KEGG ENZYME: 1.11.1.13

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

PXB:

103942159

MGR:

MGG_10877

SSCK:

SPSK_07949

MAW:	19250360(J3458_001674)

MAJ:

MAA_06180

MBRN:

26237979(PER)

PCHM:

VFPPC_05033 VFPPC_08848 VFPPC_11138

AMUS:

LMH87_010554

PLJ:	28888498(PLICBS_003685)

VAL:	VDBG_01180

VDA:	VDAG_00782

CFJ:	CFIO01_00059

CHIG:

CH63R_05592 CH63R_13855

CDET:

87947432(CDEST_10932) 87948564(CDEST_12064)

ELA:	UCREL1_9357

PSCO:

LY89DRAFT_784261

GLZ:	GLAREA_09081 GLAREA_12952

PNO:	SNOG_01153

PTE:

PTT_13874

PTRR:

6341580(PtrM4_069760) 6341919(PtrM4_096340)

BZE:	COCCADRAFT_100992 COCCADRAFT_6260

BSC:	COCSADRAFT_150777 COCSADRAFT_31496

BOR:	COCMIDRAFT_103568 COCMIDRAFT_26472

AALT:

CC77DRAFT_1022965 CC77DRAFT_927990 CC77DRAFT_983629

ADAC:

96084511(ACET3X_004189) 96086335(ACET3X_006013)

ARAB:

EKO05_0003464 EKO05_0005482 EKO05_0008801 EKO05_0009451

ZTR:	MYCGRDRAFT_77793

FFU:	CLAFUR5_02699 CLAFUR5_03971

BCOM:

BAUCODRAFT_148591

NPA:	UCRNP2_36 UCRNP2_7003

PPL:	POSPLDRAFT_50226

TVS:

TRAVEDRAFT_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)

DSQ:	DICSQDRAFT_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)

PCO:	PHACADRAFT_144982 PHACADRAFT_256980 PHACADRAFT_256984 PHACADRAFT_256991 PHACADRAFT_256997 PHACADRAFT_262882 PHACADRAFT_94399

SHS:	STEHIDRAFT_142136(Short-MNP2) STEHIDRAFT_161701(short-MNP4) STEHIDRAFT_171838(short-MNP1) STEHIDRAFT_182927(MnP3at) STEHIDRAFT_182931(MnP5at) STEHIDRAFT_182932(GP)

HIR:	HETIRDRAFT_101580(mnp5) HETIRDRAFT_106089(mnp1) HETIRDRAFT_108376(mnp6) HETIRDRAFT_127157(mnp7) HETIRDRAFT_181068(mnp2) HETIRDRAFT_181069(gpx1) HETIRDRAFT_181263

PSQ:	PUNSTDRAFT_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)

ADL:

AURDEDRAFT_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

FME:

FOMMEDRAFT_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)

LBC:	LACBIDRAFT_191903

CCI:	CC1G_02104

ABP:	AGABI1DRAFT71350(AGABI1DRAFT_71350) AGABI1DRAFT80178(AGABI1DRAFT_80178)

ABV:	AGABI2DRAFT188334(AGABI2DRAFT_188334) AGABI2DRAFT221245(MnP)

PCUB:

JR316_0005469 JR316_0005475 JR316_0010530 JR316_0010651 JR316_0011049 JR316_0011050 JR316_0011052 JR316_0011099

MRR:	Moror_16339 Moror_2690 Moror_3885

» 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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