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
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1.11.1.13
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lignin
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laccase
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ligninolytic
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phanerochaete
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chrysosporium
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white-rot
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basidiomycete
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decolor
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peroxidases
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pleurotus
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lignin-degrading
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trametes
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versicolor
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veratryl
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ostreatus
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straw
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mniii
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lignocellulosic
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bjerkandera
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sordida
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lignocellulolytic
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remazol
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subvermispora
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lacteus
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eryngii
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irpex
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lignin-modifying
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kraft
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sawdust
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phlebia
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adusta
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ceriporiopsis
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1-hydroxybenzotriazole
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nutrition
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lignocellulose-degrading
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ligninase
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sajor-caju
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wood-rotting
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dye-decolorizing
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tigrinus
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mnso4
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biosorption
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delignification
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delignified
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biobleaching
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degradation
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synthesis
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lentinula
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biotreatment
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non-phenolic
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industry
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decolourisation
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2,6-dimethoxyphenol
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paper production
-
low-nitrogen
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environmental protection
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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
results (
results (pH Stability
pH Stability on EC 1.11.1.13 - manganese peroxidase
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pH STABILITY 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3 - 7.5
purified enzyme, 30°C, full stability at pH 4.5, below 10% activity remaining at pH 3.0 and pH 7.5, 90% at pH 4.0, 80% at pH 5.0, and 30% at pH 6.0
765693
3.5 - 4.7
over 50% of maximal activity remains, recombinant enzyme, pH stability profile, overview
764089
3.5 - 5.5
-
the enzyme shows a half-life of 8.8 h at pH 3.5, the half-lives of MnP activity at pH 4.5, 5.0, and 5.5 are 89.5, 99, and 101 h, respectively
699016
3.5 - 7.5
purified recombinant refolded His6-tagged enzyme retaining 75% of maximal activity within this range
763871
4.5
8
-
recombinant MnP: inactivation within 1 min, native MnP: inactivation within 15 min, A48C/A63C double mutant MnP: 1 h, 80% loss of activity
439853
additional information
3
recombinant wild-type enzyme retains 26% activity after 24 h, while mutant A172W/K168V shows increased stability and retains 54% activity after 24 h, measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate
764473
4.5
-
recombinant MnP, native MnP and A48C/A63C double mutant MnP are stable
439853
4.5
-
in supernatant from pH 4.5 fermentations, 25% of activity of the recombinant enzyme is lost during the first 6 h, and another 25% decrease occurrs in the following 18 h. A much higher rate of loss of recombinant enzyme activity is observed in whole pH 4.5 culture, from which the yeast cells are not removed via centrifugation, than in either of the cell-free supernatants. The rate of loss of rMnP activity in pH 4.5 bioreactor cultures and culture supernatant is higher in samples obtained after 72 h of fermentation than in samples taken after 48 h
684525
6
recombinant wild-type enzyme retains 38% activity after 24 h, while mutant A172W/K168V shows increased stability and retains 72% activity after 24 h, measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate
764473
6
-
native and A48C/A63C double mutant MnP: 1 h, less than 40% loss of activity
439853
6
-
recombinant MnP produced by Pichia pastoris alphaMnP1-1 in pH 6 fed-batch fermentations is not stable in pure pH 6.0 buffers. In 0.01 M potassium phosphate buffer, activity of the recombinant enzyme decreases by 25% in 4 h. Half-lives of 6.7, 3.4, and 0.4 h for 0.01 M phosphate, 0.1 M phosphate, and 0.01 M sodium citrate buffers, respectively. In culture supernatants obtained from pH 6.0 bioreactor fermentations, the recombinant enzyme is stable for up to 6 h before a measurable loss of activity occurrs, and only 25% of the initial activity is lost after 24 h incubation
684525
7
-
native MnP: 1 h, 80% loss of activity, A48C/A63C double mutant MnP: 1 h, 60% loss of activity
439853
additional information
-
polyethylene glycol-modified enzyme shows greater stability to lower pH than native enzyme
439841
additional information
-
recombinant MnP is more sensitive than native MnP as a result of lack of glycosylation
439853
