Catalase is a common enzyme found in nearly all living organisms exposed to oxygen. It catalyzes the decomposition of hydrogen peroxide to water and oxygen.[1] It is a very important enzyme in reproductive reactions. Likewise, catalase has one of the highest turnover numbers of all enzymes; one catalase molecule can convert millions of molecules of hydrogen peroxide to water and oxygen each second.[2]
Catalase is a tetramer of four polypeptide chains, each over 500 amino acids long.[3] It contains four porphyrin heme (iron) groups that allow the enzyme to react with the hydrogen peroxide. The optimum pH for human catalase is approximately 7,[4] and has a fairly broad maximum (the rate of reaction does not change appreciably at pHs between 6.8 and 7.5).[5] The pH optimum for other catalases varies between 4 and 11 depending on the species.[6] The optimum temperature also varies by species.[7]
Catalase was first noticed in 1818 when Louis Jacques Thénard, who discovered H2O2 (hydrogen peroxide), suggested that peroxide's breakdown is caused by an unknown substance. In 1900, Oscar Loew was the first to give it the name catalase, and found its presence in many plants and animals.[8] In 1937 catalase from beef liver was crystallised by James B. Sumner[9] and the molecular weight was worked out in 1938.[10]
In 1969, the amino acid sequence of bovine catalase was worked out.[11] Then in 1981, the 3D structure of the protein was revealed.[12]
The reaction of catalase in the decomposition of hydrogen peroxide is:
- 2 H2O2 → 2 H2O + O2
The presence of catalase in a microbial or tissue sample can be tested by adding a volume of hydrogen peroxide and observing the reaction. The formation of bubbles, oxygen, indicates a positive result. This easy assay, which can be seen with the naked eye, without the aid of instruments, is possible because catalase has a very high specific activity, which produces a detectable response.
While the complete mechanism of catalase is not currently known,[13] the reaction is believed to occur in two stages:
- H2O2 + Fe(III)-E → H2O + O=Fe(IV)-E(.+)
- H2O2 + O=Fe(IV)-E(.+) → H2O + Fe(III)-E + O2[13]
- 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 that iron is not completely oxidized to +V but receives some "supporting electron" from the heme ligand. This heme has to be drawn then as radical cation (.+).
As hydrogen peroxide enters the active site, it interacts with the amino acids Asn147 (asparagine at position 147) and His74, 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.[13] The reactivity of the iron center may be improved by the presence of the phenolate ligand of Tyr357 in the fifth iron ligand, 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 His74 and Asn147 with reaction intermediates.[13] In general, the rate of the reaction can be determined by the Michaelis-Menten equation.[14]
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:
- H2O2 + H2R → 2H2O + 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. Also, the poison cyanide is a competitive inhibitor of catalase, strongly binding to the heme of catalase and stopping the enzyme's action.
Three-dimensional protein structures of the peroxidated catalase intermediates are available at the Protein Data Bank. This enzyme is commonly used in laboratories as a tool for learning the effect of enzymes upon reaction rates.
Hydrogen peroxide is a harmful by-product of many normal 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 decomposition of hydrogen peroxide into less reactive gaseous oxygen and water molecules.[15]
The true biological significance of catalase is not always straightforward to assess: Mice genetically engineered to lack catalase are phenotypically normal, indicating that this enzyme is dispensable in animals under some conditions.[16] A Catalase deficiency may increase the likelihood of developing Type II Diabetes.[17][18] Some human beings have very low levels of catalase (acatalasia), yet show few ill effects. It is likely that the predominant scavengers of H2O2 in normal mammalian cells are peroxiredoxins rather than catalase.[citation needed]
Human catalase works at an optimum temperature of 37 °C,[5] which is approximately the temperature of the human body. In contrast, catalase isolated from the hyperthermophile archaea Pyrobaculum calidifontis has a temperature optimum of 90 °C.[19]
Catalase is usually located in a cellular, bipolar environment organelle called the peroxisome.[20] 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 (N2) to reactive nitrogen atoms). Hydrogen peroxide is used as a potent antimicrobial agent when cells are infected with a pathogen. Pathogens that are catalase-positive, such as Mycobacterium tuberculosis, Legionella pneumophila, and Campylobacter jejuni, make catalase in order to deactivate the peroxide radicals, thus allowing them to survive unharmed within the host.[21]
Catalase contributes to ethanol metabolism in the body after ingestion of alcohol, however it only breaks down a small fraction of the alcohol in the body.[22]
All known animals use catalase in every organ, with particularly high concentrations occurring in the liver. One unique use of catalase occurs in bombardier beetle. The beetle has two sets of chemicals ordinarily stored separately in its paired glands. The larger of the pair, the storage chamber or reservoir, contains hydroquinones and hydrogen peroxide, whereas the smaller of the pair, the reaction chamber, contains catalases and peroxidases. 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.[23] The oxidation reaction is very exothermic (ΔH = −202.8 kJ/mol) which rapidly heats the mixture to the boiling point.[24]
Catalase is also universal among plants, and many fungi are also high producers of the enzyme.[25]
Almost all aerobic microorganisms use catalase. Catalase is also present in some anaerobic microorganisms, such as Methanosarcina barkeri.[26]
Catalase is used in the food industry for removing hydrogen peroxide from milk prior to cheese production.[27] Another use is in food wrappers where it prevents food from oxidizing.[28] Catalase is also used in the textile industry, removing hydrogen peroxide from fabrics to make sure the material is peroxide-free.[29]
A minor use is in contact lens hygiene - a few lens-cleaning products 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.[30] Recently, catalase has also begun to be used in the aesthetics industry. Several mask treatments combine the enzyme with hydrogen peroxide on the face with the intent of increasing cellular oxygenation in the upper layers of the epidermis.
The catalase test is also one of the main three tests used by microbiologists to identify species of bacteria. The presence of catalase enzyme in the test isolate is detected using hydrogen peroxide. If the bacteria possess catalase (i.e., are catalase-positive), when a small amount of bacterial isolate is added to hydrogen peroxide, bubbles of oxygen are observed.
In microbiology, the catalase test is used to differentiate between bacterial species in the lab. The test is done by placing a drop of hydrogen peroxide on a microscope slide. Using an applicator stick, a scientist touches the colony and then smears a sample into the hydrogen peroxide drop.
- If bubbles or froth forms, the organism is said to be catalase-positive. Staphylococci[31] and Micrococci[32] are catalase-positive. Other catalase positive organisms include Listeria, Corynebacterium diphtheriae, Burkholderia cepacia, Nocardia, the Family Enterobacteriaceae (Citrobacter, E. coli, Enterobacter, Klebsiella, Shigella, Yersinia, Proteus, Salmonella, Serratia, Pseudomonas), Mycobacterium tuberculosis, Aspergillus, and Cryptococcus.
While the catalase test alone cannot identify a particular organism, combined with other tests such as antibiotic resistance, it can aid diagnosis. The presence of catalase in bacterial cells depends on both the growth condition and the medium used to grow the cells.
According to recent scientific studies, low levels of catalase may play a role in the greying process of human hair. Hydrogen peroxide is naturally produced by the body and catalase breaks it down. If there is a dip in catalase levels, hydrogen peroxide cannot be broken down. This causes the hydrogen peroxide to bleach the hair from the inside out. This finding may someday be incorporated into anti-greying treatments for aging hair.[34][35][36]
The peroxisomal disorder acatalasia is due to a deficiency in the function of catalase. Genetic polymorphisms in catalase and its altered expression and activity are associated with oxidative DNA damage and subsequently the individual’s risk of cancer susceptibility.[37]
Catalase has been shown to interact with ABL2[38] and Abl gene.[38]
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- ^ "EC 1.11.1.6 - catalase". BRENDA: The Comprehensive Enzyme Information System. Department of Bioinformatics and Biochemistry, Technische Universität Braunschweig. http://www.brenda-enzymes.org/php/result_flat.php4?ecno=1.11.1.6&Suchword=&organism%5B%5D=&show_tm=0. Retrieved 2009-05-26.
- ^ Toner K, Sojka G, Ellis R. "A Quantitative Enzyme Study; CATALASE". bucknell.edu. Archived from the original on 2000-06-12. http://web.archive.org/web/20000612104029/http://www.facstaff.bucknell.edu/toner/gb/lab121/labs34.html. Retrieved 2007-02-11.
- ^ Loew O (May 1900). "A New Enzyme of General Occurrence in Organisms". Science 11 (279): 701–702. DOI:10.1126/science.11.279.701. PMID 17751716.
- ^ Sumner JB, Dounce AL (April 1937). "Crystalline catalase". Science 85 (2206): 366–367. DOI:10.1126/science.85.2206.366. PMID 17776781.
- ^ Sumner JB, Gralén N (March 1938). "The molecular weight of crystalline catalase". Science 87 (2256): 284–284. DOI:10.1126/science.87.2256.284. PMID 17831682.
- ^ Schroeder WA, Shelton JR, Shelton JB, Robberson B, Apell G (May 1969). "The amino acid sequence of bovine liver catalase: a preliminary report". Arch. Biochem. Biophys. 131 (2): 653–655. DOI:10.1016/0003-9861(69)90441-X. PMID 4892021.
- ^ Murthy MR, Reid TJ, Sicignano A, Tanaka N, Rossmann MG (October 1981). "Structure of beef liver catalase". J. Mol. Biol. 152 (2): 465–499. DOI:10.1016/0022-2836(81)90254-0. PMID 7328661.
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PEX1, PEX2 - PXMP3, PEX3, PEX5, PEX6, PEX7, PEX10, PEX11A, PEX11B, PEX11G, PEX12, PEX13, PEX14, PEX16, PEX19, PEX26
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