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Metabolic Modeling Tutorial
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MetaCyc Enzyme: lignin peroxidase

Gene: lipI Accession Number: G-10937 (MetaCyc)

Synonyms: O282

Species: Phanerochaete chrysosporium

Summary:
lignin peroxidases (LiPs) are monomeric hemoproteins with molecular masses around 40 kDa, and resemble classical peroxidases in that their Fe3+ is pentacoordinated to the four heme tetrapyrrole nitrogens and to a histidine residue. Like the classical peroxidases, LiPs are oxidized by hydrogen peroxide to give a two electron-oxidized intermediate (known as Compound I) in which the iron is present as Fe+4 and a free radical resides on the tetrapyrrole ring. Compound I then oxidizes a donor substrate by one electron, yielding a substrate-free radical and Compound II, in which the iron is still present as Fe+4, but no radical is present on the tetrapyrrole. The process continues when Compound II oxidizes a second molecule of donor substrate, giving another substrate-free radical and restoring the resting state of the peroxidase. Unlike classical peroxidases, LiPs can oxidize aromatic rings that are only moderately activated by electron-donating substituents, such as the major nonphenolic structures of lignin [Hammel08].

An important feature in LiPs is an invariant tryptophan residue - trp171 in the isozyme termed LiPA, which is thought to participate in longrange electron transfer from aromatic substrates that cannot make direct contact with the oxidized heme [Doyle98].

10 LiP genes designated lipA through lipJ are present in the Phanerochaete chrysosporium genome [Gaskell94]. It is not well understood why so many LiP copies are required.

This gene was first reported by [Schalch89] and corroborated by [Gaskell94].

Locations: extracellular space

Gene-Reaction Schematic: ?

GO Terms:

Cellular Component: GO:0005576 - extracellular region

Credits:
Created 28-Oct-2008 by Caspi R , SRI International


Enzymatic reaction of: lignin peroxidase

EC Number: 1.11.1.14

veratryl alcohol + hydrogen peroxide <=> veratraldehyde + 2 H2O

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

Reversibility of this reaction is unspecified.

Cofactors or Prosthetic Groups: heme b , Ca2+


References

Doyle98: Doyle WA, Blodig W, Veitch NC, Piontek K, Smith AT (1998). "Two substrate interaction sites in lignin peroxidase revealed by site-directed mutagenesis." Biochemistry 37(43);15097-105. PMID: 9790672

Gaskell94: Gaskell J, Stewart P, Kersten PJ, Covert SF, Reiser J, Cullen D (1994). "Establishment of genetic linkage by allele-specific polymerase chain reaction: application to the lignin peroxidase gene family of Phanerochaete chrysosporium." Biotechnology (N Y) 12(13);1372-5. PMID: 7765568

Hammel08: Hammel KE, Cullen D (2008). "Role of fungal peroxidases in biological ligninolysis." Curr Opin Plant Biol 11(3);349-55. PMID: 18359268

Schalch89: Schalch H, Gaskell J, Smith TL, Cullen D (1989). "Molecular cloning and sequences of lignin peroxidase genes of Phanerochaete chrysosporium." Mol Cell Biol 9(6);2743-7. PMID: 2761543


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 Mon Nov 24, 2014, biocyc14.