Human catalase: looking for complete identity
Open accessAbstract
Catalases are well studied enzymes that play critical roles in protecting cells against the toxic effects of hydrogen peroxide. The ubiquity of the enzyme and the availability of substrates made heme catalases the focus of many biochemical and molecular biology studies over 100 years. In human, this has been implicated in various physiological and pathological conditions. Advancement in proteomics revealed many of novel and previously unknown features of this mysterious enzyme, but some functional aspects are yet to be explained. Along with discussion on future research area, this mini-review compile the information available on the structure, function and mechanism of action of human catalase.
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Gaetani, G., Galiano, S., Canepa, L., Ferraris, A., & Kirkman, H. (1989) · Blood · doi:10.1182/blood.v73.1.334.334 · Cited by 298 · see citing works
Predominant role of catalase in the disposal of hydrogen peroxide within human erythrocytes
Gaetani, G., Ferraris, A., Rolfo, M., Mangerini, R., Arena, S., & Kirkman, H. (1996) · Blood · doi:10.1182/blood.v87.4.1595.bloodjournal8741595 · Cited by 296 · see citing works
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Role of peroxisomes in ros/rns-metabolism: Implications for human disease
Fransen, M., Nordgren, M., Wang, B., & Apanasets, O. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.12.001 · Cited by 644 · see citing works
Peng, M., Shao, M., Dong, H., Han, X., Hao, M., Yang, Q., Lyu, Q., Tang, D., Shen, Z., Wang, K., et al. (2023) · Communications Biology · doi:10.1038/s42003-023-04473-2 · Cited by 22 · see citing works
- Authors
- Goyal, M. M., & Basak, A.
- Affiliations
- Datta Meghe Institute of Higher Education and Research (IN)
- Corresponding author
- Goyal, Madhur M.
- ORCID
- Basak, Anjan
- Venue
- Protein & Cell
- Publisher
- Oxford University Press (OUP)
- Published
- 2010-10
- Volume
- 1
- Issue
- 10
- Pages
- 888-897
- ISSN
- 1674-800X (ISSN-L)
- 1674-8018
- PMC
- PMC4875117
- OpenAlex
- W2062991061
- Cited by
- 273
- References
- 2
- Citations by year
- 2026: 26 · 2025: 26 · 2024: 30 · 2023: 34 · 2022: 30 · 2021: 29 · 2020: 14 · 2019: 18 · 2018: 3 · 2017: 11 · 2016: 4 · 2015: 5 · 2014: 13 · 2013: 14 · 2012: 11
- FWCI
- 0.85
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Protein & Cell (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Keywords
- hydrogen peroxide detoxification, enzyme structure, enzyme mechanism, oxidative stress
- MeSH terms
- Catalase, Heme, Humans, Hydrogen Peroxide
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