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InterPro: IPR011614 Catalase, N-terminal

Protein matchesHelp
UniProtKB
Matches:
2432 proteins
AccessionHelp IPR011614 Catalase_N
SecondaryHelp IPR002226
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR020835 Catalase-like domain, haem-dependent
Contains IPR002226 Catalase
IPR010582 Catalase-related immune responsive
IPR018028 Catalase related subgroup
GO Term annotationHelp
Process GO:0006979 response to oxidative stress
GO:0055114 oxidation reduction
Function GO:0004096 catalase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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 conserved region within catalase enzymes (EC:1.11.1.6).

Structural linksHelp
PDB - click here
SCOP: e.5.1.1 , e.5.1.2
CATH: 2.40.180.10
Database linksHelp
Enzyme: EC:1.11.1.6
PANDIT: PF00199
Blocks: IPB011614

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR011614 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O61235 Catalase-2

P04040 Catalase

P15202 Peroxisomal catalase A

P17336 Catalase

P24270 Catalase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR002226 Catalase
IPR018028 Catalase related subgroup
IPR020835 Catalase-like domain, haem-dependent
IPR011614 Catalase, N-terminal
IPR010582 Catalase-related immune responsive
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain

PublicationsHelp
1. Bai J, Cederbaum AI.
Mitochondrial catalase and oxidative injury.
10 189-99 2001 [PubMed: 11351128]
2. Chelikani P, Fita I, Loewen PC.
Diversity of structures and properties among catalases.
Cell. Mol. Life Sci. 61 192-208 2004 [PubMed: 14745498]
http://dx.doi.org/10.1007/s00018-003-3206-5

Additional ReadingHelp
Oldham ML, Brash AR, Newcomer ME.
The structure of coral allene oxide synthase reveals a catalase adapted for metabolism of a fatty acid hydroperoxide.
Proc. Natl. Acad. Sci. U.S.A. 102 2005 297-302 [PubMed: 15625113]
http://dx.doi.org/10.1073/pnas.0406352102
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
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
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
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InterPro 23.1