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discounted EARLY registration ends Dec 31, 2014
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MetaCyc Reaction: 1.11.1.16/1.11.1.21

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 1.11.1.16 , 1.11.1.21

Enzymes and Genes:
hydroperoxidase I Inferred from experiment : katG ( Escherichia coli K-12 substr. MG1655 )
versatile peroxidase VPL1 Inferred from experiment : vpl1 ( Pleurotus eryngii )
versatile peroxidase VPL2 Inferred from experiment : vpl2 ( Pleurotus eryngii )

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Mass balance status: Balanced.

Enzyme Commission Primary Name for 1.11.1.16: versatile peroxidase

Enzyme Commission Synonyms for 1.11.1.16: VP, hybrid peroxidase, polyvalent peroxidase

Enzyme Commission Primary Name for 1.11.1.21: catalase-peroxidase

Enzyme Commission Synonyms for 1.11.1.21: katG (gene name)

Enzyme Commission Summary for 1.11.1.16:
This ligninolytic peroxidase combines the substrate-specificity characteristics of the two other ligninolytic peroxidases, EC 1.11.1.13, manganese peroxidase and EC 1.11.1.14, lignin peroxidase. It is also able to oxidize phenols, hydroquinones and both low- and high redox-potential dyes, due to a hybrid molecular architecture that involves multiple binding sites for substrates [Heinfling98, Camarero99].

Enzyme Commission Summary for 1.11.1.21:
Differs from EC 1.11.1.7, peroxidase in having a relatively high catalase (EC 1.11.1.6) activity with hydrogen peroxide as donor, releasing oxygen; both activities use the same heme active site. In Mycobacterium tuberculosis it is responsible for activation of the commonly used antitubercular drug, isoniazid.

Citations: [Martinez96, RuizDuenas99, RuizDuenas99a, Camarero00, RuizDuenas01, Banci03, PerezBoada05, Caramelo99, Loewen85, Hochman91, Fraaije96, Bertrand04, Vlasits10]

Gene-Reaction Schematic: ?

Unification Links: KEGG:R03532

Relationship Links: BRENDA:EC:1.11.1.16 , BRENDA:EC:1.11.1.21 , ENZYME:EC:1.11.1.16 , ENZYME:EC:1.11.1.21 , IUBMB-ExplorEnz:EC:1.11.1.16 , IUBMB-ExplorEnz:EC:1.11.1.21

Credits:
Revised 13-Sep-2012 by Caspi R , SRI International


References

Banci03: Banci L, Camarero S, Martinez AT, Martinez MJ, Perez-Boada M, Pierattelli R, Ruiz-Duenas FJ (2003). "NMR study of manganese(II) binding by a new versatile peroxidase from the white-rot fungus Pleurotus eryngii." J Biol Inorg Chem 8(7);751-60. PMID: 12884090

Bertrand04: Bertrand T, Eady NA, Jones JN, Jesmin , Nagy JM, Jamart-Gregoire B, Raven EL, Brown KA (2004). "Crystal structure of Mycobacterium tuberculosis catalase-peroxidase." J Biol Chem 279(37);38991-9. PMID: 15231843

Camarero00: Camarero S, Ruiz-Duenas FJ, Sarkar S, Martinez MJ, Martinez AT (2000). "The cloning of a new peroxidase found in lignocellulose cultures of Pleurotus eryngii and sequence comparison with other fungal peroxidases." FEMS Microbiol Lett 191(1);37-43. PMID: 11004397

Camarero99: Camarero S, Sarkar S, Ruiz-Duenas FJ, Martinez MJ, Martinez AT (1999). "Description of a versatile peroxidase involved in the natural degradation of lignin that has both manganese peroxidase and lignin peroxidase substrate interaction sites." J Biol Chem 274(15);10324-30. PMID: 10187820

Caramelo99: Caramelo L, Martinez MJ, Martinez AT (1999). "A search for ligninolytic peroxidases in the fungus pleurotus eryngii involving alpha-keto-gamma-thiomethylbutyric acid and lignin model dimers." Appl Environ Microbiol 65(3);916-22. PMID: 10049842

Fraaije96: Fraaije MW, Roubroeks HP, Hagen WR, Van Berkel WJ (1996). "Purification and characterization of an intracellular catalase-peroxidase from Penicillium simplicissimum." Eur J Biochem 235(1-2);192-8. PMID: 8631329

Heinfling98: Heinfling A, Ruiz-Duenas FJ, Martinez MJ, Bergbauer M, Szewzyk U, Martinez AT (1998). "A study on reducing substrates of manganese-oxidizing peroxidases from Pleurotus eryngii and Bjerkandera adusta." FEBS Lett 428(3);141-6. PMID: 9654123

Hochman91: Hochman A, Goldberg I (1991). "Purification and characterization of a catalase-peroxidase and a typical catalase from the bacterium Klebsiella pneumoniae." Biochim Biophys Acta 1077(3);299-307. PMID: 2029529

Loewen85: Loewen PC, Triggs BL, George CS, Hrabarchuk BE (1985). "Genetic mapping of katG, a locus that affects synthesis of the bifunctional catalase-peroxidase hydroperoxidase I in Escherichia coli." J Bacteriol 1985;162(2);661-7. PMID: 3886630

Martinez96: Martinez MJ, Ruiz-Duenas FJ, Guillen F, Martinez AT (1996). "Purification and catalytic properties of two manganese peroxidase isoenzymes from Pleurotus eryngii." Eur J Biochem 237(2);424-32. PMID: 8647081

PerezBoada05: Perez-Boada M, Ruiz-Duenas FJ, Pogni R, Basosi R, Choinowski T, Martinez MJ, Piontek K, Martinez AT (2005). "Versatile peroxidase oxidation of high redox potential aromatic compounds: site-directed mutagenesis, spectroscopic and crystallographic investigation of three long-range electron transfer pathways." J Mol Biol 354(2);385-402. PMID: 16246366

RuizDuenas01: Ruiz-Duenas FJ, Camarero S, Perez-Boada M, Martinez MJ, Martinez AT (2001). "A new versatile peroxidase from Pleurotus." Biochem Soc Trans 29(Pt 2);116-22. PMID: 11356138

RuizDuenas99: Ruiz-Duenas FJ, Martinez MJ, Martinez AT (1999). "Molecular characterization of a novel peroxidase isolated from the ligninolytic fungus Pleurotus eryngii." Mol Microbiol 31(1);223-35. PMID: 9987124

RuizDuenas99a: Ruiz-Duenas FJ, Martinez MJ, Martinez AT (1999). "Heterologous expression of Pleurotus eryngii peroxidase confirms its ability to oxidize Mn(2+) and different aromatic substrates." Appl Environ Microbiol 65(10);4705-7. PMID: 10508113

Vlasits10: Vlasits J, Jakopitsch C, Bernroitner M, Zamocky M, Furtmuller PG, Obinger C (2010). "Mechanisms of catalase activity of heme peroxidases." Arch Biochem Biophys 500(1);74-81. PMID: 20434429


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Wed Dec 17, 2014, BIOCYC14B.