Catalase Enzyme
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A Catalase Enzyme is an oxidoreductase that is an enzyme that catalyzes the decomposition of hydrogen peroxide into water and oxygen.
- Context:
- It can (often) exists as a Tetramer, meaning that it's composed of four subunits.
- …
- Example(s):
- Counter-Example(s):
- See: Enzyme Kinetics, Enzyme Activity, Enzyme Inhibition, Oxidative Stress, Reactive Oxygen Species, Turnover Number, Tetrameric Protein, Amino Acid.
References
2023
- (Wikipedia, 2023) ⇒ https://en.wikipedia.org/wiki/Catalase Retrieved:2023-6-10.
- Catalase is a common enzyme found in nearly all living organisms exposed to oxygen (such as bacteria, plants, and animals) which catalyzes the decomposition of hydrogen peroxide to water and oxygen.[1] It is a very important enzyme in protecting the cell from oxidative damage by reactive oxygen species (ROS). Catalase has one of the highest turnover numbers of all enzymes; one catalase molecule can convert millions of hydrogen peroxide molecules to water and oxygen each second.
Catalase is a tetramer of four polypeptide chains, each over 500 amino acids long.[2] 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,[3] and has a fairly broad maximum: the rate of reaction does not change appreciably between pH 6.8 and 7.5.[4] The pH optimum for other catalases varies between 4 and 11 depending on the species.[5] The optimum temperature also varies by species.[6]
- Catalase is a common enzyme found in nearly all living organisms exposed to oxygen (such as bacteria, plants, and animals) which catalyzes the decomposition of hydrogen peroxide to water and oxygen.[1] It is a very important enzyme in protecting the cell from oxidative damage by reactive oxygen species (ROS). Catalase has one of the highest turnover numbers of all enzymes; one catalase molecule can convert millions of hydrogen peroxide molecules to water and oxygen each second.
- ↑ Chelikani P, Fita I, Loewen PC (January 2004). “Diversity of structures and properties among catalases". Cellular and Molecular Life Sciences. 61 (2): 192–208. doi:10.1007/s00018-003-3206-5. hdl:10261/111097. PMID 14745498. S2CID 4411482.
- ↑ Boon EM, Downs A, Marcey D. "Catalase: H2O2: H2O2 Oxidoreductase". Catalase Structural Tutorial Text. Retrieved 2007-02-11.
- ↑ Maehly AC, Chance B (1954). “The assay of catalases and peroxidases". Methods of Biochemical Analysis. Methods of Biochemical Analysis. Vol. 1. pp. 357–424. doi:10.1002/9780470110171.ch14. ISBN 978-0-470-11017-1. PMID 13193536.
- ↑ Aebi H (1984). Catalase in vitro. Methods in Enzymology. Vol. 105. pp. 121–6. doi:10.1016/S0076-6879(84)05016-3. ISBN 978-0-12-182005-3. PMID 6727660.
- ↑ "EC 1.11.1.6 - catalase". BRENDA: The Comprehensive Enzyme Information System. Department of Bioinformatics and Biochemistry, Technische Universität Braunschweig. 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. Retrieved 2007-02-11.