Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

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 Thu Nov 27, 2014, biocyc13.