 |
InterPro: IPR018028 Catalase related subgroup
Protein matches
|
UniProtKB Matches: 2327 proteins |
|
Accession
|
IPR018028 Catalase_rel_subgroup |
Type
|
Domain |
Signatures
|
|
InterPro Relationships
|
|
Found in
|
IPR011614 Catalase, N-terminal
IPR020835 Catalase-like domain, haem-dependent
|
|
Contains
|
IPR002226 Catalase
|
|
InterPro annotation
|
|
Entry Details in BioMart
|
Abstract
|
Catalases (EC:1.11.1.6) are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water and molecular oxygen, serving to protect cells from its toxic effects [1]. Hydrogen peroxide is produced as a consequence of oxidative cellular metabolism and can be converted to the highly reactive hydroxyl radical via transition metals, this radical being able to damage a wide variety of molecules within a cell, leading to oxidative stress and cell death. Catalases act to neutralise hydrogen peroxide toxicity, and are produced by all aerobic organisms ranging from bacteria to man. Most catalases are mono-functional, haem-containing enzymes, although there are also bifunctional haem-containing peroxidase/catalases (IPR000763) that are closely related to plant peroxidases, and non-haem, manganese-containing catalases (IPR007760) that are found in bacteria [2].
This entry represents a subgroup within catalase enzymes (EC:1.11.1.6).
|
Structural links
|
|
Database links
|
|
Additional Reading
|
|
Loewen PC, Carpena X, Rovira C, Ivancich A, Perez-Luque R, Haas R, Odenbreit S, Nicholls P, Fita I.
Structure of Helicobacter pylori catalase, with and without formic acid bound, at 1.6 A resolution.
Biochemistry 43 2004 3089-103
[PubMed: 15023060]
http://dx.doi.org/10.1021/bi035663i
|
|
Murthy MR, Reid TJ 3rd, Sicignano A, Tanaka N, Rossmann MG.
Structure of beef liver catalase.
J. Mol. Biol. 152 1981 465-99
[PubMed: 7328661]
http://dx.doi.org/10.1016/0022-2836(81)90254-0
|
|
Andreoletti P, Sainz G, Jaquinod M, Gagnon J, Jouve HM.
High-resolution structure and biochemical properties of a recombinant Proteus mirabilis catalase depleted in iron.
Proteins 50 2003 261-71
[PubMed: 12486720]
http://dx.doi.org/10.1002/prot.10283
|
|
Hakansson KO, Brugna M, Tasse L.
The three-dimensional structure of catalase from Enterococcus faecalis.
Acta Crystallogr. D Biol. Crystallogr. 60 2004 1374-80
[PubMed: 15272159]
http://dx.doi.org/10.1107/S0907444904012004
|
|
Chelikani P, Carpena X, Fita I, Loewen PC.
An electrical potential in the access channel of catalases enhances catalysis.
J. Biol. Chem. 278 2003 31290-6
[PubMed: 12777389]
http://dx.doi.org/10.1074/jbc.M304076200
|
|
von Ossowski I, Mulvey MR, Leco PA, Borys A, Loewen PC.
Nucleotide sequence of Escherichia coli katE, which encodes catalase HPII.
J. Bacteriol. 173 1991 514-20
[PubMed: 1987146]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=1987146&action=stream&blobtype=pdf
|
|
Ni WT, Trelease RN.
Two genes encode the two subunits of cottonseed catalase.
Arch. Biochem. Biophys. 289 1991 237-43
[PubMed: 1898069]
http://dx.doi.org/10.1016/0003-9861(91)90467-W
|
|
Alfonso-Prieto M, Borovik A, Carpena X, Murshudov G, Melik-Adamyan W, Fita I, Rovira C, Loewen PC.
The structures and electronic configuration of compound I intermediates of Helicobacter pylori and Penicillium vitale catalases determined by X-ray crystallography and QM/MM density functional theory calculations.
J. Am. Chem. Soc. 129 2007 4193-205
[PubMed: 17358056]
http://dx.doi.org/10.1021/ja063660y
|
|
|
InterPro 23.1
|