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MetaCyc Enzyme: manganese peroxidase 1

Gene: MNP1 Accession Number: G-10927 (MetaCyc)

Species: Phanerochaete chrysosporium

Summary:
The manganese peroxidase (MnP) from the lignin-degrading fungus Phanerochaete chrysosporium, a hydrogen peroxide-dependent heme enzyme, oxidizes a variety of organic compounds but only in the presence of Mn2+. The enzyme binds 2 calcium ions, a B-type heme per subunit, and one Mn2+ ion.

The actual role of the enzyme is to oxidize the bound Mn2+ ion to Mn+3 in the presence of hydrogen peroxide. The product, Mn+3, is released from the active site if various bidentate chelators are available to stabilize it against disproportionation to Mn2+ and insoluble Mn4+. The physiological chelator is thought to be oxalate, an extracellular metabolite of many white rot fungi [Kuan93].

It is the complexed Mn+3 ion, not the enzyme, that oxidizes lignin and other organic substrates [Glenn86]. The purpose of this design is likey to transfer the oxidizing power of the manganese peroxidase to a small agent (the Mn+3 ion) that can diffuse into the lignified cell wall and attack it from within.

The MNP1 gene has been cloned and characterized [Pribnow89, Godfrey90], and the crystal structure of the protein has been determined.[Sundaramoorthy94, Sundaramoorthy97].

Analysis of the P. chrysosporium genome has shown that it encodes five MnPs [Martinez04].

Locations: extracellular space

Molecular Weight of Polypeptide: 39.557 kD (from nucleotide sequence)

Unification Links: Protein Model Portal:Q02567 , SMR:Q02567 , UniProt:Q02567

Relationship Links: Entrez-Nucleotide:PART-OF:M60672 , InterPro:IN-FAMILY:IPR001621 , InterPro:IN-FAMILY:IPR002016 , InterPro:IN-FAMILY:IPR010255 , InterPro:IN-FAMILY:IPR019793 , InterPro:IN-FAMILY:IPR019794 , InterPro:IN-FAMILY:IPR024589 , PDB:Structure:1MN1 , PDB:Structure:1MN2 , PDB:Structure:1MNP , PDB:Structure:1YYD , PDB:Structure:1YYG , PDB:Structure:1YZP , PDB:Structure:1YZR , PDB:Structure:3M5Q , PDB:Structure:3M8M , Pfam:IN-FAMILY:PF00141 , Pfam:IN-FAMILY:PF11895 , Prints:IN-FAMILY:PR00458 , Prints:IN-FAMILY:PR00462 , Prosite:IN-FAMILY:PS00435 , Prosite:IN-FAMILY:PS00436 , Prosite:IN-FAMILY:PS50873

Gene-Reaction Schematic: ?

GO Terms:

Cellular Component: GO:0005576 - extracellular region

Credits:
Created 27-Oct-2008 by Caspi R , SRI International


Enzymatic reaction of: manganese peroxidase

EC Number: 1.11.1.13

2 Mn2+ + hydrogen peroxide + 2 H+ <=> 2 Mn+3 + 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.

The reaction is favored in the direction shown.

In Pathways: manganese oxidation I

Cofactors or Prosthetic Groups: Ca2+

pH(opt): 5 [Sundaramoorthy94]


References

Glenn86: Glenn JK, Akileswaran L, Gold MH (1986). "Mn(II) oxidation is the principal function of the extracellular Mn-peroxidase from Phanerochaete chrysosporium." Arch Biochem Biophys 251(2);688-96. PMID: 3800395

Godfrey90: Godfrey BJ, Mayfield MB, Brown JA, Gold MH (1990). "Characterization of a gene encoding a manganese peroxidase from Phanerochaete chrysosporium." Gene 93(1);119-24. PMID: 2227420

Kuan93: Kuan IC, Tien M (1993). "Stimulation of Mn peroxidase activity: a possible role for oxalate in lignin biodegradation." Proc Natl Acad Sci U S A 90(4);1242-6. PMID: 8433984

Martinez04: Martinez D, Larrondo LF, Putnam N, Gelpke MD, Huang K, Chapman J, Helfenbein KG, Ramaiya P, Detter JC, Larimer F, Coutinho PM, Henrissat B, Berka R, Cullen D, Rokhsar D (2004). "Genome sequence of the lignocellulose degrading fungus Phanerochaete chrysosporium strain RP78." Nat Biotechnol 22(6);695-700. PMID: 15122302

Pribnow89: Pribnow D, Mayfield MB, Nipper VJ, Brown JA, Gold MH (1989). "Characterization of a cDNA encoding a manganese peroxidase, from the lignin-degrading basidiomycete Phanerochaete chrysosporium." J Biol Chem 264(9);5036-40. PMID: 2925681

Sundaramoorthy94: Sundaramoorthy M, Kishi K, Gold MH, Poulos TL (1994). "The crystal structure of manganese peroxidase from Phanerochaete chrysosporium at 2.06-A resolution." J Biol Chem 269(52);32759-67. PMID: 7806497

Sundaramoorthy97: Sundaramoorthy M, Kishi K, Gold MH, Poulos TL (1997). "Crystal structures of substrate binding site mutants of manganese peroxidase." J Biol Chem 272(28);17574-80. PMID: 9211904


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 Dec 22, 2014, BIOCYC13A.