The peroxidase database
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Classes

Non Animal peroxidase superfamily: Class I

  Contact author: Christophe Dunand

  Last update: 2017-03-15 (Marcel Zamocky)

Class I peroxidase
-Ascorbate peroxidase (APx)
-Catalase peroxidase (CP)
-Cytochrome C peroxidase (CcP)
-Hybrid Ascorbate-Cytochrome C peroxidase (APx-CcP)
Profiles

Pfam: PF00141, peroxidase.
Interpro: IPR010255, Haem peroxidase and IPR002016, Haem peroxidase, plant/fungal/bacterial (non animal peroxidase).
The profiles do not make distinction between animal and non animal peroxidases and between the different non animal peroxidase classes.

Class I peroxidase
Interpro: IPR000763, Catalase-peroxidase haem and IPR002207, Plant ascorbate peroxidase.
The latter profile do not make distinction between Ascorbate peroxidase (APx) and Cytochrome c peroxidase (CcP).

Description Class I peroxidases have been found in plants, fungi, and prokaryotes. They are not glycosylated and do not have signal peptides, calcium ions, or disulfide bridges.

-Ascorbate peroxidase (APx) (EC 1.11.1.11, L-ascorbate:hydrogen-peroxide oxidoreductase): APx are found in chloroplastic organisms. They show a particularly strong specificity for the electron donor ascorbate. In higher plants, APx are separated, according to their cellular localization, into cytosolic, peroxisomal and chloroplastic.

-Catalase peroxidase (CP) (EC 1.11.1.6, hydrogen-peroxide:hydrogen-peroxide oxidoreductase): CP or HPI (hydroperoxidase I) or KatG, are mainly present in prokaryotes and marginaly in some fungi and some protists. They are fusion protein and typically have a dual catalytic activity, acting both as a catalase and as a peroxidase. In bateria, they are controlled as part of the OxyR regulon, which senses active oxygen species. the catalatic reaction of catalase-peroxidases takes place via the same two stages reaction of monofunctional catalases.

Enz (Por-FeIII) + H2O2 Cpd I (Por+.-FeIV = O) + H2O
Cpd I (Por+.-FeIV= O) + H2O2 Enz (Por-FeIII) + H2O + O2

In addition CP can use organic as electron donors for the reduction of compound I to the resting state via two one-electron transfers.

Cpd I(Por+.-FeIV= O) + 2AH2 Enz(Por-FeIII) + 2AH + H2O

-Cytochrome C peroxidase (CcP) (EC 1.11.1.5, ferrocytochrome-c: hydrogen-peroxide oxidoreductase): CcP play a major role scavenging H2O2 generated during aerobic respiration from the oxidation of cytochrome c in the mitochondrial intermembrane space. CcP are abscent from non mitochondrial organisms.

-APx-CcP: hybrid sequences containing APx- and CcP-specific motifs. They have been found mainly in unicellular organisms containing mitochondria and chloroplasts.
Literature
Zamocky M. Phylogenetic relationships in class I of the superfamily of bacterial, fungal, and plant peroxidases. Eur J Biochem. 2004 Aug;271(16):3297-309. PMID: 15291807

Zamocky M, Dunand C. Divergent evolutionary lines of fungal cytochrome c peroxidases belonging to the superfamily of bacterial, fungal and plant heme peroxidases. FEBS Lett. 2006 Dec 11;580(28-29):6655-64. Epub 2006 Nov 16. PMID: 17126331

Passardi F, Zamocky M, Favet J, Jakopitsch C, Penel C, Obinger C, Dunand C. Phylogenetic distribution of catalase-peroxidases: are there patches of order in chaos? Gene. 2007 Aug 1;397(1-2):101-13. Epub 2007 Apr 21. PMID: 17561356

Zámocký M, Gasselhuber B, Furtmüller PG, Obinger C (2014) Turning points in the evolution of peroxidase-catalase superfamily - molecular phylogeny of hybrid heme peroxidases. Cell. Mol. Life Sci. 71:4681-4696
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