1.11.1.13: manganese peroxidase
This is an abbreviated version!
For detailed information about manganese peroxidase, go to the full flat file.
Word Map on EC 1.11.1.13
-
1.11.1.13
-
lignin
-
laccase
-
ligninolytic
-
phanerochaete
-
chrysosporium
-
white-rot
-
basidiomycete
-
decolor
-
peroxidases
-
pleurotus
-
lignin-degrading
-
trametes
-
versicolor
-
veratryl
-
ostreatus
-
straw
-
mniii
-
lignocellulosic
-
bjerkandera
-
sordida
-
lignocellulolytic
-
remazol
-
subvermispora
-
lacteus
-
eryngii
-
irpex
-
lignin-modifying
-
kraft
-
sawdust
-
phlebia
-
adusta
-
ceriporiopsis
-
1-hydroxybenzotriazole
-
nutrition
-
lignocellulose-degrading
-
ligninase
-
sajor-caju
-
wood-rotting
-
dye-decolorizing
-
tigrinus
-
mnso4
-
biosorption
-
delignification
-
delignified
-
biobleaching
-
degradation
-
synthesis
-
lentinula
-
biotreatment
-
non-phenolic
-
industry
-
decolourisation
-
2,6-dimethoxyphenol
-
paper production
-
low-nitrogen
-
environmental protection
-
biotechnology
-
biofuel production
- 1.11.1.13
- lignin
- laccase
-
ligninolytic
- phanerochaete
- chrysosporium
-
white-rot
-
basidiomycete
-
decolor
- peroxidases
- pleurotus
-
lignin-degrading
- trametes
- versicolor
-
veratryl
- ostreatus
- straw
-
mniii
-
lignocellulosic
- bjerkandera
- sordida
-
lignocellulolytic
-
remazol
- subvermispora
- lacteus
- eryngii
- irpex
-
lignin-modifying
-
kraft
- sawdust
- phlebia
- adusta
-
ceriporiopsis
- 1-hydroxybenzotriazole
- nutrition
-
lignocellulose-degrading
-
ligninase
- sajor-caju
-
wood-rotting
-
dye-decolorizing
- tigrinus
- mnso4
-
biosorption
-
delignification
-
delignified
-
biobleaching
- degradation
- synthesis
- lentinula
-
biotreatment
-
non-phenolic
- industry
-
decolourisation
- 2,6-dimethoxyphenol
- paper production
-
low-nitrogen
- environmental protection
- biotechnology
- biofuel production
Reaction
2 Mn(II)
+
2 H+
+
Synonyms
CmMnP, extralong PMnP, hybrid Mn-peroxidase, Il-MnP1, Il-MnP6, L-MnP, LeMnP2, long PMnP, manganese peroxidase, manganese peroxidase 2, manganese-dependent peroxidase, MGmn2, MGmnp1, MGmnp3, Mn-dependent (NADH-oxidizing) peroxidase, Mn2+: hydrogen peroxide oxidoreductase, Mn2+:H2O2 oxidoreductase, Mn2+:hydrogen peroxide oxidoreductase, MnP, MnP 1, MnP II, MnP-BBP6, MnP-GY, MnP-PGY, mnp1, MnP10, MnP117436, MnP12, MnP157986, MnP2, MnP3, MnP50297, MnP6, Moror_3885, MP, MrMnP1, multifunctional manganese peroxidase, Nf b19 MNP2, peroxidase, manganese, peroxidase-M2, rMnP3-BBP6, short manganese peroxidase, short MnP
ECTree
1.11.1.13 manganese peroxidaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.11.1.13 - manganese peroxidase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,2'-azino-bis(3-ethylbenzothiazoline)-6-sulphonate + H2O2
?
-
reaction with and without Mn2+
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
2,2'-azinobis(3-ethylbenzthiazoline)-6-sulfonic acid + H2O2 + Mn2+
?
-
-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
coerulignone + 2 H2O
Phlebia sp. MG-60
MnP activity is determined spectrophotometrically by measuring the oxidation of 2,6-dimethoxyphenol to coerulignone (epsilon = 49.6 mM/cm) in 50 mM malonate buffer (pH 4.5) containing 1.0 mM MnSO4, 1.0 mM 2,6-dimethoxyphenol, and 0.2 mM H2O2 at 469 nm, 37°C
-
-
?
4-(4-hydroxy-3-methoxy-phenyl)-2-butanone + H2O2
4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-butan-2-one + 4-(4-hydroxy-3-methoxyphenyl)-3-buten-2-one + 4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-3-buten-2-one + 3-(3-oxo-butyl)-hexa-2,4-dienedioic acid-1-methyl ester
alizarin red S + H2O2
? + 2 H2O
substrate of A172W variants mutant enzymes, poor activity with the wild-type enzyme
-
-
?
benzo[a]pyrene + ?
?
-
key enzyme in degradation of benzo[a]pyrene and other polycyclic aromatic hydrocarbons
-
-
?
benzo[a]pyrene + ?
benzo[a]pyrene-1,6-quinone + ?
-
oxidation in presence of Tween 80
-
-
?
Co2+ + H+ + H2O2
Co3+ + H2O
-
reduction of enzyme compound II, oxidation at 2% the rate of Mn2+ oxidation
-
?
crystal violet + H2O2
? + 2 H2O
substrate of wild-type and A172W variants mutant enzymes
-
-
?
fluorene + H2O2
9H-fluorene-3,4-diol
denim bleaching PAH degradation, product analysis by HPLC
-
-
?
guaiacol + 2 H+ + H2O2
oxidized guaiacol 4'-hydroxy-3',5-dimethoxy[1,1'-biphenyl]-3,4-dione + 2 H2O
Il-MnP1 oxidizes guaiacol and provides a first radical A, which undergoes a variety of non-enzymatic reactions that mainly consists of reactions of resonance stabilization to generate the next radical B. In turn the C-C radical coupling of two B radicals generates a dimeric 3',5-dimethoxy-3,4-dihydro[1,1'-biphenyl]-4,4'-diol, which can be further oxidized by Il-MnP1 to produce 3,3'-dimethoxy[1,1'-bi(cyclohexa-2,5-diene)]-4,4'-dione and 1-[[1(1')Z]-3'-methoxy-4,4'-dioxo[1,1'-bi(cyclohexa-2,5-dien-1-yliden)]-3-yl]-1-methyldioxidan-1-ium. Furthermore, Il-MnP1 oxidizes 3',5-dimethoxy-3,4-dihydro[1,1'-biphenyl]-4,4'-diol to produce a radical C,which is also subject to a variety of non-enzymatic reactions to produce a radical D. Finally, radical D is subjected to further oxidation and C-C coupling for the production of 4'-hydroxy-3',5-dimethoxy[1,1'-biphenyl]-3,4-dione, 1(3),2(5),3(3)-trimethoxy-2(3),2(4)-dihydro[1(1),2(1):2(3),3(1)-terphenyl]-1(4),2(4),3(4)-triol, and [1(1)(2(1))E]-3(4)-hydroxy-1(3),2(5),3(3)-trimethoxy-1(4)H,2(4)H-[1(1),2(1):2(3),3(1)-terphenyl]-1(4),2(4)-dione
-
-
?
guaiacylglycerol-beta-guaiacyl ether + H2O2
? + 2 H2O
substrate of A172W variants mutant enzymes
-
-
?
indigo carmine + H2O2
? + 2 H2O
substrate of wild-type and A172W variants mutant enzymes
-
-
?
methyl orange + H2O2
? + 2 H2O
substrate of wild-type and A172W variants mutant enzymes
-
-
?
Mn2+ + di(2-methylpent-2-enyl) sulfide + H+
Mn3+ + 2,4-dimethylthiophene + 2-methyl-2-pentenal + H2O
-
-
-
-
?
phenanthrene + 2 H+ + 2 H2O2
phenanthrene-9,10-dione + 2 H2O
denim bleaching PAH degradation, product analysis by HPLC
-
-
?
Reactive Black 5 + 2 H+ + H2O2
Reactive Black 5 + 2 H2O
dye decolorization
-
-
?
Reactive Blue 19 + 2 H+ + H2O2
oxidized Reactive Blue 19 + 2 H2O
dye decolorization
-
-
?
remazol brilliant blue R + H2O2
? + 2 H2O
substrate of wild-type and A172W variants mutant enzymes
-
-
?
veratryl alcohol + H2O2 + Mn2+
?
-
veratryl alcohol oxidation requires the simultaneous presence of H2O2 and Mn2+
-
-
?
veratrylglycerol-beta-guaiacyl ether + H2O2
? + 2 H2O
substrate of A172W variants mutant enzymes
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
the kcat value for the reaction is dependent of the Mn(III) chelator molecules malonate, lactate and oxalate, indicating that the enzyme oxidizes chelated Mn(II) to Mn(III)
-
-
?
2 Mn2+ + H2O2 + aflatoxin B1
2 Mn3+ + aflatoxin B1-8,9-dihydrodiol
-
maximum elimination of 86.0% of aflatoxin B1 is observed after 48 h in a reaction mixture containing 5 nkat of enzyme, and the addition of Tween 80 enhances elimination. The treatment of aflatoxin B1 by 20 nkat MnP reduces the mutagenic activity by 69.2%. Analysis suggests that aflatoxin B1 is first oxidized to aflatoxin B1-8,9-epoxide and then hydrolyzed to aflatoxin B1-8,9-dihydrodiol
-
-
?
2 Mn2+ + H2O2 + aflatoxin B1
2 Mn3+ + aflatoxin B1-8,9-dihydrodiol
-
maximum elimination of 86.0% of aflatoxin B1 is observed after 48 h in a reaction mixture containing 5 nkat of enzyme, and the addition of Tween 80 enhances elimination. The treatment of aflatoxin B1 by 20 nkat MnP reduces the mutagenic activity by 69.2%. Analysis suggests that aflatoxin B1 is first oxidized to aflatoxin B1-8,9-epoxide and then hydrolyzed to aflatoxin B1-8,9-dihydrodiol
-
-
?
2 veratryl alcohol + H2O2
2 veratraldehyde + H2O
no substrate of wild-type
-
-
?
2 veratryl alcohol + H2O2
2 veratraldehyde + H2O
no substrate of wild-type
-
-
?
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid) + H2O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
ABTS
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
ABTS
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
Irpex lacteus CCTCC AF2014020
ABTS
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
Irpex lacteus F17
ABTS
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
Irpex lacteus F17
ABTS
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
substrate of A172W variants mutant enzymes
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
substrate of A172W variants mutant enzymes
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonate) + H2O2
?
-
in absence or presence of Mn2+
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonate) + H2O2
?
-
in absence or presence of Mn2+
-
-
?
2,2'-azino-bis(3-ethylbenzthiazole-6-sulfonic acid) + H2O2
?
no substrate of wild-type
-
-
?
2,2'-azino-bis(3-ethylbenzthiazole-6-sulfonic acid) + H2O2
?
no substrate of wild-type
-
-
?
2,2'-azino-bis(3-ethylbenzthiazole-6-sulfonic acid) + H2O2 + H+
?
-
-
-
-
r
2,2'-azino-bis(3-ethylbenzthiazole-6-sulfonic acid) + H2O2 + H+
?
-
-
-
-
r
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + Mn2+ + ?
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + Mn2+ + ?
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + Mn2+ + ?
?
-
-
-
-
?
2,4,6-trichlorophenol + H2O2
?
-
no oxidation in absence of Mn2+
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
-
-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
Bacillus velezensis Al-Dhabi 140
-
-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
Irpex lacteus CCTCC AF2014020
-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
substrate of A172W variants mutant enzymes, very low activity with the wild-type enzyme
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
substrate of A172W variants mutant enzymes, very low activity with the wild-type enzyme
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
reaction in absence or in presence of Mn2+
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
the highest relative activity for 2,6-dimethoxyphenol oxidation is observed in the presence of 10 mM malonate
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
the highest relative activity for 2,6-dimethoxyphenol oxidation is observed in the presence of 10 mM malonate
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
reaction in absence or in presence of Mn2+
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
the highest relative activity for 2,6-dimethoxyphenol oxidation is observed in the presence of 10 mM malonate
-
-
?
4-(4-hydroxy-3-methoxy-phenyl)-2-butanone + H2O2
4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-butan-2-one + 4-(4-hydroxy-3-methoxyphenyl)-3-buten-2-one + 4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-3-buten-2-one + 3-(3-oxo-butyl)-hexa-2,4-dienedioic acid-1-methyl ester
-
3-(3-oxo-butyl)-hexa-2,4-dienedioic acid-1-methyl ester is the dominant product
-
-
?
4-(4-hydroxy-3-methoxy-phenyl)-2-butanone + H2O2
4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-butan-2-one + 4-(4-hydroxy-3-methoxyphenyl)-3-buten-2-one + 4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-3-buten-2-one + 3-(3-oxo-butyl)-hexa-2,4-dienedioic acid-1-methyl ester
Phanerodontia chrysosporium BKM-F-1767
-
3-(3-oxo-butyl)-hexa-2,4-dienedioic acid-1-methyl ester is the dominant product
-
-
?
4-(4-hydroxy-3-methoxy-phenyl)-2-butanone + H2O2
4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-butan-2-one + 4-(4-hydroxy-3-methoxyphenyl)-3-buten-2-one + 4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-3-buten-2-one + 3-(3-oxo-butyl)-hexa-2,4-dienedioic acid-1-methyl ester
-
-
-
-
?
H2O2 + 2,2'-azino-bis(3-ethyl)-benzothiazoline-6-sulfonic acid
H2O + ?
-
oxidized at a faster rate in presence of Mn(II) than in absence of Mn(II)
-
-
?
H2O2 + 2,2'-azino-bis(3-ethyl)-benzothiazoline-6-sulfonic acid
H2O + ?
-
oxidized at a faster rate in presence of Mn(II) than in absence of Mn(II)
-
-
?
H2O2 + 2,6-dimethoxyphenol
H2O + ?
-
oxidized at a faster rate in presence of Mn(II) than in absence of Mn(II)
-
-
?
H2O2 + 2,6-dimethoxyphenol
H2O + ?
-
oxidized at a faster rate in presence of Mn(II) than in absence of Mn(II)
-
-
?
H2O2 + guaiacol
H2O + ?
-
oxidized at a faster rate in presence of Mn(II) than in absence of Mn(II)
-
-
?
H2O2 + guaiacol
H2O + ?
-
oxidized at a faster rate in presence of Mn(II) than in absence of Mn(II)
-
-
?
H2O2 + Poly R-478
?
-
Mn2+ is required for reaction with Poly R-478 with MnP3
-
-
?
H2O2 + Poly R-478
?
-
MnP2 depolymerizes the polymeric azo dye,Poly R-478, regardless of the presence of Mn2+, to complete its catalytic cycle
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Deuteromycotina sp.
-
-
product Mn3+ possibly migrates into polymer molecules, such as lignin, nylon and melanin, and initiates nonspecific oxidation, Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Deuteromycotina sp.
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Deuteromycotina sp.
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
specifically oxidizes Mn2+
alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme, dicarboxylic acids facilitate the dissociation of Mn3+ from enzyme, Mn3+ oxidizes o-phenylenediamine and p-anisidine, Mn3+ oxidizes o-dianisidine, Mn3+ oxidizes amines, Mn3+ oxidizes a variety of phenols, Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
single Mn2+ binding site in the vicinity of the heme
alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme, dicarboxylic acids facilitate the dissociation of Mn3+ from enzyme, Mn3+ oxidizes o-phenylenediamine and p-anisidine, Mn3+ oxidizes o-dianisidine, Mn3+ oxidizes amines, Mn3+ oxidizes a variety of phenols, Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme, dicarboxylic acids facilitate the dissociation of Mn3+ from enzyme, Mn3+ oxidizes o-phenylenediamine and p-anisidine, Mn3+ oxidizes o-dianisidine, Mn3+ oxidizes amines, Mn3+ oxidizes a variety of phenols, Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by Mn2+
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
chelating organic acids facilitate the dissociation of Mn3+ from enzyme, Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes vanillylacetone, chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
in presence of Mn2+, H2O2 and glutathione MnP oxidizes by Mn3+ nonphenolic beta-aryl ether lignin model compounds, veratryl alcohol, anisyl alcohol, benzyl alcohol and thiols to thiyl radicals which abstracts a hydrogen from the substrate forming a benzylic radical, mechanism, glutathione can be replaced by dithiothreitol, dithioerythritol or cysteine
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes o-dianisidine
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes a variety of phenols, Mn3+ oxidizes methoxy benzenes: 1,2,4-tri-, 1,2,3,5-tetra-, 1,2,4,5-tetra-, pentamethoxybenzene, veratryl alcohol is oxidized by thiyl radicals derived from Mn3+ oxidation of glutathione, not directly by Mn3+
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
oxidation and cleavage of a phenolic lignin model dimer and its products, MnP catalyzes C-alpha-C-beta cleavages, C-alpha-oxidation and alkyl-aryl cleavages of phenolic syringyl type beta-1 lignin structures via Mn3+
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
Mn3+ oxidizes lignin
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
Mn3+ oxidizes lignin
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
Mn3+ oxidizes lignin, Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
each catalytic cycle step is irreversible
alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme, Mn3+ oxidizes phenolic lignin model compounds, Mn3+ oxidizes vanillyl alcohol, Mn3+ oxidizes lignin, Mn3+-organic acid complexes oxidize terminal phenolic substrates in a second-order reaction, Mn3+ oxidizes thiols, Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines, the diffusible product is Mn3+, Mn3+ oxidizes amines, chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
specifically oxidizes Mn2+
product Mn3+ is a nonspecific oxidant which in turn oxidizes a variety of organic compounds, Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
specifically oxidizes Mn2+
Mn3+ complexed to lactate or other alpha-hydroxy acids acts as an obligatory oxidation intermediate in the oxidation of various dyes and lignin model compounds, Mn3+-lactate complex oxidizes all dyes oxidized by the enzyme in presence of Mn2+: NADH, pinacyanol, phenol red and poly B-411, the diffusible product is Mn3+
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
specifically oxidizes Mn2+
Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
specifically oxidizes Mn2+
chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
in presence of H2O2 enzyme oxidizes Mn2+ significantly faster than all other substrates, main function of enzyme is oxidation of Mn2+ to Mn3+
Mn3+ complexed to lactate or other alpha-hydroxy acids acts as an obligatory oxidation intermediate in the oxidation of various dyes and lignin model compounds, Mn3+-lactate complex oxidizes all dyes oxidized by the enzyme in presence of Mn2+: NADH, pinacyanol, phenol red and poly B-411, the diffusible product is Mn3+, chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
role for Arg-177 in promoting efficient Mn2+ binding and oxidation by MnP
freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates, Mn3+ oxidizes lignin
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ complex oxidizes a variety of organic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes vanillylacetone, Mn3+ oxidizes syringyl alcohol, syringyl aldehyde, syringic acid, syringaldazine, coniferyl alcohol, sinapic acid
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes vanillyl alcohol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes 2,6-dimethoxyphenol, Mn3+ oxidizes o-dianisidine, the diffusible product is Mn3+, Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
oxidation of Mn2+ to Mn3+ at a redox potential of 1.5 V
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates, Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
Mn3+ oxidizes syringic acid, 4-hydroxy-3-methoxycinnamic acid, isoeugenol, ascorbate, Mn3+ oxidizes vanillyl alcohol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
Mn3+ oxidizes vanillyl alcohol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
Mn3+ oxidizes o-dianisidine, Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines, Mn3+ oxidizes p-cresol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
free divalent Mn is the substrate, not Mn2+-complexes
alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme, Mn3+ oxidizes phenolic lignin model compounds, Mn3+ oxidizes vanillyl alcohol, Mn3+ oxidizes lignin, Mn3+-organic acid complexes oxidize terminal phenolic substrates in a second-order reaction, Mn3+ oxidizes thiols, Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines, the diffusible product is Mn3+, Mn3+ oxidizes amines, chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Mn2+ is an obligatory substrate for MnP compound II, whereas compound I formation occurs with Mn2+, p-cresol and organic peroxides, e.g. peracetic acid, m-chloroperoxybenzoic acid and p-nitroperoxybenzoic acid
alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme, Mn3+ oxidizes phenolic lignin model compounds, Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines, Mn3+ oxidizes p-cresol, Mn3+ oxidizes amines, Mn3+ oxidizes a variety of phenols, chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Mn2+ binds to a common site close to the delta-meso-carbon without blocking the approach of small molecules to the heme edge
Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
Mn3+-chelate-complexes catalyze decarboxylation and demeth(ox)ylation of aromatic substrates, Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
role of manganese in organic compound oxidations by MnP is to serve as a one-electron transfer mediator
Mn3+ complex oxidizes a variety of organic substrates, Mn3+ oxidizes phenolic lignin model compounds, Mn3+-chelate-complexes catalyze decarboxylation and demeth(ox)ylation of aromatic substrates, Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
little or no enzyme activity in absence of Mn2+
Mn3+ oxidizes vanillylacetone, Mn3+ oxidizes phenol red, Mn3+ oxidizes a variety of phenols, Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
oxidizes Mn2+ in presence of H2O2 to a higher oxidation state, enzyme activity is dependent on Mn2+ acting as electron carriers
Mn3+ complex oxidizes a variety of organic substrates, Mn3+ oxidizes phenolic lignin model compounds, Mn3+ oxidizes vanillylacetone, Mn3+ oxidizes syringyl alcohol, syringyl aldehyde, syringic acid, syringaldazine, coniferyl alcohol, sinapic acid, Mn3+ oxidizes 2,6-dimethoxyphenol, Mn3+ oxidizes o-dianisidine, the diffusible product is Mn3+, Mn3+ oxidizes a variety of phenols, Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
MnP isoenzymes serve different functions in lignin biodegradation, each may have a preferred substrate
the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by Mn2+
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
Mn3+ functions not as a primary oxidant of nonphenolic units in lignin, i.e. it plays another role in lignin-degradation than lignin peroxidase
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by veratryl alcohol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
initial depolymerization of the lignin polymer
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Mn2+ is a component of woody plant tissues
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
Mn3+ is stabilized by chelating agents, malonate is the most effective physiological chelator excreted by the fungus
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
freely diffusible, enzyme-generated Mn(III)-organic-acid complex is an catalyst for the oxidative depolymerization of lignin in wood
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
Mn3+ is produced under lignolytic conditions
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation, the mechanism enables the fungus to oxidize structures within woods which are inaccessible to enzymes
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
acts together with lignin peroxidase in lignin-degradation of white rot fungi
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
acts together with lignin peroxidase in lignin-degradation of white rot fungi
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
acts together with lignin peroxidase in lignin-degradation of white rot fungi
Mn3+ functions not as a primary oxidant of nonphenolic units in lignin, i.e. it plays another role in lignin-degradation than lignin peroxidase
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
in absence of H2O2 it may play a role in fungal peroxide production under ligninolytic conditions
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium BKM-F 1767
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium BKM-F 1767
-
little or no enzyme activity in absence of Mn2+
Mn3+ oxidizes vanillylacetone, Mn3+ oxidizes phenol red
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium BKM-F 1767
-
-
Mn3+ oxidizes phenolic lignin model compounds, Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium BKM-F 1767
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
each catalytic cycle step is irreversible
alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme, Mn3+ oxidizes phenolic lignin model compounds
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
completion of MnP catalytic cycle requires Mn2+
freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates, Mn3+ oxidizes phenolic lignin model compounds, Mn3+ oxidizes vanillyl alcohol, chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
Mn2+ binds to a common site close to the delta-meso-carbon without blocking the approach of small molecules to the heme edge
Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
-
Mn3+ oxidizes phenolic lignin model compounds, in presence of Mn2+, H2O2 and glutathione MnP oxidizes by Mn3+ nonphenolic beta-aryl ether lignin model compounds, veratryl alcohol, anisyl alcohol, benzyl alcohol and thiols to thiyl radicals which abstracts a hydrogen from the substrate forming a benzylic radical, mechanism, glutathione can be replaced by dithiothreitol, dithioerythritol or cysteine, Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
important component of lignin degradation system
Mn3+ is produced under lignolytic conditions
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
Mn3+ oxidizes lignin
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
Mn3+ oxidizes phenolic lignin model compounds, Mn3+ oxidizes lignin, Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium VKM F-1767
-
oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
Mn3+-chelate-complexes catalyze decarboxylation and demeth(ox)ylation of aromatic substrates, Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium VKM F-1767
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium VKM F-1767
-
role of manganese in organic compound oxidations by MnP is to serve as a one-electron transfer mediator
Mn3+ complex oxidizes a variety of organic substrates, Mn3+ oxidizes phenolic lignin model compounds, Mn3+-chelate-complexes catalyze decarboxylation and demeth(ox)ylation of aromatic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium VKM F-1767
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium VKM F-1767
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by Mn2+
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes vanillylacetone, Mn3+ oxidizes phenol red, Mn3+ oxidizes a variety of phenols, Mn3+ oxidizes several methoxylated and hydroxylated phenolic compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes vanillylideneacetone, Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes phenol red, Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
preferential degradation of lignin in wheat straw
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes syringaldazine, Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
oxidizes Mn2+ as the best substrate
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
preferential degradation of lignin in wheat straw
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
oxidizes Mn2+ as the best substrate
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
-
?
Reactive Black 5 + 2 H+ + H2O2
oxidized Reactive Black 5 + 2 H2O
dye decolorization, substrate of A172W variants mutant enzymes
-
-
?
Reactive Black 5 + 2 H+ + H2O2
oxidized Reactive Black 5 + 2 H2O
dye decolorization, substrate of A172W variants mutant enzymes
-
-
?
Reactive Black 5 + H2O2
? + H2O
no substrate of wild-type
-
-
?
Reactive Black 5 + H2O2
? + H2O
no substrate of wild-type
-
-
?
Remazol Brilliant Blue R + H2O2
?
dye decolorization
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzoic acid + 2 H2O
substrate of A172W variants mutant enzymes
-
-
?
additional information
?
-
-
in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
the enzyme is essential for lignin degradation
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-
?
additional information
?
-
-
Mn2+-dependent and Mn2+-independent peroxidase activities, substrates: 2,6-dimethoxyphenol, 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate, guaiacol and veratryl alcohol
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-
?
additional information
?
-
-
enzyme oxidizes 4-aminophenol and hydroquinone
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-
?
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
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-
?
additional information
?
-
-
MnP oxidizes phenolic and nonphenolic aromatic compounds, e.g. phenol red and veratryl alcohol
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-
?
additional information
?
-
-
in absence of Mn2+ enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate, o-phenylenediamine and phenol red, the former two are stimulated, the latter is inhibited by Mn2+, guaiacol and pyrocatechol are oxidized only in presence of Mn2+
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-
?
additional information
?
-
-
the enzyme is essential for lignin degradation
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-
?
additional information
?
-
-
catalyzes the oxidation of Mn(II) to Mn(III), which in turn can oxidize phenolic substrates
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-
?
additional information
?
-
-
no activity with veratryl alcohol
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-
?
additional information
?
-
-
in absence of Mn2+ enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate, o-phenylenediamine and phenol red, the former two are stimulated, the latter is inhibited by Mn2+, guaiacol and pyrocatechol are oxidized only in presence of Mn2+
-
-
?
additional information
?
-
-
Mn2+-dependent and Mn2+-independent peroxidase activities, substrates: 2,6-dimethoxyphenol, 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate, guaiacol and veratryl alcohol
-
-
?
additional information
?
-
-
enzyme oxidizes 4-aminophenol and hydroquinone
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-
?
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
enzyme oxidizes 2,6-dimethoxyphenol
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-
?
additional information
?
-
-
Mn-mediated and Mn-independent activity on phenolic and non-phenolic aromatic substrates
-
-
?
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
?
additional information
?
-
-
MnP oxidizes phenolic and nonphenolic aromatic compounds, e.g. phenol red and veratryl alcohol
-
-
?
additional information
?
-
-
Mn-mediated and Mn-independent activity on phenolic and non-phenolic aromatic substrates
-
-
?
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
?
additional information
?
-
-
the enzyme is essential for lignin degradation
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-
?
additional information
?
-
evaluation of the dye decolorization ability of the purified enzyme, MnP-BBP6, the enzyme is used to decolorize different types of synthetic dyes including RBBR, Congo red (CR), brilliant blue R (BBR), methyl orange (MO), bromophenol blue (BPB), and crystal violet (CV). Denim bleaching by the purified MnP-BBP6
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-
-
additional information
?
-
isozyme MnP3 shows a broad substrate specificity
-
-
-
additional information
?
-
Cerrena unicolor BBP6
isozyme MnP3 shows a broad substrate specificity
-
-
-
additional information
?
-
Cerrena unicolor BBP6
evaluation of the dye decolorization ability of the purified enzyme, MnP-BBP6, the enzyme is used to decolorize different types of synthetic dyes including RBBR, Congo red (CR), brilliant blue R (BBR), methyl orange (MO), bromophenol blue (BPB), and crystal violet (CV). Denim bleaching by the purified MnP-BBP6
-
-
-
additional information
?
-
-
enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
-
-
?
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
?
additional information
?
-
-
enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
-
-
?
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
?
additional information
?
-
-
no activity with veratryl alcohol
-
-
?
additional information
?
-
-
no oxidation of Fe2+, Cu2+, Zn2+
-
-
?
additional information
?
-
-
the enzyme is essential for lignin degradation
-
-
?
additional information
?
-
-
MnP oxidizes polycyclic aromatic hydrocarbons
-
-
?
additional information
?
-
-
MnP oxidizes chlorophenols and arsenic-containing warefare agents
-
-
?
additional information
?
-
no activity with veratryl alcohol (VA)
-
-
-
additional information
?
-
the oxidation of guaiacol mainly belongs to a series of polymeric reactions of radicals initiated by isozyme Il-MnP1,whether they are in the presence and absence of Mn2+ at either pH 4.0 or pH 7.4. Both wild-type Il-MnP1 and the variants exhibit negligible activity on veratryl alcohol oxidation in the absence of Mn2+
-
-
-
additional information
?
-
-
the oxidation of guaiacol mainly belongs to a series of polymeric reactions of radicals initiated by isozyme Il-MnP1,whether they are in the presence and absence of Mn2+ at either pH 4.0 or pH 7.4. Both wild-type Il-MnP1 and the variants exhibit negligible activity on veratryl alcohol oxidation in the absence of Mn2+
-
-
-
additional information
?
-
Irpex lacteus CCTCC AF2014020
the oxidation of guaiacol mainly belongs to a series of polymeric reactions of radicals initiated by isozyme Il-MnP1,whether they are in the presence and absence of Mn2+ at either pH 4.0 or pH 7.4. Both wild-type Il-MnP1 and the variants exhibit negligible activity on veratryl alcohol oxidation in the absence of Mn2+
-
-
-
additional information
?
-
Irpex lacteus F17
the oxidation of guaiacol mainly belongs to a series of polymeric reactions of radicals initiated by isozyme Il-MnP1,whether they are in the presence and absence of Mn2+ at either pH 4.0 or pH 7.4. Both wild-type Il-MnP1 and the variants exhibit negligible activity on veratryl alcohol oxidation in the absence of Mn2+
-
-
-
additional information
?
-
-
enzyme oxidizes non-phenolic lignin-related compounds, including veratryl alcohol
-
-
?
additional information
?
-
-
enzyme is able to oxidatively depolymerize both dimeric lignin-model compounds and milled spruce-wood lignin
-
-
?
additional information
?
-
-
protein complex containing MnP, laccase and beta-glucosidase
-
-
?
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
enzyme oxidizes 3,3,5,5-tetramethylbenzidine
-
-
?
additional information
?
-
-
enzyme oxidizes veratryl alcohol and o-tolidine
-
-
?
additional information
?
-
-
MnP oxidizes phenolic and nonphenolic aromatic compounds, e.g. phenol red and veratryl alcohol
-
-
?
additional information
?
-
-
in presence of H2O2 and Mn2+ the enzyme oxidizes lignin and lignin-model compounds
-
-
?
additional information
?
-
-
MnP oxidizes phenolic and nonphenolic aromatic compounds, e.g. phenol red and veratryl alcohol
-
-
?
additional information
?
-
the phenolic and non-phenolic lignin dimers guaiacylglycerol-beta-guaiacyl ether (Ge) and veratrylglycerol-beta-guaiacyl ether (Ve) are tested as substrates at pH 3.0-5.0. The phenolic lignin dimer Ge is barely oxidized by the wild-type enzyme (2% conversion), but after introduction of the A172W mutation around 33% can be degraded at pH 3.0 and pH 4.0, and around 15% at pH 5.0. All additional mutations (except for A269R) further increased the activity towards guaiacylglycerol-beta-guaiacyl ether at pH 3.0 and pH 4.0, with the A172W K168V mutant showing the highest conversion of up to 56% at pH 3.0. The more recalcitrant non-phenolic lignin dimer veratrylglycerol-beta-guaiacyl ether is oxidized only by the mutants, but not by the wild-type enzyme. The activity of the mutants is more similar to the substrate specificity of EC 1.11.1.14. The wild-type enzyme and the mutants are active with dyes: crystal violet, methyl orange, alizarin red S, indigo carmine, and remazol brilliant blue R, except for the poor activity of the wild-type enzyme with alizarin red S, overview. The mutants show similar tendencies, decolorization at pH 3.0 is stronger than that with wild-type enzyme. The wild-type MrMnP1 is able to convert ABTS, 2,6-DMP, and Mn2+, but not high-redox-potential substrates, such as Reactive Black 5 or veratryl alcohol
-
-
-
additional information
?
-
-
the phenolic and non-phenolic lignin dimers guaiacylglycerol-beta-guaiacyl ether (Ge) and veratrylglycerol-beta-guaiacyl ether (Ve) are tested as substrates at pH 3.0-5.0. The phenolic lignin dimer Ge is barely oxidized by the wild-type enzyme (2% conversion), but after introduction of the A172W mutation around 33% can be degraded at pH 3.0 and pH 4.0, and around 15% at pH 5.0. All additional mutations (except for A269R) further increased the activity towards guaiacylglycerol-beta-guaiacyl ether at pH 3.0 and pH 4.0, with the A172W K168V mutant showing the highest conversion of up to 56% at pH 3.0. The more recalcitrant non-phenolic lignin dimer veratrylglycerol-beta-guaiacyl ether is oxidized only by the mutants, but not by the wild-type enzyme. The activity of the mutants is more similar to the substrate specificity of EC 1.11.1.14. The wild-type enzyme and the mutants are active with dyes: crystal violet, methyl orange, alizarin red S, indigo carmine, and remazol brilliant blue R, except for the poor activity of the wild-type enzyme with alizarin red S, overview. The mutants show similar tendencies, decolorization at pH 3.0 is stronger than that with wild-type enzyme. The wild-type MrMnP1 is able to convert ABTS, 2,6-DMP, and Mn2+, but not high-redox-potential substrates, such as Reactive Black 5 or veratryl alcohol
-
-
-
additional information
?
-
the phenolic and non-phenolic lignin dimers guaiacylglycerol-beta-guaiacyl ether (Ge) and veratrylglycerol-beta-guaiacyl ether (Ve) are tested as substrates at pH 3.0-5.0. The phenolic lignin dimer Ge is barely oxidized by the wild-type enzyme (2% conversion), but after introduction of the A172W mutation around 33% can be degraded at pH 3.0 and pH 4.0, and around 15% at pH 5.0. All additional mutations (except for A269R) further increased the activity towards guaiacylglycerol-beta-guaiacyl ether at pH 3.0 and pH 4.0, with the A172W K168V mutant showing the highest conversion of up to 56% at pH 3.0. The more recalcitrant non-phenolic lignin dimer veratrylglycerol-beta-guaiacyl ether is oxidized only by the mutants, but not by the wild-type enzyme. The activity of the mutants is more similar to the substrate specificity of EC 1.11.1.14. The wild-type enzyme and the mutants are active with dyes: crystal violet, methyl orange, alizarin red S, indigo carmine, and remazol brilliant blue R, except for the poor activity of the wild-type enzyme with alizarin red S, overview. The mutants show similar tendencies, decolorization at pH 3.0 is stronger than that with wild-type enzyme. The wild-type MrMnP1 is able to convert ABTS, 2,6-DMP, and Mn2+, but not high-redox-potential substrates, such as Reactive Black 5 or veratryl alcohol
-
-
-
additional information
?
-
-
no activity with veratryl alcohol
-
-
?
additional information
?
-
-
MnP oxidizes polycyclic aromatic hydrocarbons
-
-
?
additional information
?
-
-
MnP oxidizes polycyclic aromatic hydrocarbons
-
-
?
additional information
?
-
-
catalytic cycle of enzyme, oxidation states: native enzyme via compound I via compound II to native enzyme, Mn2+ and phenols reduce MnP compound I to compound II, but only Mn2+ is a substrate for MnP compound II, Mn(II)/Mn(III) redox couple enables enzyme to rapidly oxidize terminal phenolic substrates
-
-
?
additional information
?
-
-
catalytic cycle of enzyme, oxidation states: native enzyme via compound I via compound II to native enzyme, Mn2+ and phenols reduce MnP compound I to compound II, but only Mn2+ is a substrate for MnP compound II, Mn(II)/Mn(III) redox couple enables enzyme to rapidly oxidize terminal phenolic substrates
-
-
?
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
?
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme shows Mn-dependent oxidase activity against glutathione, dithiothreitol and dihydroxymaleic acid, forming H2O2 at the expense of oxygen
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme shows Mn-dependent oxidase activity against glutathione, dithiothreitol and dihydroxymaleic acid, forming H2O2 at the expense of oxygen
-
-
?
additional information
?
-
-
primary reaction product of peroxidation with H2O2 is enzyme compound I, formation of compound II from I follows second-order kinetic
-
-
?
additional information
?
-
-
enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
-
-
?
additional information
?
-
-
enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
-
-
?
additional information
?
-
-
enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
-
-
?
additional information
?
-
-
in absence of Mn2+ the enzyme oxidizes pinacyanol as most easily oxidized dye at 1.7% of the rate of the Mn2+ oxidation
-
-
?
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADH to NAD+, generating H2O2 for oxidizing other substrates
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADH to NAD+, generating H2O2 for oxidizing other substrates
-
-
?
additional information
?
-
-
in presence of H2O2 and Mn2+ the enzyme oxidizes a variety of phenolic compounds, especially vinyl and syringyl side-chain substituted substrates
-
-
?
additional information
?
-
-
in presence of H2O2 and Mn2+ the enzyme oxidizes a variety of phenolic compounds, especially vinyl and syringyl side-chain substituted substrates
-
-
?
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
?
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
?
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
?
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
?
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
?
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
?
additional information
?
-
-
no activity with veratryl alcohol
-
-
?
additional information
?
-
-
catalytic cycle: MnP is oxidized by H2O2 to compound I, Mn2+, ferrocyanide or phenols reduce compound I to compound II, which is reduced to the ferric state by Mn2+ or ferrocyanide, but not by phenols, Mn2+ completes the cycle, substrates are oxidized via delta-meso heme edge of the enzyme, model of the active site
-
-
?
additional information
?
-
-
large substrates have no ready access to the catalytic center
-
-
?
additional information
?
-
-
large substrates have no ready access to the catalytic center
-
-
?
additional information
?
-
-
presence of proximal and distal histidines at the active center
-
-
?
additional information
?
-
-
Mn2+-dependent oxidation of 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
Mn2+-independent oxidase activity on NAD(P)H
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
-
-
?
additional information
?
-
-
no other metal can substitute Mn2+
-
-
?
additional information
?
-
-
Mn2+-independent oxidation of small phenolic compounds, such as guaiacol and dimethoxyphenol, rates are greatly reduced compared with the Mn-mediated reaction
-
-
?
additional information
?
-
-
MnP oxidizes nitroaromatic compounds
-
-
?
additional information
?
-
-
enzyme oxidizes 2,6-dimethoxyphenol
-
-
?
additional information
?
-
-
enzyme oxidizes the polymeric dyes poly R-481 and poly B-411
-
-
?
additional information
?
-
-
in presence of Mn2+ enzyme oxidizes various organic compounds
-
-
?
additional information
?
-
-
in presence of Mn2+ enzyme oxidizes various organic compounds
-
-
?
additional information
?
-
-
in presence of Mn2+ enzyme oxidizes various organic compounds
-
-
?
additional information
?
-
-
in presence of Mn2+ enzyme oxidizes various organic compounds
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADH to NAD+
-
-
?
additional information
?
-
-
manganese peroxidase (MnP) is applied to induce the in vitro oxidation of the broad-spectrum antibiotic sulfamethoxazole (SMX). 87.04% of the SMX is transformed following first-order kinetics (kobs = 0.438/h) within 6 h when 40 U/l of MnP is added. The reaction kinetics are investigated under different conditions, including pH, MnP activity, and H2O2 concentration. The active species Mn3+ is responsible for the oxidation of SMX, and the Mn3+ production rate is monitored to reveal the interaction among MnP, Mn3+, and SMX, computational analysis, overview. Possible oxidation pathways of SMX are proposed based on single-electron transfer mechanism, which primarily included the S-N bond cleavage, the C-S bond cleavage, and one electron loss without bond breakage. It is then transformed to hydrolysis, N-H oxidation, self-coupling, and carboxylic acid coupling products. SMX stepwise undergoes an N-H oxidation and eventually converts into nitroso benzene and a nitro benzene compound. In addition, the sulfamethoxazole cation radical can also turn into self-coupling products, such as SMX-dimer
-
-
-
additional information
?
-
Phanerodontia chrysosporium BKM-F 1767
-
enzyme oxidizes phenol red
-
-
?
additional information
?
-
Phanerodontia chrysosporium BKM-F 1767
-
in presence of Mn2+ enzyme oxidizes various organic compounds
-
-
?
additional information
?
-
Phanerodontia chrysosporium BKM-F 1767
-
in absence of H2O2 the enzyme shows Mn-dependent oxidase activity against glutathione, dithiothreitol and dihydroxymaleic acid, forming H2O2 at the expense of oxygen
-
-
?
additional information
?
-
Phanerodontia chrysosporium BKM-F 1767
-
in presence of H2O2 and Mn2+ the enzyme oxidizes a variety of phenolic compounds, especially vinyl and syringyl side-chain substituted substrates
-
-
?
additional information
?
-
Phanerodontia chrysosporium BKM-F 1767
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
-
-
?
additional information
?
-
Phanerodontia chrysosporium BKM-F 1767
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADH to NAD+
-
-
?
additional information
?
-
Phanerodontia chrysosporium BKMF-1767
-
manganese peroxidase (MnP) is applied to induce the in vitro oxidation of the broad-spectrum antibiotic sulfamethoxazole (SMX). 87.04% of the SMX is transformed following first-order kinetics (kobs = 0.438/h) within 6 h when 40 U/l of MnP is added. The reaction kinetics are investigated under different conditions, including pH, MnP activity, and H2O2 concentration. The active species Mn3+ is responsible for the oxidation of SMX, and the Mn3+ production rate is monitored to reveal the interaction among MnP, Mn3+, and SMX, computational analysis, overview. Possible oxidation pathways of SMX are proposed based on single-electron transfer mechanism, which primarily included the S-N bond cleavage, the C-S bond cleavage, and one electron loss without bond breakage. It is then transformed to hydrolysis, N-H oxidation, self-coupling, and carboxylic acid coupling products. SMX stepwise undergoes an N-H oxidation and eventually converts into nitroso benzene and a nitro benzene compound. In addition, the sulfamethoxazole cation radical can also turn into self-coupling products, such as SMX-dimer
-
-
-
additional information
?
-
Phanerodontia chrysosporium CCTCC AF96007
-
manganese peroxidase (MnP) is applied to induce the in vitro oxidation of the broad-spectrum antibiotic sulfamethoxazole (SMX). 87.04% of the SMX is transformed following first-order kinetics (kobs = 0.438/h) within 6 h when 40 U/l of MnP is added. The reaction kinetics are investigated under different conditions, including pH, MnP activity, and H2O2 concentration. The active species Mn3+ is responsible for the oxidation of SMX, and the Mn3+ production rate is monitored to reveal the interaction among MnP, Mn3+, and SMX, computational analysis, overview. Possible oxidation pathways of SMX are proposed based on single-electron transfer mechanism, which primarily included the S-N bond cleavage, the C-S bond cleavage, and one electron loss without bond breakage. It is then transformed to hydrolysis, N-H oxidation, self-coupling, and carboxylic acid coupling products. SMX stepwise undergoes an N-H oxidation and eventually converts into nitroso benzene and a nitro benzene compound. In addition, the sulfamethoxazole cation radical can also turn into self-coupling products, such as SMX-dimer
-
-
-
additional information
?
-
structural properties
-
-
?
additional information
?
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
Phanerodontia chrysosporium OGC101
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
?
additional information
?
-
Phanerodontia chrysosporium OGC101
-
large substrates have no ready access to the catalytic center
-
-
?
additional information
?
-
Phanerodontia chrysosporium OGC101
-
enzyme oxidizes 2,6-dimethoxyphenol
-
-
?
additional information
?
-
Phanerodontia chrysosporium OGC101
-
presence of proximal and distal histidines at the active center
-
-
?
additional information
?
-
Phanerodontia chrysosporium OGC101
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
Phanerodontia chrysosporium OGC101
-
catalytic cycle: MnP is oxidized by H2O2 to compound I, Mn2+, ferrocyanide or phenols reduce compound I to compound II, which is reduced to the ferric state by Mn2+ or ferrocyanide, but not by phenols, Mn2+ completes the cycle, substrates are oxidized via delta-meso heme edge of the enzyme, model of the active site
-
-
?
additional information
?
-
Phanerodontia chrysosporium OGC101
-
enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
-
-
?
additional information
?
-
Phanerodontia chrysosporium OGC101
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
Phanerodontia chrysosporium OGC101
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADH to NAD+, generating H2O2 for oxidizing other substrates
-
-
?
additional information
?
-
Phanerodontia chrysosporium OGC101
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
-
-
?
additional information
?
-
Phanerodontia chrysosporium OGC101
-
no other metal can substitute Mn2+
-
-
?
additional information
?
-
Phanerodontia chrysosporium OGC101
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
?
additional information
?
-
Phanerodontia chrysosporium OGC101
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
?
additional information
?
-
Phanerodontia chrysosporium OGC101
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
?
additional information
?
-
Phanerodontia chrysosporium OGC101
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Mn2+-independent oxidation of small phenolic compounds, such as guaiacol and dimethoxyphenol, rates are greatly reduced compared with the Mn-mediated reaction
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-
?
additional information
?
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Phanerodontia chrysosporium VKM F-1767
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catalytic cycle with oxidized intermediates MnP compound I and II
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-
?
additional information
?
-
Phanerodontia chrysosporium VKM F-1767
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enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
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-
?
additional information
?
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Phanerodontia chrysosporium VKM F-1767
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catalytic cycle with oxidized intermediates MnP compound I and II
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-
?
additional information
?
-
Phanerodontia chrysosporium VKM F-1767
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Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
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-
?
additional information
?
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Phanerodontia chrysosporium VKM F-1767
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enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
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-
?
additional information
?
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Phanerodontia chrysosporium VKM F-1767
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no activity with veratryl alcohol
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-
?
additional information
?
-
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poor substrates: benzoate, benzaldehyde or benzyl alcohol
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-
?
additional information
?
-
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enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
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-
?
additional information
?
-
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in absence of H2O2 the enzyme oxidizes Mn-dependently NADH to NAD+, generating H2O2 for oxidizing other substrates
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-
?
additional information
?
-
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catalytic cycle with oxidized intermediates MnP compound I and II
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-
?
additional information
?
-
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Mn-dependent oxidation of phenols requires superoxide anion and H2O2, phenolic hydroxyl group is essential
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-
?
additional information
?
-
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in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
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-
?
additional information
?
-
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in presence of Mn2+ enzyme oxidizes various organic compounds
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-
?
additional information
?
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Phlebia radiata 79 / ATCC 64658
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poor substrates: benzoate, benzaldehyde or benzyl alcohol
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-
?
additional information
?
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Phlebia radiata 79 / ATCC 64658
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enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
?
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
?
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
?
additional information
?
-
-
Mn2+-independent peroxidase activity against phenolic substrates, e.g. phenol red
-
-
?
additional information
?
-
-
Mn2+-dependent oxidation of 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
Mn2+-independent oxidase activity on NAD(P)H
-
-
?
additional information
?
-
-
Mn2+-independent oxidase activity on NAD(P)H
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-
?
additional information
?
-
-
MnP oxidizes phenolic and nonphenolic aromatic compounds, e.g. phenol red and veratryl alcohol
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-
?
additional information
?
-
-
in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
?
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
?
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
?
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
Mn2+-independent oxidase activity on NAD(P)H
-
-
?
additional information
?
-
-
Mn2+-independent oxidase activity on NAD(P)H
-
-
?
additional information
?
-
-
Mn2+-dependent and Mn2+-independent peroxidase activities when tested on the phenolic substrates 2,6-dimethoxyphenol, 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate, guaiacol and syringaldazine, more rapid oxidation in presence of Mn2+
-
-
?
additional information
?
-
-
in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
?
additional information
?
-
-
Mn2+-independent oxidase activity on NAD(P)H
-
-
?
additional information
?
-
-
in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
?
additional information
?
-
-
Mn2+-independent oxidase activity on NAD(P)H
-
-
?
additional information
?
-
Pseudolagarobasidium sp. PP17-33
-
MnP activity is determined by monitoring the oxidation of 2,6-dimethoxyphenol (DMP) as the oxidation of Mn2+ to Mn3+ by following the formation of the Mn3+-tartrate complex at 469 nm
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-
-
additional information
?
-
-
the enzyme efficiently decolorized azo dyes such as Congo Red, Orange G and Orange IV
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-
?
additional information
?
-
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the enzyme efficiently decolorized azo dyes such as Congo Red, Orange G and Orange IV
-
-
?
additional information
?
-
-
MnP oxidizes nitroaromatic compounds
-
-
?
additional information
?
-
-
the enzyme is essential for lignin degradation
-
-
?
additional information
?
-
-
the enzyme is essential for lignin degradation
-
-
?
additional information
?
-
-
the enzyme is essential for lignin degradation
-
-
?
additional information
?
-
-
the enzyme is essential for lignin degradation
-
-
?
additional information
?
-
-
lingnin containing agricultural waste, like almond shells, hazelnut husks, clover straw, sunflower stems and hazelnut cobs are used as substrate for submerged cultures
-
-
?
additional information
?
-
-
the enzyme is essential for lignin degradation
-
-
?
additional information
?
-
-
no oxidation of veratryl alcohol
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-
?
