KEGG   ENZYME: 1.11.1.13
Entry
EC 1.11.1.13                Enzyme                                 
Name
manganese peroxidase;
peroxidase-M2;
Mn-dependent (NADH-oxidizing) peroxidase
Class
Oxidoreductases;
Acting on a peroxide as acceptor;
Peroxidases
Sysname
Mn(II):hydrogen-peroxide oxidoreductase
Reaction(IUBMB)
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O [RN:R00011]
Reaction(KEGG)
R00011
Substrate
Mn(II) [CPD:C19610];
H+ [CPD:C00080];
H2O2 [CPD:C00027]
Product
Mn(III) [CPD:C19611];
H2O [CPD:C00001]
Comment
A hemoprotein. The enzyme from white rot basidiomycetes is involved in the oxidative degradation of lignin. The enzyme oxidizes a bound Mn2+ ion to Mn3+ in the presence of hydrogen peroxide. The product, Mn3+, is released from the active site in the presence of a chelator (mostly oxalate and malate) that stabilizes it against disproportionation to Mn2+ and insoluble Mn4+ [4]. The complexed Mn3+ ion can diffuse into the lignified cell wall, where it oxidizes phenolic components of lignin and other organic substrates [1]. It is inactive with veratryl alcohol or nonphenolic substrates.
History
EC 1.11.1.13 created 1992
Orthology
K20205  manganese peroxidase
Genes
PXB103942159
MGRMGG_10877
PPEIPpBr36_03798 PpBr36_04335
SSCKSPSK_07949
MAWMAC_06049
MAJMAA_06180
PLJVFPFJ_06374
VALVDBG_01180
VDAVDAG_00782
CFJCFIO01_00059
CHIGCH63R_02113 CH63R_05117 CH63R_05592 CH63R_06587 CH63R_06834 CH63R_13855
ELAUCREL1_9357
PSCOLY89DRAFT_784261
GLZGLAREA_09081 GLAREA_12952
PNOSNOG_01153
PTEPTT_13874
BZECOCCADRAFT_100992 COCCADRAFT_6260
BSCCOCSADRAFT_150777 COCSADRAFT_31496
BORCOCMIDRAFT_103568 COCMIDRAFT_26472
AALTCC77DRAFT_1022965 CC77DRAFT_927990 CC77DRAFT_983629
ZTRMYCGRDRAFT_77793
FFUCLAFUR5_02699 CLAFUR5_03971
BCOMBAUCODRAFT_148591
NPAUCRNP2_36 UCRNP2_7003
PPLPOSPLDRAFT_50226
TVSTRAVEDRAFT_112835(MnP2s) TRAVEDRAFT_130496(MnP4s) TRAVEDRAFT_131080(MnP3s) TRAVEDRAFT_133560(MnP12s) TRAVEDRAFT_26239(VP2) TRAVEDRAFT_28895(VP3at) TRAVEDRAFT_43477(MnP5s) TRAVEDRAFT_44897(MnP10s) TRAVEDRAFT_51375(MnP1s) TRAVEDRAFT_51442(MnP13) TRAVEDRAFT_51451(MnP7s) TRAVEDRAFT_51455(MnP6s) TRAVEDRAFT_51457(MnP9s) TRAVEDRAFT_74179(MnP8s) TRAVEDRAFT_74595(MnP11s)
DSQDICSQDRAFT_108150(MnP8-short) DICSQDRAFT_141471(MnP7-short) DICSQDRAFT_150431(MnP9-short) DICSQDRAFT_155734(VP3) DICSQDRAFT_169526(MnP6-short) DICSQDRAFT_169843(MnP3) DICSQDRAFT_169849(MnP4) DICSQDRAFT_173638(VP1) DICSQDRAFT_50355(MnP5-short) DICSQDRAFT_59877(MnP2) DICSQDRAFT_70857(MnP1)
PCOPHACADRAFT_144982 PHACADRAFT_256980 PHACADRAFT_256984 PHACADRAFT_256991 PHACADRAFT_256997 PHACADRAFT_262882 PHACADRAFT_94399
SHSSTEHIDRAFT_142136(Short-MNP2) STEHIDRAFT_161701(short-MNP4) STEHIDRAFT_171838(short-MNP1) STEHIDRAFT_182927(MnP3at) STEHIDRAFT_182931(MnP5at) STEHIDRAFT_182932(GP)
HIRHETIRDRAFT_101580(mnp5) HETIRDRAFT_106089(mnp1) HETIRDRAFT_108376(mnp6) HETIRDRAFT_127157(mnp7) HETIRDRAFT_181068(mnp2) HETIRDRAFT_181069(gpx1) HETIRDRAFT_181263
PSQPUNSTDRAFT_131002(MnP8l) PUNSTDRAFT_133299(MnP3-short) PUNSTDRAFT_133979(MnP9l) PUNSTDRAFT_134820(MnP2) PUNSTDRAFT_143055(MnP4-short) PUNSTDRAFT_59952(MnP10l) PUNSTDRAFT_60510(GP1) PUNSTDRAFT_67813(MnP5el) PUNSTDRAFT_68159(MnP1) PUNSTDRAFT_74133(MnP6-long) PUNSTDRAFT_91363(MnP7l)
ADLAURDEDRAFT_111702(GP1) AURDEDRAFT_115060(MnP3) AURDEDRAFT_138865(GP9) AURDEDRAFT_159695(MnP6) AURDEDRAFT_160740(GP2) AURDEDRAFT_160749(GP3) AURDEDRAFT_166460(MnP2) AURDEDRAFT_166489(GP4) AURDEDRAFT_166511(GP5) AURDEDRAFT_166512(GP6) AURDEDRAFT_166515(GP7) AURDEDRAFT_166530(GP8) AURDEDRAFT_170472(MnP4) AURDEDRAFT_172093(MnP5) AURDEDRAFT_173082(GP10) AURDEDRAFT_173267(GP11) AURDEDRAFT_199636
FMEFOMMEDRAFT_107469(FmMnP7l) FOMMEDRAFT_123070(FmMnP2s) FOMMEDRAFT_133892(FmMnP6l) FOMMEDRAFT_133924(FmMnP5l) FOMMEDRAFT_143664(FmMnP1l) FOMMEDRAFT_145801(FmMnP2l) FOMMEDRAFT_146495(FmMnP9l) FOMMEDRAFT_146522(FmGP) FOMMEDRAFT_149577(FmMnP8l) FOMMEDRAFT_150512(FmMnP1a) FOMMEDRAFT_150522(FmMnP1s) FOMMEDRAFT_152661(FmMnP4l) FOMMEDRAFT_157870(FmMnP11l) FOMMEDRAFT_16475(FmMnP2a) FOMMEDRAFT_29597(FmMnP10l) FOMMEDRAFT_84718(FmMnP3l) FOMMEDRAFT_91941(FmMnP3s)
LBCLACBIDRAFT_191903
MRRMoror_16339 Moror_2690 Moror_3885
CCICC1G_02104
ABPAGABI1DRAFT71350(AGABI1DRAFT_71350) AGABI1DRAFT80178(AGABI1DRAFT_80178)
ABVAGABI2DRAFT188334(AGABI2DRAFT_188334) AGABI2DRAFT221245(MnP)
 » show all
Reference
1  [PMID:3800395]
  Authors
Glenn JK, Akileswaran L, Gold MH.
  Title
Mn(II) oxidation is the principal function of the extracellular Mn-peroxidase from Phanerochaete chrysosporium.
  Journal
Arch Biochem Biophys 251:688-96 (1986)
DOI:10.1016/0003-9861(86)90378-4
Reference
2  [PMID:3080953]
  Authors
Paszczynski A, Huynh VB, Crawford R.
  Title
Comparison of ligninase-I and peroxidase-M2 from the white-rot fungus Phanerochaete chrysosporium.
  Journal
Arch Biochem Biophys 244:750-65 (1986)
DOI:10.1016/0003-9861(86)90644-2
Reference
3  [PMID:3167051]
  Authors
Wariishi H, Akileswaran L, Gold MH.
  Title
Manganese peroxidase from the basidiomycete Phanerochaete chrysosporium: spectral characterization of the oxidized states and the catalytic cycle.
  Journal
Biochemistry 27:5365-70 (1988)
DOI:10.1021/bi00414a061
Reference
4  [PMID:8433984]
  Authors
Kuan IC, Tien M
  Title
Stimulation of Mn peroxidase activity: a possible role for oxalate in lignin biodegradation.
  Journal
Proc Natl Acad Sci U S A 90:1242-6 (1993)
DOI:10.1073/pnas.90.4.1242
Other DBs
ExplorEnz - The Enzyme Database: 1.11.1.13
IUBMB Enzyme Nomenclature: 1.11.1.13
ExPASy - ENZYME nomenclature database: 1.11.1.13
UM-BBD (Biocatalysis/Biodegradation Database): 1.11.1.13
BRENDA, the Enzyme Database: 1.11.1.13
CAS: 114995-15-2

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