|Gene:||MNP1||Accession Number: G-10927 (MetaCyc)|
Species: Phanerochaete chrysosporium
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.
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)
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
|Cellular Component:||GO:0005576 - extracellular region|
Enzymatic reaction of: manganese peroxidase
EC Number: 18.104.22.168
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]
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
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
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493