 |pages=1500–1505 |date= August 2006 |doi=10.1111/j.1530-0277.2006.00181.x |pmid=16930212 }}</ref>

== Distribution among organisms ==
The large majority of known organisms use catalase in every [[organ (anatomy)|organ]], with particularly high concentrations occurring in the [[liver]] in mammals.<ref>{{cite journal| vauthors = Ilyukha VA | journal=Journal of Evolutionary Biochemistry and Physiology | title = Superoxide Dismutase and Catalase in the Organs of Mammals of Different Ecogenesis |date=2001|volume=37|issue=3|pages=241–245|doi=10.1023/A:1012663105999| s2cid=38916410 }}</ref> Catalase is found primarily in [[peroxisome]]s and the [[cytosol]] of [[erythrocyte]]s (and sometimes in [[mitochondria]]<ref name="pmid11351128">{{cite journal | vauthors = Bai J, Cederbaum AI | title = Mitochondrial catalase and oxidative injury | journal = Biological Signals and Receptors | volume = 10 | issue = 3–4 | pages = 189–199 | year = 2001 | pmid = 11351128 | doi = 10.1159/000046887 | s2cid = 33795198 }}</ref>)

Almost all [[aerobic microorganisms]] use catalase. It is also present in some [[Anaerobic organism|anaerobic]] [[microorganisms]], such as ''[[Methanosarcina barkeri]]''.<ref name="pmid16735730">{{cite journal | vauthors = Brioukhanov AL, Netrusov AI, Eggen RI | title = The catalase and superoxide dismutase genes are transcriptionally up-regulated upon oxidative stress in the strictly anaerobic archaeon Methanosarcina barkeri | journal = Microbiology | volume = 152 | issue = Pt 6 | pages = 1671–1677 | date = June 2006 | pmid = 16735730 | doi = 10.1099/mic.0.28542-0 | doi-access = free }}</ref> Catalase is also universal among [[plants]] and occurs in most [[fungi]].<ref>{{cite journal | vauthors = Hansberg W, Salas-Lizana R, Domínguez L | title = Fungal catalases: function, phylogenetic origin and structure | journal = Archives of Biochemistry and Biophysics | volume = 525 | issue = 2 | pages = 170–180 | date = September 2012 | pmid = 22698962 | doi = 10.1016/j.abb.2012.05.014 }}</ref>

One unique use of catalase occurs in the [[bombardier beetle]]. This beetle has two sets of liquids that are stored separately in two paired glands. The larger of the pair, the storage chamber or reservoir, contains [[hydroquinone]]s and hydrogen peroxide, while the smaller, the reaction chamber, contains catalases and [[peroxidase]]s. To activate the noxious spray, the beetle mixes the contents of the two compartments, causing oxygen to be liberated from hydrogen peroxide. The oxygen oxidizes the hydroquinones and also acts as the propellant.<ref name="pmid10449758">{{cite journal | vauthors = Eisner T, Aneshansley DJ | title = Spray aiming in the bombardier beetle: photographic evidence | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 96 | issue = 17 | pages = 9705–9709 | date = August 1999 | pmid = 10449758 | pmc = 22274 | doi = 10.1073/pnas.96.17.9705 | bibcode = 1999PNAS...96.9705E | doi-access = free }}</ref> The oxidation reaction is very [[exothermic]] (ΔH = −202.8 kJ/mol) and rapidly heats the mixture to the boiling point.<ref name="Beheshti_2006">{{cite journal|vauthors=Beheshti N, McIntosh AC|year=2006|title=A biomimetic study of the explosive discharge of the bombardier beetle|url=http://www.heveliusforum.org/Artykuly/Biomimetics.pdf|journal=International Journal of Design & Nature|volume=1|issue=1|pages=1–9|archive-url=https://web.archive.org/web/20110726145856/http://www.heveliusforum.org/Artykuly/Biomimetics.pdf|archive-date=2011-07-26}}</ref>

Long-lived queens of the [[termite]] ''[[Reticulitermes]] speratus'' have significantly lower [[DNA oxidation|oxidative damage to their DNA]] than non-reproductive individuals (workers and soldiers).<ref name="pmid28076409">{{cite journal | vauthors = Tasaki E, Kobayashi K, Matsuura K, Iuchi Y | title = An Efficient Antioxidant System in a Long-Lived Termite Queen | journal = PLOS ONE | volume = 12 | issue = 1 | article-number = e0167412 | date = 2017 | pmid = 28076409 | pmc = 5226355 | doi = 10.1371/journal.pone.0167412 | doi-access = free | bibcode = 2017PLoSO..1267412T }}</ref>  Queens have more than two times higher catalase activity and seven times higher expression levels of the catalase gene RsCAT1 than workers.<ref name="pmid28076409" />  It appears that the efficient [[antioxidant]] capability of termite queens can partly explain how they attain longer life.

Catalase enzymes from various species have vastly differing optimum temperatures. [[Poikilotherm]]ic animals typically have catalases with optimum temperatures in the range of {{convert|15|-|25|C}}, while mammalian or avian catalases might have optimum temperatures above {{convert|35|C}},<ref name="mits56" /><ref name="imm03">{{cite journal| vauthors = Çetinus ŞA, Öztop HN |title=Immobilization of catalase into chemically crosslinked chitosan beads|journal=Enzyme and Microbial Technology|date=June 2003|volume=32|issue=7|pages=889–894|doi=10.1016/S0141-0229(03)00065-6}}</ref> and catalases from plants vary depending on their [[growth habit]].<ref name="mits56">{{cite journal| vauthors = Mitsuda H |title=Studies on Catalase|journal=Bulletin of the Institute for Chemical Research, Kyoto University|date=1956-07-31|volume=34|issue=4|pages=165–192|url=https://repository.kulib.kyoto-u.ac.jp/dspace/bitstream/2433/75561/1/chd034_4_165.pdf |archive-url=https://ghostarchive.org/archive/20221009/https://repository.kulib.kyoto-u.ac.jp/dspace/bitstream/2433/75561/1/chd034_4_165.pdf |archive-date=2022-10-09 |url-status=live|access-date=27 September 2017}}</ref> In contrast, catalase isolated from the [[hyperthermophile]] [[archaeon]] ''[[Pyrobaculum calidifontis]]'' has a temperature optimum of {{convert|90|C}}.<ref name="pmid12029047">{{cite journal | vauthors = Amo T, Atomi H, Imanaka T | title = Unique presence of a manganese catalase in a hyperthermophilic archaeon, Pyrobaculum calidifontis VA1 | journal = Journal of Bacteriology | volume = 184 | issue = 12 | pages = 3305–3312 | date = June 2002 | pmid = 12029047 | pmc = 135111 | doi = 10.1128/JB.184.12.3305-3312.2002 }}</ref>

== Clinical significance and application ==
[[Image:Wasserstoffperoxid.svg|left|thumb|Hydrogen peroxide]]
Catalase is used in the food industry for removing [[hydrogen peroxide]] from [[milk]] prior to [[cheese]] production.<ref name="urlCatalase - Worthington Enzyme Manual">{{cite web | url = http://www.worthington-biochem.com/CTL/default.html | title = Catalase | work = Worthington Enzyme Manual | publisher = Worthington Biochemical Corporation | access-date = 2009-03-01}}</ref> Another use is in food wrappers, where it prevents food from [[oxidation|oxidizing]].<ref name="urlRe: how is catalase used in industry?">{{cite web | url = http://madsci.org/posts/archives/mar99/921636249.Gb.r.html | title = Re: how is catalase used in industry? | author = Hengge A | date = 1999-03-16 | work = General Biology | publisher = MadSci Network | access-date = 2009-03-01 | archive-date = 2019-09-07 | archive-url = https://web.archive.org/web/20190907080521/http://madsci.org/posts/archives/mar99/921636249.Gb.r.html }}</ref> Catalase is also used in the [[textile]] industry, removing hydrogen peroxide from fabrics to make sure the material is peroxide-free.<ref name="urltextile industry">{{cite web | url = http://www.p2pays.org/ref/11/10842.htm | title = textile industry | work = Case study 228 | publisher = International Cleaner Production Information Clearinghouse | access-date = 2009-03-01 | archive-url = https://web.archive.org/web/20081104083335/http://www.p2pays.org/ref/11/10842.htm | archive-date = 2008-11-04 }}</ref>

A minor use is in [[contact lens]] hygiene – a few lens-cleaning products [[disinfection|disinfect]] the lens using a hydrogen peroxide solution; a solution containing catalase is then used to decompose the hydrogen peroxide before the lens is used again.<ref>{{US patent reference | number = 5521091 | y = 1996 | m = 05 | d = 28 | inventor = Cook JN, Worsley JL | title = Compositions and method for destroying hydrogen peroxide on contact lens }}</ref>

=== Bacterial identification (catalase test) ===
[[Image:Catalase reaction.jpg|300px|thumb|Positive catalase reaction]]
The catalase test is one of the three main tests used by microbiologists to identify species of bacteria. If the bacteria possess catalase (i.e., are catalase-positive), bubbles of oxygen are observed when a small amount of bacterial [[Isolation (microbiology)|isolate]] is added to hydrogen peroxide. The catalase test is done by placing a drop of hydrogen peroxide on a [[microscope slide]]. An applicator stick is touched to the colony, and the tip is then smeared onto the hydrogen peroxide drop.
* If the mixture produces bubbles or froth, the organism is said to be 'catalase-positive'. [[Staphylococcus|Staphylococci]]<ref name="urlBSCI 424 Pathogenic Microbiology -- Bacterial Pathogen List">{{cite web | url = http://www.life.umd.edu/classroom/bsci424/pathogendescriptions/PathogenList.htm | title = Bacterial Pathogen List | author = Rollins DM | date = 2000-08-01 | work = BSCI 424 Pathogenic Microbiology | publisher = University of Maryland | access-date = 2009-03-01}}</ref> and [[Micrococcus|Micrococci]]<ref name="urlBiochemical Tests">{{cite web | url = http://www.mc.maricopa.edu/~johnson/labtools/Dbiochem/cat.html | title = Catalase Production | author = Johnson M | work = Biochemical Tests | publisher = Mesa Community College | access-date = 2009-03-01 | archive-url = https://web.archive.org/web/20081211073437/http://www.mc.maricopa.edu/~johnson/labtools/Dbiochem/cat.html | archive-date = 2008-12-11 }}</ref> are catalase-positive. Other catalase-positive organisms include ''[[Listeria]], [[Corynebacterium diphtheriae]], [[Burkholderia cepacia]], [[Nocardia]]'', the family [[Enterobacteriaceae]] (''[[Citrobacter]], [[Escherichia coli|E. coli]], [[Enterobacter]], [[Klebsiella]], [[Shigella]], [[Yersinia]], [[Proteus (bacterium)|Proteus]], [[Salmonella]], [[Serratia]]''), ''[[Pseudomonas]]'', ''[[Mycobacterium tuberculosis]], [[Aspergillus]]'', [[Cryptococcus (fungus)|''Cryptococcus'']], and ''[[Rhodococcus equi]]''.
* If not, the organism is 'catalase-negative'. ''[[Streptococcus]]''<ref name="urlStreptococcus pneumoniae and Staphylococci">{{cite web | url = http://pathmicro.med.sc.edu/fox/strep-staph.htm | title = Streptococcus pneumoniae and Staphylococci | author = Fox A | publisher = University of South Carolina | access-date = 2009-03-01}}</ref> and ''[[Enterococcus]]'' spp. are catalase-negative.

While the catalase test alone cannot identify a particular organism, it can aid identification when combined with other tests such as antibiotic resistance. The presence of catalase in bacterial cells depends on both the growth condition and the medium used to grow the cells.

[[Capillary tube]]s may also be used. A small sample of bacteria is collected on the end of the capillary tube, without blocking the tube, to avoid [[false negative]] results. The opposite end is then dipped into hydrogen peroxide, which is drawn into the tube through [[capillary action]], and turned upside down, so that the bacterial sample points downwards. The hand holding the tube is then tapped on the bench, moving the hydrogen peroxide down until it touches the bacteria. If bubbles form on contact, this indicates a positive catalase result. This test can detect catalase-positive bacteria at concentrations above about 10<sup>5</sup> cells/mL,<ref>{{Cite book|url=https://books.google.com/books?id=_orkBwAAQBAJ&pg=PA35|title=Fisheries Processing: Biotechnological applications| vauthors = Martin AM |date=2012-12-06|publisher=Springer Science & Business Media|isbn=978-1-4615-5303-8|language=en}}</ref> and is simple to use.

=== Bacterial virulence ===
[[Neutrophil]]s and other [[phagocyte]]s use peroxide to kill bacteria. The enzyme [[NADPH oxidase]] generates [[superoxide]] within the [[phagosome]], which is converted via hydrogen peroxide to other oxidising substances like [[hypochlorous acid]] which kill [[phagocytosed]] pathogens.<ref>{{cite journal | vauthors = Winterbourn CC, Kettle AJ, Hampton MB | title = Reactive Oxygen Species and Neutrophil Function | journal = Annual Review of Biochemistry | volume = 85 | issue = 1 | pages = 765–792 | date = June 2016 | pmid = 27050287 | doi = 10.1146/annurev-biochem-060815-014442 | bibcode = 2016ARBio..85..765W }}</ref> In individuals with [[chronic granulomatous disease]] (CGD), phagocytic peroxide production is impaired due to a defective NADPH oxidase system. Normal cellular metabolism will still produce a small amount of peroxide and this peroxide can be used to produce hypochlorous acid to eradicate the bacterial infection. However, if individuals with CGD are infected with catalase-positive bacteria, the bacterial catalase can destroy the excess peroxide before it can be used to produce other oxidising substances. In these individuals the pathogen survives and becomes a chronic infection. This chronic infection is typically surrounded by macrophages in an attempt to isolate the infection. This wall of macrophages surrounding a pathogen is called a [[granuloma]]. Many bacteria are catalase positive, but some are better catalase-producers than others. Some catalase-positive bacteria and fungi include: ''[[Nocardia]], [[Pseudomonas]], [[Listeria]], [[Aspergillus]], [[Candida albicans|Candida]], [[Escherichia coli|E. coli]], [[Staphylococcus]], [[Serratia]], [[Burkholderia cepacia complex|B. cepacia]]'' and ''[[Helicobacter pylori|H. pylori]]''.<ref>{{Cite book|title=First aid for the USMLE step 1 2017: a student-to-student guide |isbn=978-1-259-83762-3 |edition=27th |location=New York |publisher=McGraw-Hill Education |oclc=986222844| vauthors = Le T, Bhushan V, Sochat M, Kallianos K, Chavda Y, Zureick AH |date = 2017-01-06}}</ref>

=== Acatalasia ===
[[Acatalasia]] is a condition caused by homozygous mutations in CAT, resulting in a lack of catalase. Symptoms are mild and include oral ulcers. A heterozygous CAT mutation results in lower, but still present catalase.<ref>{{cite web |title=OMIM Entry - # 614097 - ACATALASEMIA |url=http://www.omim.org/entry/614097 |website=www.omim.org |language=en-us}}</ref>

=== Gray hair ===
Low levels of catalase may play a role in the [[Human hair color#Gray and white hair|graying]] process of human hair. Hydrogen peroxide is naturally produced by the body and broken down by catalase. Hydrogen peroxide can accumulate in hair follicles and if catalase levels decline, this buildup can cause oxidative stress and graying.<ref>{{Cite web |title=Gray hair cure? Scientists find root cause of discoloration |url=http://www.nbcnews.com/healthmain/gray-hair-cure-scientists-find-root-cause-discoloration-6C9802771 |access-date=2022-07-31 |website=NBC News |date=6 May 2013 |language=en}}</ref> These low levels of catalase are associated with old age. Hydrogen peroxide interferes with the production of [[melanin]], the pigment that gives hair its color.<ref name="ScienceDaily_Grey_Hair">{{cite web | url = https://www.sciencedaily.com/releases/2009/02/090223131123.htm | title = Why Hair Turns Gray Is No Longer A Gray Area: Our Hair Bleaches Itself As We Grow Older | date = 2009-02-24 | work = Science News | publisher = ScienceDaily | access-date = 2009-03-01}}</ref><ref name="pmid19237503">{{cite journal | vauthors = Wood JM, Decker H, Hartmann H, Chavan B, Rokos H, Spencer JD, Hasse S, Thornton MJ, Shalbaf M, Paus R, Schallreuter KU | title = Senile hair graying: H2O2-mediated oxidative stress affects human hair color by blunting methionine sulfoxide repair | journal = FASEB Journal | volume = 23 | issue = 7 | pages = 2065–2075 | date = July 2009 | pmid = 19237503 | doi = 10.1096/fj.08-125435 | doi-access = free | arxiv = 0706.4406 | s2cid = 16069417 }}</ref>

== Interactions ==
Catalase has been shown to [[protein–protein interaction|interact]] with the ''[[ABL2]]''<ref name="pmid12777400">{{cite journal | vauthors = Cao C, Leng Y, Kufe D | title = Catalase activity is regulated by c-Abl and Arg in the oxidative stress response | journal = The Journal of Biological Chemistry | volume = 278 | issue = 32 | pages = 29667–29675 | date = August 2003 | pmid = 12777400 | doi = 10.1074/jbc.M301292200 | doi-access = free }}</ref> and ''[[Abl gene|Abl]]'' genes.<ref name=pmid12777400/>  Infection with the [[murine leukemia virus]] causes catalase activity to decline in the lungs, heart and kidneys of mice.  Conversely, dietary fish oil increased catalase activity in the heart, and kidneys of mice.<ref>{{cite journal |doi=10.1016/S0271-5317(00)00214-1 |title=Effects of dietary fish oil on tissue glutathione and antioxidant defense enzymes in mice with murine aids |journal=Nutrition Research |volume=20 |issue=9 |pages=1287–99 |year=2000 | vauthors = Xi S, Chen LH }}</ref>

== Methods for determining catalase activity ==
In 1870, Schoenn discovered a formation of yellow color from the interaction of hydrogen peroxide with molybdate;<ref>{{Cite journal| vauthors = Isaacs ML |date=1922|title=A colorimetric determination of hydrogen peroxide|url=https://pubs.acs.org/doi/pdf/10.1021/ja01429a006|journal=Journal of the American Chemical Society|language=|volume=44|issue=8|pages=1662–1663|doi=10.1021/ja01429a006|bibcode=1922JAChS..44.1662I |s2cid= |issn=}}</ref> then, from the middle of the 20th century, this reaction began to be used for colorimetric determination of unreacted hydrogen peroxide in the catalase activity assay.<ref>{{Cite journal| vauthors = Peizer LR, Widelock D |date=1955|title=A colorimetric test for measuring catalase activity of cultures of M. tuberculosis|url=https://www.atsjournals.org/doi/abs/10.1164/artpd.1955.71.2.305 |journal= American Review of Tuberculosis|language=|volume=71|issue=2|pages=305–313|doi=10.1164/artpd.1955.71.2.305|doi-broken-date=10 May 2026 |pmid=14350192 |s2cid= |issn=}}</ref> The reaction became widely used after publications by Korolyuk et al. (1988)<ref>{{cite journal | vauthors = Koroliuk MA, Ivanova LI, Maĭorova IG, Tokarev VE | title = [A method of determining catalase activity] | journal = Laboratornoe Delo | issue = 1 | pages = 16–19 | date = 1988 | pmid = 2451064 }}</ref> and Goth (1991).<ref name="pmid2029780">{{cite journal | vauthors = Góth L | title = A simple method for determination of serum catalase activity and revision of reference range | journal = Clinica Chimica Acta; International Journal of Clinical Chemistry | volume = 196 | issue = 2–3 | pages = 143–151 | date = February 1991 | pmid = 2029780 | doi = 10.1016/0009-8981(91)90067-m | bibcode = 1991ClChA.196..143G | hdl = 2437/123655 }}</ref> The first paper describes serum catalase assay with no buffer in the reaction medium; the latter describes the procedure based on phosphate buffer as a reaction medium. Since phosphate ion reacts with ammonium molybdate,<ref name="pmid2029780" /> the use of MOPS buffer as a reaction medium is more appropriate.<ref>{{cite journal | vauthors = Razygraev AV | title = Catalase enzymatic activity in adult mosquitoes (Diptera: Culicidae): taxonomic distribution of the continuous trait suggests its relevance for phylogeny research |url=https://www.mapress.com/zt/article/view/zootaxa.5339.2.3 | journal = Zootaxa | volume = 5339 | issue = 2 | pages = 159–176 | date = 2023 | pmid = 38221060| doi = 10.11646/zootaxa.5339.2.3 | s2cid = 261383164 }}</ref>

Direct UV measurement of the decrease in the concentration of hydrogen peroxide is also widely used after the publications by Beers & Sizer<ref>{{cite journal | vauthors = Beers RF, Sizer IW | title = A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase | journal = The Journal of Biological Chemistry | volume = 195 | issue = 1 | pages = 133–140 | date = March 1952 | doi = 10.1016/S0021-9258(19)50881-X | pmid = 14938361 | doi-access = free }}</ref> and Aebi.<ref>{{cite book | vauthors = Aebi H | chapter = Catalase in vitro |title=Oxygen Radicals in Biological Systems | series = Methods in Enzymology | volume = 105 | pages = 121–126 | date = January 1984 | pmid = 6727660 | doi = 10.1016/s0076-6879(84)05016-3 | publisher = Academic Press | isbn = 978-0-12-182005-3 }}</ref>

== See also ==
* [[Enzyme kinetics]]
* [[Glutathione peroxidase]]
* [[Peroxidase]]
* [[Superoxide dismutase]]

== References ==
{{Reflist|35em}}

== External links ==
* {{cite web | url = http://genomics.senescence.info/genes/entry.php?hugo=CAT | title = GenAge entry for CAT (Homo sapiens) | publisher = Human Ageing Genomic Resources | access-date = 2009-03-05}}
* {{cite web | url = http://madsci.org/FAQs/catalase.html | title = Catalase | work = MadSci FAQ | publisher = madsci.org | access-date = 2009-03-05 | archive-date = 2009-03-09 | archive-url = https://web.archive.org/web/20090309011654/http://www.madsci.org/FAQs/catalase.html }}
* {{cite web | url = http://www.tgw1916.net/video_pages/catalase.html | title = Catalase and oxidase test video | publisher = Regnvm Prokaryotae | access-date = 2009-03-05}}
* {{cite web | url = http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 | title = EC 1.11.1.6 - catalase | publisher = Brenda: The Comprehensive Enzyme Information System| access-date = 2009-03-05}}
* {{cite web|url=http://peroxibase.isb-sib.ch/ |title=PeroxiBase - The peroxidase database |publisher=[[Swiss Institute of Bioinformatics]] |access-date=2009-03-05 |archive-url=https://web.archive.org/web/20081013084336/http://peroxibase.isb-sib.ch/ |archive-date=2008-10-13 }}
* {{cite web | url = http://microbeid.com/Methods/catalase.html | title = Catalase Procedure | publisher = MicrobeID.com | access-date = 2009-04-22}}
* {{cite web | url = http://www.rcsb.org/pdb/101/motm.do?momID=57.html | title = Catalase Molecule of the Month | publisher = Protein Data Bank | access-date = 2013-01-08 | archive-url = https://web.archive.org/web/20130511202517/http://www.rcsb.org/pdb/101/motm.do?momID=57.html | archive-date = 2013-05-11 }}
* {{PDBe-KB2|P04040|Catalase}}
 
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