Information on EC 1.11.1.13 - manganese peroxidase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
1.11.1.13
-
RECOMMENDED NAME
GeneOntology No.
manganese peroxidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
show the reaction diagram
mechanism; shows properties of a peroxidase and an oxidase
-
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
show the reaction diagram
kinetic mechanism
-
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
show the reaction diagram
ping-pong mechanism
-
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
show the reaction diagram
mechanism; ping-pong mechanism
-
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
show the reaction diagram
mechanism
-
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
show the reaction diagram
mechanism
-
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
show the reaction diagram
mechanism
Phanerochaete chrysosporium BKM-F 1767, Phanerochaete chrysosporium BKM-F-1767
-
-
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
show the reaction diagram
shows properties of a peroxidase and an oxidase
Phanerochaete chrysosporium BKM-F 1767, Phanerochaete chrysosporium BKM-F-1767
-
-
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
show the reaction diagram
mechanism; mechanism; ping-pong mechanism
Phanerochaete chrysosporium OGC101, Phanerochaete chrysosporium VKM F-1767
-
-
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
show the reaction diagram
mechanism
-
-
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidation
-
-
oxidation
-
-
oxidation
-
-
oxidation
-
-
oxidation
Ceriporiopsis subvermispora FP-105752, Lentinula edodes SR-1, Lentinus tigrinus 577.79, Lentinus tigrinus CBS 577.79, Trametes ochracea 1215, Trichaptum biforme 117
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
reduction
-
-
reduction
-
-
reduction
-
-
reduction
-
-
reduction
Ceriporiopsis subvermispora FP-105752, Lentinula edodes SR-1, Lentinus tigrinus 577.79, Lentinus tigrinus CBS 577.79, Trametes ochracea 1215, Trichaptum biforme 117
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
manganese oxidation I
-
SYSTEMATIC NAME
IUBMB Comments
Mn(II):hydrogen-peroxide oxidoreductase
A hemoprotein. Involved in the oxidative degradation of lignin in white rot basidiomycetes.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hybrid Mn-peroxidase
-
-
hybrid Mn-peroxidase
Lentinus tigrinus 8/18
-
-
-
LeMnP2
B5U990
-
LeMnP2
Lentinula edodes SR-1
B5U990
-
-
manganese peroxidase
-
-
manganese peroxidase
Abortiporus biennis ECN 100601
-
-
-
manganese peroxidase
Agaricus sp., Agrocybe aegerita, Agrocybe sp. 1, Agrocybe sp. 2
-
-
manganese peroxidase
-
-
manganese peroxidase
-
-
manganese peroxidase
-
-
manganese peroxidase
-
-
manganese peroxidase
Clitocybe sp., Coprinopsis atramentaria, Cortinarius sp. 1, Cortinarius sp. 2
-
-
manganese peroxidase
Cortinarius sp. 2 ECN 100602
-
-
-
manganese peroxidase
-
-
manganese peroxidase
-
-
manganese peroxidase
Ganoderma carnosum ECN 100603
-
-
-
manganese peroxidase
Inocybe lacera, Inocybe longicystis, Lactarius deliciosus
-
-
manganese peroxidase
Lactarius deliciosus ECN 100604
-
-
-
manganese peroxidase
-
-
manganese peroxidase
B5U990
-
manganese peroxidase
Lentinula edodes SR-1
B5U990
-
-
manganese peroxidase
-
-
manganese peroxidase
Lentinus tigrinus 577.79, Lentinus tigrinus CBS 577.79
-
-
-
manganese peroxidase
Lepiota naucina, Lepiota sp. 1, Lepiota sp. 2, Lepista nuda
-
-
manganese peroxidase
Lepista nuda ECN 100605
-
-
-
manganese peroxidase
Leptonia lazunila, Lyophyllum subglobisporium
-
-
manganese peroxidase
Lyophyllum subglobisporium ECN 100606
-
-
-
manganese peroxidase
-
-
manganese peroxidase
-
-
manganese peroxidase
-
-
manganese peroxidase
Pleurotus ostreatus ECN 100607
-
-
-
manganese peroxidase
-
-
manganese peroxidase
Ramaria stricta ECN 100608
-
-
-
manganese peroxidase
-
-
manganese peroxidase
-
-
manganese peroxidase
-
-
manganese peroxidase
Trametes ochracea 1215
-
-
-
manganese peroxidase
-
-
manganese peroxidase
-
-
manganese peroxidase
Trametes versicolor ECN 100609
-
-
-
manganese peroxidase
-
-
manganese peroxidase
Trichaptum biforme 117
-
-
-
manganese peroxidase
Volvariella sp.
-
-
manganese-dependent peroxidase
-
-
manganese-dependent peroxidase
-
-
manganese-dependent peroxidase
-
-
manganese-dependent peroxidase
Ceriporiopsis subvermispora FP-105752
-
-
-
manganese-dependent peroxidase
-
-
manganese-dependent peroxidase
-
-
manganese-dependent peroxidase
-
-
manganese-dependent peroxidase
-
-
Mn-dependent (NADH-oxidizing) peroxidase
-
-
-
-
Mn2+: hydrogen peroxide oxidoreductase
-
-
Mn2+: hydrogen peroxide oxidoreductase
Lentinus tigrinus 577.79, Lentinus tigrinus CBS 577.79
-
-
-
Mn2+:hydrogen peroxide oxidoreductase
-
-
Mn2+:hydrogen peroxide oxidoreductase
Lentinus tigrinus 577.79, Lentinus tigrinus CBS 577.79
-
-
-
MnP
-
-
-
-
MnP
Inocutis jamaicensis MVHC11379
-
-
-
MnP
B5U990
-
MnP
Lentinula edodes SR-1
B5U990
-
-
MnP
Trametes ochracea 1215
-
-
-
MnP
Trichaptum biforme 117
-
-
-
MnP
Trichophyton rubrum LSK-27
-
-
-
MnP II
Lentinus tigrinus 577.79, Lentinus tigrinus CBS 577.79
-
-
-
MnP-GY
-
isoenzyme synthesized in glucose-yeast extract medium has VTCATGQTTANE at the N-terminus
MnP-PGY
-
isoenzyme synthesized in peptone-glucose-yeast extract medium has ATCADGRTTANA at the N-terminus
MP
-
-
-
-
multifunctional manganese peroxidase
-
-
Nf b19 MNP2
Nematoloma frowardii
Q70LM3
-
Nf b19 MNP2
Nematoloma frowardii b19
Q70LM3
-
-
peroxidase, manganese
-
-
-
-
peroxidase-M2
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
114995-15-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain ECN 100601
-
-
Manually annotated by BRENDA team
Abortiporus biennis ECN 100601
strain ECN 100601
-
-
Manually annotated by BRENDA team
MnP1 and MnP2, ligninolytic fungus
-
-
Manually annotated by BRENDA team
Agaricus sp.
-
-
-
Manually annotated by BRENDA team
strain TM 70.84, 2 isoenzymes
-
-
Manually annotated by BRENDA team
Agrocybe praecox TM 70.84
strain TM 70.84, 2 isoenzymes
-
-
Manually annotated by BRENDA team
Agrocybe sp. 1
-
-
-
Manually annotated by BRENDA team
Agrocybe sp. 2
-
-
-
Manually annotated by BRENDA team
Auricularia sp.
strain M37
-
-
Manually annotated by BRENDA team
Auricularia sp. M37
strain M37
-
-
Manually annotated by BRENDA team
strain 90-41, white rot fungus
-
-
Manually annotated by BRENDA team
strain UAMH 8258
-
-
Manually annotated by BRENDA team
Bjerkandera adusta 90-41
strain 90-41, white rot fungus
-
-
Manually annotated by BRENDA team
Bjerkandera adusta UAMH
strain UAMH 8258
-
-
Manually annotated by BRENDA team
Bjerkandera sp.
-
-
-
Manually annotated by BRENDA team
Bjerkandera sp.
strain BOS55
-
-
Manually annotated by BRENDA team
Bjerkandera sp.
strain BOS55, 2 isoenzymes: BOS1 and BOS2
-
-
Manually annotated by BRENDA team
Bjerkandera sp. BOS55
strain BOS55
-
-
Manually annotated by BRENDA team
Bjerkandera sp. BOS55
strain BOS55, 2 isoenzymes: BOS1 and BOS2
-
-
Manually annotated by BRENDA team
strain FP-105752
-
-
Manually annotated by BRENDA team
up to 11 isoenzymes
-
-
Manually annotated by BRENDA team
white rot fungus, strains L-14807, L-15225, FP-104027, FP-90031-sp, FP-105752
-
-
Manually annotated by BRENDA team
Ceriporiopsis subvermispora FP-105752
strain FP-105752
-
-
Manually annotated by BRENDA team
Clitocybe sp.
-
-
-
Manually annotated by BRENDA team
Clitocybula dusenii
-
-
-
Manually annotated by BRENDA team
Clitocybula dusenii
strain b11, agaric white rot basidomycete
-
-
Manually annotated by BRENDA team
Clitocybula dusenii b11
strain b11, agaric white rot basidomycete
-
-
Manually annotated by BRENDA team
strain 146
-
-
Manually annotated by BRENDA team
Coriolopsis trogii 146
strain 146
-
-
Manually annotated by BRENDA team
Coriolus pruinosum
-
-
-
Manually annotated by BRENDA team
Cortinarius sp. 1
-
-
-
Manually annotated by BRENDA team
Cortinarius sp. 2
strain ECN 100602
-
-
Manually annotated by BRENDA team
Cortinarius sp. 2 ECN 100602
strain ECN 100602
-
-
Manually annotated by BRENDA team
Deuteromycotina sp.
-
-
-
Manually annotated by BRENDA team
Deuteromycotina sp.
fungi IZU-154, FERM BP-1859, hyperlignolytic fungus IZU-154, belongs to the family Deuteromycotina and is deposited as the strain name of NK-1148, 4 isoenzymes
-
-
Manually annotated by BRENDA team
strain CBS 432.34, 2 isoenzymes: MnP1 and MnP2, syn. Polyporus anceps; white rot fungus
-
-
Manually annotated by BRENDA team
white rot fungus
-
-
Manually annotated by BRENDA team
Dichomitus squalens CBS 432.34
strain CBS 432.34, 2 isoenzymes: MnP1 and MnP2, syn. Polyporus anceps
-
-
Manually annotated by BRENDA team
syn. Irpex
-
-
Manually annotated by BRENDA team
strain 649. No activity in strain 938
-
-
Manually annotated by BRENDA team
strain 845
-
-
Manually annotated by BRENDA team
Ganoderma adspersum 845
strain 845
-
-
Manually annotated by BRENDA team
strain ECN 100603
-
-
Manually annotated by BRENDA team
Ganoderma carnosum ECN 100603
strain ECN 100603
-
-
Manually annotated by BRENDA team
strain 447
-
-
Manually annotated by BRENDA team
Ganoderma lucidum 447
strain 447
-
-
Manually annotated by BRENDA team
Inocutis jamaicensis MVHC11379
-
-
-
Manually annotated by BRENDA team
Inocybe longicystis
-
-
-
Manually annotated by BRENDA team
strain ECN 100604
-
-
Manually annotated by BRENDA team
Lactarius deliciosus ECN 100604
strain ECN 100604
-
-
Manually annotated by BRENDA team
dikaryotic strain TMI 800, protein complex containing MnP, laccase and beta-glucosidase activities; white rot basidomycete, produces edible shiitake mushroom
-
-
Manually annotated by BRENDA team
strain SR-1
UniProt
Manually annotated by BRENDA team
syn. Lentinus edodes, heterodikaryon strain 861; white rot basidomycete, produces edible shiitake mushroom
-
-
Manually annotated by BRENDA team
Lentinula edodes SR-1
strain SR-1
UniProt
Manually annotated by BRENDA team
white rot fungus, strain MUCL 29757
-
-
Manually annotated by BRENDA team
; strain 577.79
-
-
Manually annotated by BRENDA team
Lentinus tigrinus 577.79
strain 577.79
-
-
Manually annotated by BRENDA team
Lentinus tigrinus 8/18
8/18
-
-
Manually annotated by BRENDA team
Lentinus tigrinus CBS 577.79
-
-
-
Manually annotated by BRENDA team
Lepiota naucina
-
-
-
Manually annotated by BRENDA team
Lepiota sp. 1
-
-
-
Manually annotated by BRENDA team
Lepiota sp. 2
-
-
-
Manually annotated by BRENDA team
strain ECN 100605
-
-
Manually annotated by BRENDA team
Lepista nuda ECN 100605
strain ECN 100605
-
-
Manually annotated by BRENDA team
Leptonia lazunila
-
-
-
Manually annotated by BRENDA team
Lyophyllum subglobisporium
strain ECN 100606
-
-
Manually annotated by BRENDA team
Lyophyllum subglobisporium ECN 100606
strain ECN 100606
-
-
Manually annotated by BRENDA team
Merulius sp.
strain M15
-
-
Manually annotated by BRENDA team
Merulius sp. M15
strain M15
-
-
Manually annotated by BRENDA team
Nematoloma frowardii
-
-
-
Manually annotated by BRENDA team
Nematoloma frowardii
precursor. Molecular characterization of the basidiomycete isolate Nematoloma frowardii b19 and its manganese peroxidase places the fungus in the corticioid genus Phlebia
SwissProt
Manually annotated by BRENDA team
Nematoloma frowardii
syn. Hypholoma, strain b19, agaric white rot basidomycete
-
-
Manually annotated by BRENDA team
Nematoloma frowardii b19
precursor. Molecular characterization of the basidiomycete isolate Nematoloma frowardii b19 and its manganese peroxidase places the fungus in the corticioid genus Phlebia
SwissProt
Manually annotated by BRENDA team
strain 174
-
-
Manually annotated by BRENDA team
Omphalotus olearius 174
strain 174
-
-
Manually annotated by BRENDA team
3 isoenzymes: PCH4, PCH5, PCH6; strain VKM F-1767
-
-
Manually annotated by BRENDA team
auxotrophic strain OGC107-1; MnP1; strain OGC101
-
-
Manually annotated by BRENDA team
auxotrophic strain OGC107-1; MnP1; strain OGC101; white rot basidomycete
-
-
Manually annotated by BRENDA team
isoenzymes H3, H4 and H5; isozyme profile depends on type of nutrient limitation and growth phase: no H5 in C-limited cultures, manganese increases H3-production; overproducing strain PSBL-1; strain BKM-F 1767; white rot basidomycete
-
-
Manually annotated by BRENDA team
isoenzymes H3, H4 and H5; overproducing strain PSBL-1
-
-
Manually annotated by BRENDA team
isoenzymes H3, H4, H5 and H9 in acetate-cultures; strain BKM-F 1767
-
-
Manually annotated by BRENDA team
MnP exists as several closely related isoenzymes; strain OGC101; white rot basidomycete
-
-
Manually annotated by BRENDA team
MnP exists at 6 different isoenzymes; strain BKM-F 1767
-
-
Manually annotated by BRENDA team
MnP1; strain OGC101; white rot basidomycete
-
-
Manually annotated by BRENDA team
MnP2; strain ATCC 64314
Uniprot
Manually annotated by BRENDA team
strain ATCC 24725
-
-
Manually annotated by BRENDA team
strain BKM-F 1767; white rot basidomycete
-
-
Manually annotated by BRENDA team
strain ME446; white rot basidomycete
-
-
Manually annotated by BRENDA team
strain OGC101; white rot basidomycete
-
-
Manually annotated by BRENDA team
strain VKM F-1767; white rot basidomycete
-
-
Manually annotated by BRENDA team
Phanerochaete chrysosporium BKM-F 1767
strain BKM-F 1767
-
-
Manually annotated by BRENDA team
Phanerochaete chrysosporium BKM-F-1767
BKM-F-1767
-
-
Manually annotated by BRENDA team
Phanerochaete chrysosporium ME446
strain ME446
-
-
Manually annotated by BRENDA team
Phanerochaete chrysosporium MnP2
MnP2
Uniprot
Manually annotated by BRENDA team
Phanerochaete chrysosporium MZKI B-223
MZKI B-223
-
-
Manually annotated by BRENDA team
Phanerochaete chrysosporium OGC101
strain OGC101
-
-
Manually annotated by BRENDA team
Phanerochaete chrysosporium VKM F-1767
strain VKM F-1767
-
-
Manually annotated by BRENDA team
white rot fungus, syn. Corticium sordidum, strain HHB-8922-sp, 3 isoenzymes: MnPI, MnPII and MnPIII
-
-
Manually annotated by BRENDA team
Phanerochaete sordida YK-624
-
-
-
Manually annotated by BRENDA team
strain 250
-
-
Manually annotated by BRENDA team
Phellinus robustus 250
strain 250
-
-
Manually annotated by BRENDA team
Phellinus trivialis
-
-
-
Manually annotated by BRENDA team
white rot fungus, strain HHB-7030-sp
-
-
Manually annotated by BRENDA team
strain 511
-
-
Manually annotated by BRENDA team
white rot fungus, strain 79
-
-
Manually annotated by BRENDA team
Phlebia radiata 511
strain 511
-
-
Manually annotated by BRENDA team
syn. Merulius
-
-
Manually annotated by BRENDA team
white rot fungus, strain CBS 613.91, 2 isoenzymes: MnP1 and MnP2
-
-
Manually annotated by BRENDA team
importance of media composition in the production of different isoenzymes; strain CBS 411.71; white rot basidomycete, 3 isoenzymes: MnP1, MnP2 and MnP3
-
-
Manually annotated by BRENDA team
strain CBS 411.71
-
-
Manually annotated by BRENDA team
strain ECN 100607
-
-
Manually annotated by BRENDA team
white rot basidomycete, 3 isoenzymes: MnP1, MnP2 and MnP3
-
-
Manually annotated by BRENDA team
Pleurotus ostreatus CBS 411.71
strain CBS 411.71
-
-
Manually annotated by BRENDA team
Pleurotus ostreatus ECN 100607
strain ECN 100607
-
-
Manually annotated by BRENDA team
white rot fungus, strain CBS 507.85
-
-
Manually annotated by BRENDA team
strain ECN 100608
-
-
Manually annotated by BRENDA team
Ramaria stricta ECN 100608
strain ECN 100608
-
-
Manually annotated by BRENDA team
Russula sp.
-
-
-
Manually annotated by BRENDA team
Schizophyllum commune IBL-06
-
-
-
Manually annotated by BRENDA team
Schizophyllum sp.
strain F17
-
-
Manually annotated by BRENDA team
strain F17
-
-
Manually annotated by BRENDA team
strain TM 47-1, 3 isoenzymes: Mn2+-inducible MnP1 and MnP3, partly constitutive MnP2
-
-
Manually annotated by BRENDA team
Stropharia coronilla TM 47-1
strain TM 47-1, 3 isoenzymes: Mn2+-inducible MnP1 and MnP3, partly constitutive MnP2
-
-
Manually annotated by BRENDA team
Stropharia cubensis
-
-
-
Manually annotated by BRENDA team
strain 681
-
-
Manually annotated by BRENDA team
Trametes maxima 681
strain 681
-
-
Manually annotated by BRENDA team
strain 1215
-
-
Manually annotated by BRENDA team
Trametes ochracea 1215
strain 1215
-
-
Manually annotated by BRENDA team
70% degree of identity of 3 studied isozymes; syn. Coriolus versicolor, white rot basidomycete, strain PRL 572, 5 isoenzymes
-
-
Manually annotated by BRENDA team
strain 235, 428 and 775
-
-
Manually annotated by BRENDA team
strain ECN 100609
-
-
Manually annotated by BRENDA team
syn. Coriolus versicolor, white rot basidomycete, strain PRL 572, 5 isoenzymes
-
-
Manually annotated by BRENDA team
Trametes versicolor 235
strain 235, 428 and 775
-
-
Manually annotated by BRENDA team
Trametes versicolor ECN 100609
strain ECN 100609
-
-
Manually annotated by BRENDA team
Trametes zonata
strain 540
-
-
Manually annotated by BRENDA team
Trametes zonata 540
strain 540
-
-
Manually annotated by BRENDA team
strain 117
-
-
Manually annotated by BRENDA team
Trichaptum biforme 117
strain 117
-
-
Manually annotated by BRENDA team
Trichophyton rubrum LSK-27
LSK-27
-
-
Manually annotated by BRENDA team
Volvariella sp.
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
lignin-degrading enzyme
physiological function
Inocutis jamaicensis MVHC11379
-
lignin-degrading enzyme
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 KBr + 2 H+ + H2O2
Br2 + 2 H2O + 2 K+
show the reaction diagram
-
-
-
-
?
2 KI + 2 H+ + H2O2
I2 + 2 H2O + 2 K+
show the reaction diagram
-
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
show the reaction diagram
-
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+ + 2 H+ + H2O2
2 Mn3+ + 2 H2O
show the reaction diagram
Schizophyllum commune, Schizophyllum commune IBL-06
-
-
-
-
?
2 Mn2+ + H2O2 + aflatoxin B1
2 Mn3+ + aflatoxin B1-8,9-dihydrodiol
show the reaction diagram
Phanerochaete sordida, Phanerochaete sordida YK-624
-
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
-
-
?
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid) + H2O2
?
show the reaction diagram
Schizophyllum sp., Schizophyllum sp. F17
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline)-6-sulphonate + H2O2
?
show the reaction diagram
-
reaction with and without Mn2+
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonate) + H2O2
?
show the reaction diagram
Lentinus tigrinus, Lentinus tigrinus 8/18
-
in absence or presence of Mn2+
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + Mn2+ + ?
?
show the reaction diagram
Lentinus tigrinus, Lentinus tigrinus CBS 577.79, Lentinus tigrinus 577.79
-
-
-
-
?
2,2'-azinobis(3-ethylbenzthiazoline)-6-sulfonic acid + H2O2
?
show the reaction diagram
-
-
-
-
?
2,2'-azinobis(3-ethylbenzthiazoline)-6-sulfonic acid + H2O2 + Mn2+
?
show the reaction diagram
-
-
-
-
?
2,4,6-trichlorophenol + H2O2
?
show the reaction diagram
Lentinus tigrinus, Lentinus tigrinus 8/18
-
no oxidation in absence of Mn2+
-
-
?
2,6-dimethoxyphenol + H2O2
?
show the reaction diagram
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
show the reaction diagram
-
-
-
-
-
2,6-dimethoxyphenol + H2O2
?
show the reaction diagram
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
show the reaction diagram
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
show the reaction diagram
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
show the reaction diagram
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
show the reaction diagram
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
show the reaction diagram
Schizophyllum sp.
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
show the reaction diagram
Inocybe lacera, Inocybe longicystis, Lactarius deliciosus, Lepista nuda, Lepiota sp. 1, Lepiota sp. 2, Leptonia lazunila, Lyophyllum subglobisporium, Ramaria stricta, Russula rosacea, Russula sp., Agrocybe sp. 1, Agrocybe sp. 2, Clitocybe sp., Coprinopsis atramentaria, Parasola plicatilis, Cortinarius sp. 1, Cortinarius sp. 2, Ganoderma carnosum, Lepiota naucina, Rhizopogon luteolus, Volvariella sp.
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
show the reaction diagram
-
reaction in absence or in presence of Mn2+
-
-
?
2,6-dimethoxyphenol + H2O2
?
show the reaction diagram
-
reaction in presence of Mn2+
-
-
?
2,6-dimethoxyphenol + H2O2
?
show the reaction diagram
-
the highest relative activity for 2,6-dimethoxyphenol oxidation is observed in the presence of 10 mM malonate
-
-
?
2,6-dimethoxyphenol + H2O2
?
show the reaction diagram
Lactarius deliciosus ECN 100604, Ganoderma carnosum ECN 100603
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
show the reaction diagram
Lentinus tigrinus 8/18
-
reaction in absence or in presence of Mn2+
-
-
?
2,6-dimethoxyphenol + H2O2
?
show the reaction diagram
Pleurotus ostreatus ECN 100607, Cortinarius sp. 2 ECN 100602
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
show the reaction diagram
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
show the reaction diagram
Lyophyllum subglobisporium ECN 100606, Abortiporus biennis ECN 100601, Lepista nuda ECN 100605, Trametes versicolor ECN 100609
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
show the reaction diagram
Lentinus tigrinus CBS 577.79, Lentinus tigrinus 577.79
-
the highest relative activity for 2,6-dimethoxyphenol oxidation is observed in the presence of 10 mM malonate
-
-
?
2,6-dimethoxyphenol + H2O2
?
show the reaction diagram
Ramaria stricta ECN 100608
-
-
-
-
?
2,6-dimethoxyphenol + H2O2 + Mn2+
?
show the reaction diagram
-
-
-
-
?
2,6-dimethoxyphenol + Mn2+ + ?
?
show the reaction diagram
-
-
-
-
?
2-bromonaphthalene + ?
?
show the reaction diagram
-
oxidation in presence of Tween 80
-
-
?
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
show the reaction diagram
-
-
-
-
-
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
show the reaction diagram
Phanerochaete chrysosporium, Phanerochaete chrysosporium BKM-F-1767
-
3-(3-oxo-butyl)-hexa-2,4-dienedioic acid-1-methyl ester is the dominant product
-
-
?
4-aminophenol + H2O2
?
show the reaction diagram
-
reaction in presence of Mn2+
-
-
?
4-methoxyphenol + H2O2
?
show the reaction diagram
-
reaction in presence of Mn2+
-
-
?
acenaphthene + ?
?
show the reaction diagram
-
oxidation in presence of Tween 80
-
-
?
acenaphthylene + ?
?
show the reaction diagram
-
oxidation in presence of Tween 80
-
-
?
alpha-naphthol + H2O2
?
show the reaction diagram
-
reaction in presence of Mn2+
-
-
?
anthracene + ?
?
show the reaction diagram
-
oxidation in presence of Tween 80
-
-
?
benzo[a]anthracene + ?
?
show the reaction diagram
-
oxidation in presence of Tween 80
-
-
?
benzo[a]pyrene + ?
?
show the reaction diagram
-
key enzyme in degradation of benzo[a]pyrene and other polycyclic aromatic hydrocarbons
-
-
?
benzo[a]pyrene + ?
benzo[a]pyrene-1,6-quinone + ?
show the reaction diagram
-
oxidation in presence of Tween 80
-
-
?
benzo[b]fluoroanthrene + ?
?
show the reaction diagram
-
oxidation in presence of Tween 80
-
-
?
benzo[g,h,i]perylene + H2O
?
show the reaction diagram
-
oxidation in presence of Tween 80
-
-
?
bromocresol green + H2O2
?
show the reaction diagram
-
-
-
-
?
bromocresol purple + H2O2
?
show the reaction diagram
-
-
-
-
?
bromophenol blue + H2O2
?
show the reaction diagram
-
-
-
-
?
bromophenol red + H2O2
?
show the reaction diagram
-
-
-
-
?
bromothymol blue + H2O2
?
show the reaction diagram
-
-
-
-
?
catechol + H2O2
?
show the reaction diagram
-
reaction in presence of Mn2+
-
-
?
chrysene + ?
?
show the reaction diagram
-
oxidation in presence of Tween 80
-
-
?
Co2+ + H+ + H2O2
Co3+ + H2O
show the reaction diagram
-
reduction of enzyme compound II, oxidation at 2% the rate of Mn2+ oxidation
-
?
dibenzo[a,h]anthracene + ?
?
show the reaction diagram
-
oxidation in presence of Tween 80
-
-
?
fluoranthene + ?
?
show the reaction diagram
-
oxidation in presence of Tween 80
-
-
?
fluorene + ?
?
show the reaction diagram
-
oxidation in presence of Tween 80
-
-
?
guaiacol + ?
?
show the reaction diagram
Abortiporus biennis, Abortiporus biennis ECN 100601
-
-
-
-
?
guaiacol + H2O2
tetraguaiacol + H2O
show the reaction diagram
-
-
-
-
?
guaiacol + H2O2
?
show the reaction diagram
-
-
-
-
?
guaiacol + H2O2
?
show the reaction diagram
-
-
-
-
?
guaiacol + H2O2
?
show the reaction diagram
-
-
-
-
?
guaiacol + H2O2
?
show the reaction diagram
Schizophyllum sp.
-
-
-
-
?
guaiacol + H2O2
?
show the reaction diagram
Lepista nuda, Lyophyllum subglobisporium, Ramaria stricta, Cortinarius sp. 2, Ganoderma carnosum
-
-
-
-
?
guaiacol + H2O2
?
show the reaction diagram
-
no oxidation in absence of Mn2+
-
-
?
guaiacol + H2O2
?
show the reaction diagram
-
reaction in presence of Mn2+
-
-
?
guaiacol + H2O2
?
show the reaction diagram
Ganoderma carnosum ECN 100603
-
-
-
-
?
guaiacol + H2O2
?
show the reaction diagram
Lentinus tigrinus 8/18
-
no oxidation in absence of Mn2+
-
-
?
guaiacol + H2O2
?
show the reaction diagram
Pleurotus ostreatus ECN 100607, Cortinarius sp. 2 ECN 100602
-
-
-
-
?
guaiacol + H2O2
?
show the reaction diagram
-
-
-
-
?
guaiacol + H2O2
?
show the reaction diagram
Lyophyllum subglobisporium ECN 100606, Lepista nuda ECN 100605, Trametes versicolor ECN 100609
-
-
-
-
?
guaiacol + H2O2
?
show the reaction diagram
Lentinus tigrinus CBS 577.79, Lentinus tigrinus 577.79
-
-
-
-
?
guaiacol + H2O2
?
show the reaction diagram
Ramaria stricta ECN 100608
-
-
-
-
?
guaiacol + H2O2
?
show the reaction diagram
Phanerochaete chrysosporium BKM-F-1767
-
-
-
-
?
guaiacol + H2O2 + Mn2+
?
show the reaction diagram
-
-
-
-
?
guaiacol + Mn2+ + ?
?
show the reaction diagram
-
-
-
-
?
H2O2 + 2,2'-azino-bis(3-ethyl)-benzothiazoline-6-sulfonic acid
H2O + ?
show the reaction diagram
Trichophyton rubrum, Trichophyton rubrum LSK-27
-
oxidized at a faster rate in presence of Mn(II) than in absence of Mn(II)
-
-
?
H2O2 + 2,6-dimethoxyphenol
H2O + ?
show the reaction diagram
Trichophyton rubrum, Trichophyton rubrum LSK-27
-
oxidized at a faster rate in presence of Mn(II) than in absence of Mn(II)
-
-
?
H2O2 + guaiacol
H2O + ?
show the reaction diagram
Trichophyton rubrum, Trichophyton rubrum LSK-27
-
oxidized at a faster rate in presence of Mn(II) than in absence of Mn(II)
-
-
?
H2O2 + Poly R-478
?
show the reaction diagram
-
Mn2+ is required for reaction with Poly R-478 with MnP3, MnP2 depolymerizes the polymeric azo dye,Poly R-478, regardless of the presence of Mn2+, to complete its catalytic cycle
-
-
?
hydroquinone + H2O2
?
show the reaction diagram
-
reaction in absence or in presence of Mn2+
-
-
?
indeno[1,2,3-c,d]pyrene + ?
?
show the reaction diagram
-
oxidation in presence of Tween 80
-
-
?
m-cresol purple + H2O2
?
show the reaction diagram
-
-
-
-
?
Mn2+ + 2,6-dimethoxyphenol + H2O2
?
show the reaction diagram
-
-
-
-
?
Mn2+ + 2,6-dimethoxyphenol + H2O2
?
show the reaction diagram
-
activity assay
-
-
?
Mn2+ + di(2-methylpent-2-enyl) sulfide + H+
Mn3+ + 2,4-dimethylthiophene + 2-methyl-2-pentenal + H2O
show the reaction diagram
-
-
-
-
?
Mn2+ + guaiacol + H2O2
?
show the reaction diagram
Lentinula edodes, Lentinula edodes SR-1
B5U990
activity assay
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Q02567
-
-
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Phlebia brevispora, Deuteromycotina sp.
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Nematoloma frowardii, Clitocybula dusenii
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Clitocybula dusenii
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Schizophyllum sp.
-
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
B5U990
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
Mn3+ oxidizes curcumin
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
Mn3+ oxidizes vanillylideneacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
chelating organic acids facilitate the dissociation of Mn3+ from enzyme, Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
Mn3+ oxidizes phenolic lignin model compounds
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
Mn3+ oxidizes phenolic lignin model compounds
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
Mn3+ oxidizes vanillylacetone
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
Mn3+ oxidizes vanillylacetone
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
Mn3+ oxidizes vanillylacetone
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
Mn3+ oxidizes lignin
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
Mn3+ oxidizes lignin
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Phlebia radiata, Phanerochaete sordida, Nematoloma frowardii
-
-
Mn3+ oxidizes lignin
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Deuteromycotina sp.
-
-
product Mn3+ possibly migrates into polymer molecules, such as lignin, nylon and melanin, and initiates nonspecific oxidation
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
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
show the reaction diagram
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Pleurotus eryngii, Bjerkandera sp.
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Deuteromycotina sp.
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
Mn3+ oxidizes o-dianisidine
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
Mn3+ oxidizes phenol red
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
Mn3+ oxidizes syringaldazine
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
Mn3+ oxidizes amines
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
Mn3+ oxidizes a variety of phenols
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
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
show the reaction diagram
-
-
Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
Mn3+ oxidizes guaiacol
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
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
show the reaction diagram
-
-
the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by Mn2+
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
specifically oxidizes Mn2+
alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
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
show the reaction diagram
-
specifically oxidizes Mn2+
dicarboxylic acids facilitate the dissociation of Mn3+ from enzyme, Mn3+ oxidizes o-phenylenediamine and p-anisidine
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
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
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
specifically oxidizes Mn2+
Mn3+ oxidizes o-dianisidine
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
specifically oxidizes Mn2+
the diffusible product is Mn3+
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
specifically oxidizes Mn2+
Mn3+ oxidizes amines
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
specifically oxidizes Mn2+
Mn3+ oxidizes a variety of phenols
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
specifically oxidizes Mn2+
Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
specifically oxidizes Mn2+
chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
specifically oxidizes Mn2+
Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ complex oxidizes a variety of organic substrates
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
completion of MnP catalytic cycle requires Mn2+
freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes phenolic lignin model compounds
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes phenolic lignin model compounds
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes vanillylacetone
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes syringyl alcohol, syringyl aldehyde, syringic acid, syringaldazine, coniferyl alcohol, sinapic acid
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes vanillyl alcohol
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes 2,6-dimethoxyphenol, Mn3+ oxidizes o-dianisidine
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes phenol red
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
completion of MnP catalytic cycle requires Mn2+
the diffusible product is Mn3+, Mn3+ oxidizes a variety of phenols
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
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
show the reaction diagram
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes guaiacol
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes guaiacol
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes several methoxylated and hydroxylated phenolic compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
oxidation of Mn2+ to Mn3+ at a redox potential of 1.5 V
-
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
Mn3+ oxidizes vanillyl alcohol
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
Mn3+ oxidizes guaiacol
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
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
show the reaction diagram
-
oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
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
show the reaction diagram
-
oxidizes Mn2+ as the best substrate
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
involved in lignin-degradation
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Nematoloma frowardii
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
initial depolymerization of the lignin polymer
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
Mn2+ is a component of woody plant tissues
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Deuteromycotina sp.
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Deuteromycotina sp.
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Nematoloma frowardii
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Nematoloma frowardii
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Clitocybula dusenii
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Clitocybula dusenii
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
important component of lignin degradation system
Mn3+ is produced under lignolytic conditions
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation, the mechanism enables the fungus to oxidize structures within woods which are inaccessible to enzymes
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
acts together with lignin peroxidase in lignin-degradation of white rot fungi
-
-
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
acts together with lignin peroxidase in lignin-degradation of white rot fungi
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
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
show the reaction diagram
-
in absence of H2O2 it may play a role in fungal peroxide production under ligninolytic conditions
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
preferential degradation of lignin in wheat straw
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Merulius sp. M15
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Phanerochaete 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
show the reaction diagram
Phanerochaete 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
show the reaction diagram
Phanerochaete chrysosporium OGC101
-
completion of MnP catalytic cycle requires Mn2+, 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
show the reaction diagram
Phanerochaete 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
show the reaction diagram
Phanerochaete chrysosporium OGC101
-
important component of lignin degradation system
Mn3+ is produced under lignolytic conditions
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Phanerochaete 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
show the reaction diagram
Phanerochaete 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
show the reaction diagram
Phanerochaete 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
show the reaction diagram
Phanerochaete 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
show the reaction diagram
Phanerochaete chrysosporium VKM F-1767
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Phanerochaete 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
show the reaction diagram
Phanerochaete chrysosporium VKM F-1767
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Phanerochaete chrysosporium VKM F-1767
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Bjerkandera sp. BOS55
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Stropharia coronilla TM 47-1
-
-, important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Phanerochaete chrysosporium BKM-F 1767
-
-
-
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Phanerochaete chrysosporium BKM-F 1767
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Phanerochaete 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
show the reaction diagram
Phanerochaete chrysosporium BKM-F 1767
-
-
Mn3+ oxidizes phenolic lignin model compounds, Mn3+ oxidizes vanillylacetone
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Phanerochaete chrysosporium BKM-F 1767
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Phanerochaete chrysosporium BKM-F 1767
-
-
Mn3+ oxidizes curcumin
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Pleurotus ostreatus CBS 411.71
-
oxidizes Mn2+ as the best substrate, involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Pleurotus ostreatus CBS 411.71
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Pleurotus ostreatus CBS 411.71
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Bjerkandera adusta UAMH
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Auricularia sp. M37
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Agrocybe praecox TM 70.84
-
-, important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Clitocybula dusenii b11
-
-, important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Phanerochaete chrysosporium ME446
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Phanerochaete chrysosporium ME446
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Bjerkandera adusta 90-41
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Lentinus tigrinus CBS 577.79, Lentinus tigrinus 577.79
-
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Lentinula edodes SR-1
B5U990
-
-
-
?
Mn2+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
-
?
Mn2+ + H2O2
Mn3+ + H2O
show the reaction diagram
Q02567
-
-
-
?
Mn2+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
-
?
Mn2+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
-
-
Mn2+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
-
?
Mn2+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
-
?
Mn2+ + H2O2
Mn3+ + H2O
show the reaction diagram
Trichophyton rubrum LSK-27
-
-
-
-
?
Mn2+ + hydroquinone
?
show the reaction diagram
-
-
-
-
?
NADH + acetate
NAD+ + ?
show the reaction diagram
-
-
-
-
?
NADH + lactate
NAD+ + ?
show the reaction diagram
-
-
-
-
?
NADH + malate
NAD+ + ?
show the reaction diagram
-
-
-
-
?
NADH + tartrate
NAD+ + ?
show the reaction diagram
-
-
-
-
?
naphthalene + ?
?
show the reaction diagram
-
oxidation in presence of Tween 80
-
-
?
o-cresol red + H2O2
?
show the reaction diagram
-
-
-
-
?
o-dianisidine + H2O2
?
show the reaction diagram
Lentinus tigrinus, Lentinus tigrinus 8/18
-
in absence or in presence of of Mn2+
-
-
?
p-phenylenediamine + H2O2
?
show the reaction diagram
-
in absence or in presence of Mn2+
-
-
?
phenol red
?
show the reaction diagram
-
activity assay
-
-
?
phenol red + H2O2
?
show the reaction diagram
-
-
-
-
?
phenol red + H2O2
?
show the reaction diagram
-
-
-
-
-
phenol red + H2O2
?
show the reaction diagram
-
-
-
-
?
phenol red + H2O2
?
show the reaction diagram
Ganoderma lucidum, Phlebia radiata, Fomes fomentarius, Coriolopsis trogii, Trametes maxima, Ganoderma adspersum, Phellinus robustus, Trametes zonata, Omphalotus olearius, Phellinus robustus 250, Omphalotus olearius 174, Ganoderma adspersum 845, Phlebia radiata 511
-
-
-
-
?
phenol red + H2O2
?
show the reaction diagram
Phanerochaete chrysosporium BKM-F 1767
-
-
-
-
-
phenol red + H2O2
?
show the reaction diagram
Ganoderma lucidum 447, Trametes versicolor 235, Trametes maxima 681, Coriolopsis trogii 146, Trametes zonata 540
-
-
-
-
?
pyrene + ?
?
show the reaction diagram
-
oxidation in presence of Tween 80
-
-
?
pyrogallol + H2O2
?
show the reaction diagram
Lentinus tigrinus, Lentinus tigrinus CBS 577.79, Lentinus tigrinus 577.79
-
-
-
-
?
pyrogallol + H2O2 + Mn2+
?
show the reaction diagram
-
-
-
-
?
pyrogallol + Mn2+ + ?
?
show the reaction diagram
-
-
-
-
?
thymol blue + H2O2
?
show the reaction diagram
-
-
-
-
?
vanillylacetone + H2O2
?
show the reaction diagram
-
-
-
-
-
vanillylacetone + H2O2
?
show the reaction diagram
-
reaction in presence of Mn2+
-
-
?
veratryl alcohol + H2O2
? + H2O
show the reaction diagram
-
-
-
-
-
veratryl alcohol + H2O2
? + H2O
show the reaction diagram
-
reaction in absence of Mn2+
-
-
?
veratryl alcohol + H2O2 + Mn2+
?
show the reaction diagram
-
veratryl alcohol oxidation requires the simultaneous presence of H2O2 and Mn2+
-
-
?
veratryl alcohol + Mn2+ + ?
?
show the reaction diagram
-
-
-
-
?
Mn2+ + methylhydroquinone
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
Deuteromycotina sp., Agrocybe praecox
-
-
-
-
-
additional information
?
-
-
poor substrates: benzoate, benzaldehyde or benzyl alcohol
-
-
-
additional information
?
-
-
enzyme oxidizes non-phenolic lignin-related compounds, including veratryl alcohol
-
-
-
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
?
-
-
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
?
-
-
in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
-
additional information
?
-
-
enzyme is able to oxidatively depolymerize both dimeric lignin-model compounds and milled spruce-wood lignin
-
-
-
additional information
?
-
-
no oxidation of Co2+
-
-
-
additional information
?
-
-
no oxidation of Co2+
-
-
-
additional information
?
-
Bjerkandera sp.
-
Mn-mediated and Mn-independent activity on phenolic and non-phenolic aromatic substrates
-
-
-
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
?
-
-
protein complex containing MnP, laccase and beta-glucosidase
-
-
-
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
?
-
Bjerkandera sp.
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
-
additional information
?
-
-
structural properties
-
-
-
additional information
?
-
Q02567
structural properties
-
-
-
additional information
?
-
-
structural properties
-
-
-
additional information
?
-
Deuteromycotina sp.
-
structural properties
-
-
-
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 4-aminophenol and hydroquinone
-
-
-
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
?
-
Q02567
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
?
-
-
MnP oxidizes synthetic melanoidine
-
-
-
additional information
?
-
-
Mn2+-independent peroxidase activity against phenolic substrates, e.g. phenol red
-
-
-
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
?
-
-
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
?
-
-
no activity with veratryl alcohol
-
-
-
additional information
?
-
-
no activity with veratryl alcohol
-
-
-
additional information
?
-
-
no activity with veratryl alcohol
-
-
-
additional information
?
-
-
no activity with veratryl alcohol
-
-
-
additional information
?
-
-
no activity with veratryl alcohol
-
-
-
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
?
-
Nematoloma frowardii, Clitocybula dusenii
-
MnP oxidizes humic substances
-
-
-
additional information
?
-
-
enzyme oxidizes ferrocyanide
-
-
-
additional information
?
-
-
enzyme oxidizes 3,3,5,5-tetramethylbenzidine
-
-
-
additional information
?
-
-
enzyme oxidizes veratryl alcohol and o-tolidine
-
-
-
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+-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
-
-
-
additional information
?
-
-
Mn2+-independent oxidase activity on NAD(P)H
-
-
-
additional information
?
-
-
Mn-dependent oxidation of phenols requires superoxide anion and H2O2, phenolic hydroxyl group is essential
-
-
-
additional information
?
-
-
no oxidation of Fe2+, Cu2+, Zn2+
-
-
-
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
?
-
-
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
?
-
-
enzyme oxidizes phenol red
-
-
-
additional information
?
-
-
enzyme oxidizes bromide
-
-
-
additional information
?
-
-
MnP oxidizes phenolic and nonphenolic aromatic compounds, e.g. phenol red and veratryl alcohol
-
-
-
additional information
?
-
-
no other metal can substitute Mn2+
-
-
-
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
?
-
Nematoloma frowardii
-
MnP oxidizes chlorophenols and arsenic-containing warefare agents
-
-
-
additional information
?
-
-
MnP oxidizes nitroaromatic compounds
-
-
-
additional information
?
-
-
enzyme oxidizes 2,6-dimethoxyphenol
-
-
-
additional information
?
-
-
enzyme oxidizes 2,6-dimethoxyphenol
-
-
-
additional information
?
-
-
enzyme oxidizes 2,6-dimethoxyphenol
-
-
-
additional information
?
-
-
enzyme oxidizes 2,6-dimethoxyphenol
-
-
-
additional information
?
-
-
enzyme oxidizes the polymeric dyes poly R-481 and poly B-411, 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
?
-
-
no oxidation of Ni2+
-
-
-
additional information
?
-
-
no oxidation of Ni2+
-
-
-
additional information
?
-
-
in presence of H2O2 and Mn2+ the enzyme oxidizes lignin and lignin-model compounds
-
-
-
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
?
-
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADH to NAD+
-
-
-
additional information
?
-
-
direct oxidation of Rnase by MnP2
-
-
-
additional information
?
-
-
no oxidation of veratryl alcohol
-
-
-
additional information
?
-
Schizophyllum sp.
-
the enzyme efficiently decolorized azo dyes such as Congo Red, Orange G and Orange IV
-
-
-
additional information
?
-
-
catalyzes the oxidation of Mn(II) to Mn(III), which in turn can oxidize phenolic substrates
-
-
-
additional information
?
-
-
dye decolorization
-
-
-
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
?
-
Dichomitus squalens CBS 432.34
-
no oxidation of Co2+, enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+, catalytic cycle with oxidized intermediates MnP compound I and II, no activity with veratryl alcohol, no oxidation of Fe2+, Cu2+, Zn2+
-
-
-
additional information
?
-
Phanerochaete chrysosporium OGC101
-
catalytic cycle with oxidized intermediates MnP compound I and II, large substrates have no ready access to the catalytic center, enzyme oxidizes 2,6-dimethoxyphenol
-
-
-
additional information
?
-
Phanerochaete chrysosporium OGC101
-
presence of proximal and distal histidines at the active center
-
-
-
additional information
?
-
Phanerochaete chrysosporium OGC101
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate, 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, enzyme oxidizes ferrocyanide
-
-
-
additional information
?
-
Phanerochaete chrysosporium OGC101
-
enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+, enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate, in absence of H2O2 the enzyme oxidizes Mn-dependently NADH to NAD+, generating H2O2 for oxidizing other substrates, in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+, no other metal can substitute Mn2+
-
-
-
additional information
?
-
Phanerochaete chrysosporium OGC101
-
structural properties, catalytic cycle with oxidized intermediates MnP compound I and II, enzyme oxidizes ferrocyanide, enzyme oxidizes bromide
-
-
-
additional information
?
-
Phanerochaete chrysosporium OGC101
-
catalytic cycle with oxidized intermediates MnP compound I and II, enzyme oxidizes ferrocyanide
-
-
-
additional information
?
-
Phanerochaete chrysosporium OGC101
-
catalytic cycle with oxidized intermediates MnP compound I and II, Mn2+-independent oxidation of small phenolic compounds, such as guaiacol and dimethoxyphenol, rates are greatly reduced compared with the Mn-mediated reaction
-
-
-
additional information
?
-
Phanerochaete chrysosporium VKM F-1767
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
-
additional information
?
-
Phanerochaete chrysosporium VKM F-1767
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate, catalytic cycle with oxidized intermediates MnP compound I and II
-
-
-
additional information
?
-
Phanerochaete chrysosporium VKM F-1767
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol, enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+, no activity with veratryl alcohol
-
-
-
additional information
?
-
-
poor substrates: benzoate, benzaldehyde or benzyl alcohol, enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
-
additional information
?
-
Bjerkandera sp. BOS55
-
Mn-mediated and Mn-independent activity on phenolic and non-phenolic aromatic substrates, Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
-
additional information
?
-
Phanerochaete chrysosporium BKM-F 1767
-
enzyme oxidizes phenol red, in presence of Mn2+ enzyme oxidizes various organic compounds
-
-
-
additional information
?
-
Phanerochaete 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, in presence of H2O2 and Mn2+ the enzyme oxidizes a variety of phenolic compounds, especially vinyl and syringyl side-chain substituted substrates, in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+, in absence of H2O2 the enzyme oxidizes Mn-dependently NADH to NAD+
-
-
-
additional information
?
-
Trichophyton rubrum LSK-27
-
no oxidation of veratryl alcohol
-
-
-
additional information
?
-
Pleurotus ostreatus CBS 411.71
-
in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate, Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol, Mn2+-independent oxidase activity on NAD(P)H
-
-
-
additional information
?
-
Pleurotus ostreatus CBS 411.71
-
in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate, Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol, Mn2+-independent oxidase activity on NAD(P)H
-
-
-
additional information
?
-
-
the enzyme efficiently decolorized azo dyes such as Congo Red, Orange G and Orange IV
-
-
-
additional information
?
-
Bjerkandera adusta UAMH
-
Mn2+-dependent and Mn2+-independent peroxidase activities, substrates: 2,6-dimethoxyphenol, 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate, guaiacol and veratryl alcohol, enzyme oxidizes 4-aminophenol and hydroquinone, enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate, enzyme oxidizes 2,6-dimethoxyphenol
-
-
-
additional information
?
-
Agrocybe praecox TM 70.84
-
in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
-
additional information
?
-
Phanerochaete chrysosporium ME446
-
structural properties
-
-
-
additional information
?
-
Bjerkandera adusta 90-41
-
no activity with veratryl alcohol, 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+
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
benzo[a]pyrene + ?
?
show the reaction diagram
-
key enzyme in degradation of benzo[a]pyrene and other polycyclic aromatic hydrocarbons
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
B5U990
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
-
the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by Mn2+
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
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
show the reaction diagram
-
involved in lignin-degradation
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Nematoloma frowardii
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
initial depolymerization of the lignin polymer
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
Mn2+ is a component of woody plant tissues
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Deuteromycotina sp.
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Deuteromycotina sp.
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Nematoloma frowardii
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Nematoloma frowardii
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Clitocybula dusenii
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Clitocybula dusenii
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
important component of lignin degradation system
Mn3+ is produced under lignolytic conditions
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
involved in lignin-degradation, the mechanism enables the fungus to oxidize structures within woods which are inaccessible to enzymes
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
acts together with lignin peroxidase in lignin-degradation of white rot fungi
-
-
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
acts together with lignin peroxidase in lignin-degradation of white rot fungi
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
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
show the reaction diagram
-
in absence of H2O2 it may play a role in fungal peroxide production under ligninolytic conditions
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
-
preferential degradation of lignin in wheat straw
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Phanerochaete chrysosporium OGC101
-
important component of lignin degradation system
Mn3+ is produced under lignolytic conditions
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Phanerochaete chrysosporium VKM F-1767
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Phanerochaete chrysosporium VKM F-1767
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Stropharia coronilla TM 47-1
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Phanerochaete chrysosporium BKM-F 1767
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Phanerochaete chrysosporium BKM-F 1767
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Pleurotus ostreatus CBS 411.71
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Pleurotus ostreatus CBS 411.71
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Agrocybe praecox TM 70.84
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Clitocybula dusenii b11
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Phanerochaete chrysosporium ME446
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Lentinus tigrinus CBS 577.79, Lentinus tigrinus 577.79
-
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
show the reaction diagram
Lentinula edodes SR-1
B5U990
-
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
heme
-
heme protein containing protoporphyrin IX, 0.7 heme per enzyme molecule, iron ions are coordinated with prosthetic groups as high-spin ferriheme complexes
heme
-
iron protoporphyrin IX prosthetic group
heme
-
heme component at the active site
heme
-
heme protein; iron protoporphyrin IX prosthetic group
heme
-
enzyme contains a pentacoordinated, essentially high-spin ferric heme
heme
-
enzyme has a single manganese binding site near the heme; one iron protoporphyrin IX prosthetic group per enzyme molecule
heme
-
enzyme contains prosthetic heme, substrates are oxidized via delta-meso heme edge of the enzyme
heme
-
heme-iron protein; one iron protoporphyrin IX prosthetic group per enzyme molecule
heme
-
heme protein; one iron protoporphyrin IX prosthetic group per enzyme molecule
heme
-
one iron protoporphyrin IX prosthetic group per enzyme molecule
heme
-
heme iron of the native enzyme is ferric, high-spin and pentacoordinate with a proximal histidine ligand, important catalytic residues in the heme pocket are conserved: proximal His-173 and Asp-242, distal His-46, Arg-42, Asn-80 and Glu-74
heme
-
iron protoporphyrin IX prosthetic group
heme
-
enzyme contains a pentacoordinated, essentially high-spin ferric heme; one iron protoporphyrin IX prosthetic group per enzyme molecule
heme
-
one mol heme per mol of enzyme
heme
-
heme environment, Phe-190 plays a critical role in stabilizing the heme environment, it acts as a steric barrier that protects the heme from reducing agents, increasing pH from 5.0 to 8.5 induces a Fe3+ high- to a low-spin transition
heme
-
enzyme contains a pentacoordinated, essentially high-spin ferric heme; heme protein
heme
-
important cofactor for production of active recombinant enzyme. Amendment of yeast cultures with heme increases concentrations of active recombinant enzyme
heme
-
the heme content is 0.96 mol per mole of the enzyme
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
Deuteromycotina sp., Phanerochaete chrysosporium
-
MnP has 2 structural calcium ions
Ca2+
-
MnP calcium binding site, calcium content: 4 mol per mol of native MnP, 2 mol per mol of recombinant and A48C/A63C double mutant MnP, calcium decreases the rate of thermal inactivation
Cd2+
-
Cd2+ exhibizs octahedral, hexacoordinate ligation geom,etry similar to that of Mn2+. Cd2+ also binds to a putative second weak metal-binding site with tetrahedral geometry at the C-terminus of the protein
Cu2+
-
1-4 mM, about 20% stimulation
Manganese
-
-
Manganese
-
-
Manganese
-
-
Manganese
-
-
Mn2+
-
increases MnP activity, stimulates MnP production
Mn2+
-
Mn2+ causes a concentration-dependent increase in total enzyme activity, little or no activity in absence of Mn2+
Mn2+
-
stimulates oxidation of 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate and o-phenylenediamine
Mn2+
-
0.2 mM stimulates conversion of benzo[a]pyrene
Mn2+
-
required for reaction with Poly R-478 with MnP3
Mn2+
-
required for oxidation of guaiacol and 2,4,6-trichlorophenol
Mn2+
-
2,2'-azino-bis(3-ethyl-benzothiazoline)-6-sulfonic acid, guaiacol and 2,6-dimethoxyphenol are oxidized at a faster rate in presence of Mn(II) than in absence of Mn(II)
Mn2+
-
activates
Mn2+
-
the proposed role of Mn2+ chelators in the enzyme mechanism is to release Mn3+ from the enzyme
Mn2+
-
required for oxidation of 2,6-dimethoxyphenol, 4-methoxyphenol, 4-aminophenol, guaiacol, alpha-naphthol, vanillylacetone and catechol
Mn2+
-
veratryl alcohol oxidation requires the simultaneous presence of H2O2 and Mn2+
Mn2+
Abortiporus biennis, Agaricus sp., Agrocybe aegerita, Agrocybe sp. 1, Agrocybe sp. 2, Clitocybe sp., Coprinopsis atramentaria, Cortinarius sp. 1, Cortinarius sp. 2, Ganoderma carnosum, Inocybe lacera, Inocybe longicystis, Lactarius deliciosus, Lepiota naucina, Lepiota sp. 1, Lepiota sp. 2, Lepista nuda, Leptonia lazunila, Lyophyllum subglobisporium, Parasola plicatilis
-
-
Sm3+
-
coordination of Sm(III) at the Mn-binding site is octacoordinate. The reversible binding of Sm(III) may be a useful model for the reversible binding of Mn(III) to the enzyme, which is too unstable to allow similar examination
Mn2+
-
1-4 mM, about 20% stimulation
additional information
-
MnP synthesis depends on Mn2+ in growth medium
additional information
-
11 ppm Mn2+ in growth medium induces MnP synthesis
additional information
-
expression of MnP isoenzymes is dependent on the presence of Mn, expression rather than enzymatic activity is regulated by Mn
additional information
-
-
additional information
-
MnP is induced by Mn2+
additional information
Clitocybula dusenii, Nematoloma frowardii
-
MnP is induced by Mn2+
additional information
-
MnP is induced by Mn2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
inhibits competitive Mn(III)-malonate formation
2-mercaptoethanol
-
5 mM, about 60% inhibition
acetate
-
1 mM, 58% inhibition
Ag+
Schizophyllum sp.
-
-
AgNO3
-
5 mM, about 60% inhibition
ascorbic acid
-
0.1 mM, 100% inhibition
ascorbic acid
-
2 mM, complete inhibition
beta-mercaptoethanol
-
2 mM, complete inhibition
CaCl2
-
5 mM, about 20% inhibition
catalase
-
inhibits oxidation of vanillylacetone completely, oxidation of NADH at high concentrations partially
-
catalase
-
inhibits oxidation of NADH in reaction mixture containing alpha-hydroxy acid
-
Cd2+
-
competitive inhibitor to Mn2+, uncompetitive to H2O2, reversibly inhibits oxidation of Mn2+ and Mn3+-mediated oxidation of 2,6-dimethoxyphenol, but not oxidation of phenols in absence of Mn2+, Cd2+ inhibits reduction of compound I and II by Mn2+ at pH 4.5 and binds at the Mn2+-binding site, kinetics of inhibition
cellobionate
-
inhibits competitive Mn(III)-malonate formation
Co2+
-
0.1 mM, 67% inhibition
Co2+
-
at concentrations below 4 mM in presence of H2O2 competitive inhibitor to Mn2+, slightly stimulates NaN3 or alkylhydrazine inactivation
Co2+
-
competitive inhibitor to Mn2+
Cu2+
-
0.1 mM, 62% inhibition
Cu2+
-
inhibits by catalyzing the H2O2-dependent reduction of Mn3+
cysteine
-
decolorization of bromocresol purple
diphosphate
-
inhibits phenol red oxidation to 50%, NADH oxidation at high concentrations partially
diphosphate
-
inhibits oxidation of 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
EDTA
-
decolorization of bromocresol purple
EDTA
Schizophyllum sp.
-
partial inhibition
EDTA
-
5 mM, about 40% inhibition
ethylhydrazine
-
time-dependent inactivation via delta-meso-ethylheme adduct at pH 7.0, slightly stimulated by Co2+
Eu3+
-
competitive inhibitor to Mn2+
Fe2+
-
0.1 mM, 77% inhibition
-
Fe2+
Schizophyllum sp.
-
no significant effect at 0.1 mM, inhibition at 1.0 mM concentration
-
Fe3+
-
0.1 mM, 34% inhibition
-
Fe3+
Schizophyllum sp.
-
no significant effect at 0.1 mM, inhibition at 1.0 mM concentration
-
H2O2
-
inactivation fits a first-order decay, rapid initial inactivation step
H2O2
-
inhibitory at high concentrations, phenol red is the most sensitive, vanillylacetone the least sensitive substrate to inhibition, Mn2+ protects against inhibition
H2O2
Q02567
1 mM, complete, irreversible inactivation of wild-type enzyme correlated with the production of methionine sulfoxide, full activity can be retained by engineering Asn-81, which might have conformational changes due to the environment of the pocket, to a non-bulky and non-oxidizable Ser
H2O2
-
25% inhibition at 0.5 mM, 75% inhibition at 1 mM
methylhydrazine
-
slow inactivation in presence of H2O2, concentration- and time-dependent, slightly stimulated by Co2+
Mn2+
-
inhibits oxidation of phenol red
N-ethyl-5-phenylisoxazolium 3'-sulfonate
-
1 mM, 28% inhibition
Na+
Schizophyllum sp.
-
no significant effect at 1.0 mM, inhibition at 10 mM concentration
NaN3
-
complete inactivation within 2 min in presence of H2O2, accompanied by azidyl radical formation, prosthetic heme is converted to meso-azido adduct which is more rapidly oxidized by H2O2 than prosthetic heme, 2 equivalents of azide are oxidized before the enzyme molecule is inactivated, inactivation is slightly stimulated by Co2+
NaN3
-
decolorization of bromocresol purple
NaN3
-
2 mM, complete inhibition
NaN3
Schizophyllum sp.
-
partial inhibition
Nitrilotriacetate
-
inhibits competitive Mn(III)-malonate formation
Pb(NO3)2
-
5 mM, about 80% inhibition
Pc reducer
-
the activity of manganese peroxidase is inhibited by Pc reducer at concentrations higher than 0.2 mg/ml
-
phenyldiazene
-
concentration-dependent inactivation
phenylhydrazine
-
rapid inactivation, concentration-dependent, no heme adducts detectable, inactivation is slightly stimulated by Co2+
SDS
Schizophyllum sp.
-
partial inhibition
Sm3+
-
competitive inhibitor to Mn2+
Sodium metavanadate
-
partially inhibits only peroxidase activity against veratryl alcohol
Superoxide dismutase
-
inhibits oxidation of vanillylacetone by about 80%
-
Superoxide dismutase
-
inhibits phenol red oxidation to 50%, vanillylacetone oxidation to 90%, NADH oxidation at high concentrations partially
-
Superoxide dismutase
-
inhibits oxidation of NADH in reaction mixture containing acetate
-
tetramethylethylenediamine
-
5 mM, about 50% inhibition
-
Thiourea
Schizophyllum sp.
-
partial inhibition
Mn2+
-
partial inhibition of oxidation of NAD(P)H at the beginning of the reaction, NADH: 0.1 mM Mn2+ causes 97% inhibition of MP1 and 72% inhibition of MP2
additional information
-
not inhibited by 5% ethanol, v/v; not inhibited by salicylic acid
-
additional information
-
not inhibited by sodium diphosphate, mannitol, Mn3+-chelators
-
additional information
-
not inhibited by succinate
-
additional information
-
not inhibited by 0.1 mM Cu2+, Co2+ or salicylic acid; not inhibited by salicylic acid
-
additional information
-
Mn2+ inhibits MnP synthesis
-
additional information
-
not inhibited by Ca2+ and Mg2+
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
slightly activates, chelates Mn3+
alpha-hydroxy acid
-
activates by chelating and stabilizing Mn3+ rather than activating the enzyme
alpha-hydroxy acid
-
stimulates by stabilizing Mn3+
alpha-hydroxy acid
-
stimulates by chelating Mn3+ and stabilizing its high redox potential
alpha-hydroxy acid
-
activates by chelating and stabilizing Mn3+ rather than activating the enzyme
cellobionate
-
activates, chelates Mn3+
citrate
-
activates, stabilizes Mn3+ in aqueous solution with a relatively high redox potential
citrate
-
activates, forms stable Mn3+ complex
citrate
-
stimulates by chelating Mn3+ and stabilizing its high redox potential
citrate
-
activates, chelates and stabilizes Mn3+
copper
-
ACE1 transcription factor-mediated expression of genes encoding manganese peroxidase
diphosphate
-
stimulates by chelating and stabilizing Mn3+
diphosphate
-
less activation than by lactate or malonate
diphosphate
-
diphosphate proves to be the worst chelator, leading to a specific activity about 4.6% of that obtained with tartrate
dithiothreitol
-
greatly enhances the oxidation of verartryl alcohol, lignin-model compounds and lignin
gluconate
-
activates, chelates and stabilizes Mn3+
glutathione
-
greatly enhances the oxidation of verartryl alcohol, lignin-model compounds and lignin
glycolate
-
activates, chelates and stabilizes Mn3+
H2O2
-
H2O2-dependent
H2O2
-
H2O2-dependent
H2O2
-
highest Mn2+-oxidation activity when the H2O2 concentration is 0.1 mM
H2O2
-
H2O2-dependent
H2O2
-
accelerates oxidation of NADH in reaction mixture containing alpha-hydroxy acid, no acceleration in reaction mixture containing acetate
L-Malate
-
activates, forms stable Mn3+ complex
L-Malate
-
activates by chelating and stabilizing Mn3+
L-Malate
-
activates by chelating and stabilizing Mn3+
L-Malate
-
activates by chelating and stabilizing Mn3+
L-Tartrate
-
activates, stabilizes Mn3+ in aqueous solution with a relatively high redox potential
L-Tartrate
-
stimulates by chelating and stabilizing Mn3+
L-Tartrate
-
activates, forms stable Mn3+ complex
L-Tartrate
-
stimulates by chelating and stabilizing Mn3+
Lactate
-
activates, stabilizes Mn3+ in aqueous solution with a relatively high redox potential
Lactate
-
stimulates by complexing with and stabilizing Mn3+
Lactate
-
activates, chelates and stabilizes Mn3+
Lactate
-
lactate serves as a chelator for the Mn3+ chelate formation, leading to a specific activity about 48.4% of that obtained with tartrate
Maleate
-
slightly activates, chelates and stabilizes Mn3+
-
malonate
-
activates, stabilizes Mn3+ in aqueous solution with a relatively high redox potential, most effective physiological chelator excreted by the fungus
malonate
-
stimulates by chelating and stabilizing Mn3+
malonate
-
stabilizes Mn3+ at a relatively high redox potential and facilitate oxidation of organic substrates
malonate
-
stimulates by chelating and stabilizing Mn3+
malonate
-
stabilizes Mn3+ as chelator
malonate
-
the highest stimulation of 2,6-dimethoxyphenol oxidation is observed in the presence of 10 mM malonate, malonate also serves as a chelator for the Mn3+ chelate formation, leading to a specific activity about 54.8% of that obtained with tartrate
Nitrilotriacetate
-
slightly activates, chelates Mn3+
oxalate
-
activates by chelating and stabilizing Mn3+
oxalate
-
activates by chelating and stabilizing Mn3+; less activation than by lactate or malonate
oxalate
-
activates by chelating and stabilizing Mn3+
oxalate
-
activates by chelating and stabilizing Mn3+
oxalate
Clitocybula dusenii, Nematoloma frowardii
-
potent chelator of Mn3+
oxalate
-
potent chelator of Mn3+
oxalate
-
oxalate serves as a chelator for the Mn3+ chelate formation, leading to a specific activity about 64.7% of that obtained with tartrate
oxaloacetate
-
stimulates by chelating and stabilizing Mn3+
oxygen
-
stimulates
Pc reducer
-
the activity of manganese peroxidase is promoted by Pc reducer at concentrations less than 0.2 mg/ml
-
phenylacetate
-
activates, chelates and stabilizes Mn3+
phosphate
-
activates, chelates and stabilizes Mn3+
Polyglutamate
-
slightly activates, stabilizes Mn3+ in aqueous solution with a relatively high redox potential
succinate
-
activates, stabilizes Mn3+ less effective than citrate or lactate
succinate
-
slightly activates, chelates Mn3+
Tartrate
-
the highest rate of Mn3+ formation is obtained with 10 mM tartrate
Tween 80
-
enhances oxidation of benzo[a]pyrene and other polycyclic aromatic hydrocarbons
Methylmalonate
-
stimulates by chelating and stabilizing Mn3+
additional information
-
1 mM verartryl alcohol in growth medium increases activity 2fold
-
additional information
-
dramatic stimulation by chelating organic acids as C2- and C3-dicarboxylic or alpha-hydroxyl acids facilitate the dissociation of Mn(III) from manganese-enzyme complex, greater activation with weakly binding chelators with a low binding constant, e.g. lactate or tartrate; succinate is no Mn3+ chelator and activator
-
additional information
-
succinate, formate and acetate do not stabilize Mn3+
-
additional information
-
no Mn3+ chelators and activators: acetate, propionate, citrate, D-malate, ethylene glycol; succinate is no Mn3+ chelator and activator
-
additional information
-
acetate is not an effective chelator
-
additional information
-
-
-
additional information
-
production of MnP is induced by nitrogen limitation and by oxygen
-
additional information
-
strong increase of MnP levels by growth in presence of peptone, compared with glucose-ammonium tartrate medium
-
additional information
-
strong increase of MnP levels by growth in presence of peptone, compared with glucose-ammonium tartrate medium
-
additional information
-
strong increase of MnP levels by growth in presence of peptone, compared with glucose-ammonium tartrate medium
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0478
-
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
Schizophyllum sp.
-
30C, pH 4.5
0.196
-
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
-
0.0713
-
2,2'-azinobis(3-ethylbenzthiazoline)-6-sulfonic acid
-
in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2, 45C
0.196
-
2,2'-azinobis(3-ethylbenzthiazoline)-6-sulfonic acid
-
in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2 and 1.5 mM Mn2+, 45C
0.0713
-
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) Mn2+
-
-
0.0125
-
2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
Mn2+-independent activity
0.015
-
2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
Mn2+-dependent activity
0.00366
-
2,6-dimethoxyphenol
-
Mn2+-dependent activity
0.0066
-
2,6-dimethoxyphenol
-
Mn2+-dependent activity, PCH6
0.00847
-
2,6-dimethoxyphenol
-
-
0.01
-
2,6-dimethoxyphenol
-
0.1 mM Mn2+, 0.1 mM H2O2
0.011
-
2,6-dimethoxyphenol
-
0.1 mM Mn2+, 0.1 mM H2O2
0.011
-
2,6-dimethoxyphenol
Bjerkandera sp.
-
Mn2+-dependent activity, BOS2
0.011
-
2,6-dimethoxyphenol
-
Mn2+-dependent activity, PCH5
0.018
-
2,6-dimethoxyphenol
-
Mn2+-dependent activity, PCH4
0.0195
-
2,6-dimethoxyphenol
Bjerkandera sp.
-
Mn2+-dependent activity, BOS1
0.0286
-
2,6-dimethoxyphenol
-
30C, pH 4.5
0.076
-
2,6-dimethoxyphenol
-
; in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2 and 1.5 mM Mn2+, 45C
0.092
-
2,6-dimethoxyphenol
-
MnP3
0.106
-
2,6-dimethoxyphenol
Bjerkandera sp.
-
Mn2+-independent activity, BOS2
0.121
-
2,6-dimethoxyphenol
Bjerkandera sp.
-
Mn2+-independent activity, BOS1
0.1229
-
2,6-dimethoxyphenol
Schizophyllum sp.
-
30C, pH 4.5
0.1445
-
2,6-dimethoxyphenol
-
Mn2+-independent activity
0.16
0.25
2,6-dimethoxyphenol
-
0.1 mM H2O2
0.3
-
2,6-dimethoxyphenol
-
-
0.95
-
2,6-dimethoxyphenol
-
0.1 mM H2O2
6.954
-
2,6-dimethoxyphenol
-
; in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2, 45C
13
-
Bromocresol green
-
-
2000
-
bromocresol purple
-
-
31
-
Bromophenol blue
-
-
14
-
bromophenol red
-
-
154
-
bromothymol blue
-
-
0.42
-
ferrocyanide
-
MnP1 from mutant F190A
3.4
3.8
ferrocyanide
-
MnP1 from mutants F190Y, F190L, F190I
3.5
-
ferrocyanide
-
wild-type MnP1
0.0131
-
guaiacol
Schizophyllum sp.
-
30C, pH 4.5
0.213
-
guaiacol
-
; in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2 and 1.5 mM Mn2+, 45C
0.222
-
guaiacol
-
Mn2+-dependent activity
2.3
-
guaiacol
-
; in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2, 45C
4.96
-
guaiacol
-
Mn2+-independent activity
0.002
-
H2O2
-
0.1 mM Mn2+, MnP1
0.0031
-
H2O2
Bjerkandera sp.
-
0.1 mM Mn2+, BOS1
0.004
-
H2O2
-
0.1 mM 2,6-dimethoxyphenol
0.0045
-
H2O2
-
-
0.0047
-
H2O2
Bjerkandera sp.
-
0.1 mM Mn2+, BOS2
0.005
-
H2O2
-
0.1 mM Mn2+, PCH6
0.0057
-
H2O2
-
mutant R177E
0.006
0.009
H2O2
-
-
0.006
0.01
H2O2
-
0.1 mM Mn2+
0.006
-
H2O2
-
0.1 mM Mn2+, PCH5
0.0064
-
H2O2
-
reaction with Mn2+
0.0067
-
H2O2
Schizophyllum sp.
-
30C, pH 4.5
0.0078
-
H2O2
-
mutant R177Q
0.0092
-
H2O2
-
0.1 mM Mn2+, PCH4
0.0095
-
H2O2
-
pH 4.5, 25C
0.0121
-
H2O2
-
mutant R177N
0.0126
-
H2O2
-
mutant R177D
0.015
-
H2O2
-
0.1 mM Mn2+
0.016
-
H2O2
-
; pH 5.5, 45C
0.0166
-
H2O2
-
reaction with Mn2+
0.0178
-
H2O2
-
reaction with Mn2+
0.021
-
H2O2
-
isoenzyme H5
0.0293
0.0294
H2O2
-
MnP2 and MnP3
0.032
-
H2O2
-
isoenzyme H4
0.034
-
H2O2
-
isoenzyme H3
0.039
0.041
H2O2
-
MnP1 from mutants F190Y, F190L, F190I and F190A
0.039
-
H2O2
-
mutant R177A
0.039
-
H2O2
-
wild-type MnP1
0.044
-
H2O2
-
mutant R177K
0.055
-
H2O2
-
wild-type MnP
0.055
-
H2O2
-
recombinant enzyme
0.057
0.059
H2O2
-
Mn3+-tartrate formation
0.058
-
H2O2
-
wild-type enzyme
0.0714
-
H2O2
-
30C, pH 4.5
29
-
m-cresol purple
-
-
0.004
-
Mn2+
-
isoenzyme H5
0.009
-
Mn2+
-
isoenzyme H4
0.01
-
Mn2+
-
0.1 mM 2,6-dimethoxyphenol, 0.1 mM H2O2
0.012
-
Mn2+
-
0.1 mM H2O2, MnP1
0.014
-
Mn2+
-
MnP3
0.015
-
Mn2+
-
0.1 mM 2,6-dimethoxyphenol, 0.1 mM H2O2
0.016
-
Mn2+
-
isoenzyme H3
0.0165
-
Mn2+
Bjerkandera sp.
-
BOS1
0.017
-
Mn2+
-
0.1 mM H2O2, MnP1
0.018
-
Mn2+
-
0.1 mM H2O2
0.0198
-
Mn2+
-
-
0.02
-
Mn2+
-
below
0.02
-
Mn2+
-
0.1 mM H2O2
0.025
-
Mn2+
-
MnP2
0.0254
-
Mn2+
Bjerkandera sp.
-
BOS2
0.0352
-
Mn2+
Schizophyllum sp.
-
30C, pH 4.5
0.039
-
Mn2+
-
MnP1
0.0447
-
Mn2+
Deuteromycotina sp.
-
-
0.063
-
Mn2+
-
reaction with H2O2
0.074
0.08
Mn2+
-
MnP1 from mutants F190Y, F190L, F190I and F190A
0.0802
-
Mn2+
-
-
0.083
-
Mn2+
-
wild-type MnP1
0.0838
-
Mn2+
-
MnP2
0.09
-
Mn2+
-
wild-type MnP
0.124
-
Mn2+
-
; pH 5.5, 45C
0.4
-
Mn2+
-
pH 5.0, 25C
1.64
-
Mn2+
-
mutant R177A
2.15
-
Mn2+
-
mutant R177D
2.32
-
Mn2+
-
mutant R177K
2.91
-
Mn2+
-
mutant R177Q
3.61
-
Mn2+
-
mutant R177N
3.9
-
Mn2+
-
mutant R177E
0.06
0.07
NADH
-
-
0.293
-
pyrogallol
-
; in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2 and 1.5 mM Mn2+, 45C
3.74
-
pyrogallol
-
; in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2, 45C
0.022
-
vanillylacetone
-
isoenzyme H5
0.024
-
vanillylacetone
-
isoenzyme H4
0.031
-
vanillylacetone
-
isoenzyme H3
0.005
-
vanillylideneacetone
-
0.1 mM Mn2+, 0.1 mM H2O2
0.432
-
Veratryl alcohol
-
Mn2+-dependent activity
0.56
-
Veratryl alcohol
-
; in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2 and 1.5 mM Mn2+, 45C
0.646
-
Veratryl alcohol
-
-
3
3.5
Veratryl alcohol
-
0.1 mM H2O2
3
-
Veratryl alcohol
-
-
3.2
-
Veratryl alcohol
Bjerkandera sp.
-
BOS1
3.3
-
Veratryl alcohol
-
-
4.1
-
Veratryl alcohol
-
0.1 mM H2O2
5.3
-
Veratryl alcohol
-
Mn2+-independent activity
5.33
-
Veratryl alcohol
Bjerkandera sp.
-
BOS2
0.667
-
2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
0.1 mM H2O2, Mn2+-independent activity, MnP1
additional information
-
2,6-dimethoxyphenol
-
apparent Km, 216 microM/l, chromatographic MnP form 2; apparent Km, 417 microM/l, chromatographic MnP form 1; apparent Km, 516 microM/l, chromatographic MnP form 3
0.021
-
Mn(II)
-
pH 4.5, 25C
additional information
-
Mn2+
-
apparent Km, 24 microM/l, chromatographic MnP form 1; apparent Km, 44 microM/l, chromatographic MnP form 2; apparent Km, 47 microM/l, chromatographic MnP form 3
4.4
-
Mn2+
-
mutant E35Q
additional information
-
additional information
-
additional information
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
87.1
-
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
Schizophyllum sp.
-
30C, pH 4.5
20.2
-
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
-
1.87
-
2,2'-azinobis(3-ethylbenzthiazoline)-6-sulfonic acid
-
in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2, 45C
20.2
-
2,2'-azinobis(3-ethylbenzthiazoline)-6-sulfonic acid
-
in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2 and 1.5 mM Mn2+, 45C
1.87
-
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) Mn2+
-
-
120
-
2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
Mn2+-dependent activity
139
-
2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
Mn2+-independent activity
3.98
-
2,6-dimethoxyphenol
-
-
5.67
-
2,6-dimethoxyphenol
-
; in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2, 45C
26.26
-
2,6-dimethoxyphenol
-
; in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2 and 1.5 mM Mn2+, 45C
69
-
2,6-dimethoxyphenol
Schizophyllum sp.
-
30C, pH 4.5
70
-
2,6-dimethoxyphenol
-
Mn2+-independent activity
200
-
2,6-dimethoxyphenol
-
MnP3
320
-
2,6-dimethoxyphenol
-
Mn2+-dependent activity
3.4
4.2
ferrocyanide
-
MnP1 from mutants F190Y, F190L, F190I
4
-
ferrocyanide
-
wild-type MnP1
14.6
-
ferrocyanide
-
MnP1 from mutant F190A
0.74
-
guaiacol
-
; in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2, 45C
8.92
-
guaiacol
-
; in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2 and 1.5 mM Mn2+, 45C
14.5
-
guaiacol
-
Mn2+-independent activity
17.3
-
guaiacol
Schizophyllum sp.
-
30C, pH 4.5
31.7
-
guaiacol
-
Mn2+-dependent activity
40
-
guaiacol
-
isoenzyme H5
53
-
guaiacol
-
isoenzyme H3
56
-
guaiacol
-
isoenzyme H4
17.3
-
H2O2
-
mutant R177E
23.2
-
H2O2
-
mutant R177Q
28.8
-
H2O2
-
mutant R177D
35.8
-
H2O2
-
mutant R177N
100
-
H2O2
-
MnP2
121
-
H2O2
-
; with 1.5 mM Mn2+ as cosubstrate, pH 5.5, 45C
168
-
H2O2
-
recombinant enzyme
190
-
H2O2
-
mutant R177A
230
-
H2O2
-
MnP3
237
-
H2O2
-
wild-type enzyme
252
-
H2O2
-
wild-type MnP
272.4
-
H2O2
-
reaction with Mn2+
273
-
H2O2
-
mutant R177K
373
-
H2O2
Schizophyllum sp.
-
30C, pH 4.5
6.7
-
Mn(II)
-
pH 4.5, 25C
0.77
-
Mn2+
-
mutant E35Q
24
-
Mn2+
-
A48C/A63C double mutant MnP after thermal treatment at 37C for 15 min
25
-
Mn2+
-
mutant R177Q
25.5
-
Mn2+
-
mutant R177E
30.2
-
Mn2+
-
mutant R177D
34.6
-
Mn2+
-
mutant R177N
100
-
Mn2+
-
MnP2
161
-
Mn2+
Deuteromycotina sp.
-
-
184
-
Mn2+
-
mutant R177A
218
-
Mn2+
-
native MnP
230
-
Mn2+
-
MnP3
240
290
Mn2+
-
MnP1 from mutants F190Y, F190L, F190I and F190A
242.4
-
Mn2+
-
; with 0.2 mM H2O2 as cosubstrate, pH 5.5, 45C
256
-
Mn2+
-
wild-type MnP
262
-
Mn2+
-
mutant R177K
270
273
Mn2+
-
recombinant MnP and A48C/A63C double mutant MnP
290
-
Mn2+
-
wild-type MnP1
304.8
-
Mn2+
-
reactioin with H2O2
479.7
-
Mn2+
Schizophyllum sp.
-
30C, pH 4.5
98.3
-
Mn3+-tartrate
-
preparation M2
-
39
-
Phenol red
-
isoenzyme H5
41
-
Phenol red
-
isoenzyme H4
66
-
Phenol red
-
isoenzyme H3
9.98
-
pyrogallol
-
; in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2, 45C
20.95
-
pyrogallol
-
; in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2 and 1.5 mM Mn2+, 45C
76
-
vanillylacetone
-
isoenzyme H5
90.3
-
vanillylacetone
-
isoenzyme H4
97
-
vanillylacetone
-
isoenzyme H3
0.45
-
Veratryl alcohol
-
; in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2 and 1.5 mM Mn2+, 45C
5.33
-
Veratryl alcohol
-
Mn2+-independent activity
39.5
-
Veratryl alcohol
-
Mn2+-dependent activity
118
-
Mn3+-tartrate
-
preparation M1
-
additional information
-
additional information
-
-
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
320
-
Mn(II)
-
pH 4.5, 25C
23973
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.004
-
Cd2+
-
oxidation of 2,6-dimethoxyphenol
0.01
-
Cd2+
-
oxidation of Mn2+
0.402
-
methylhydrazine
-
-
additional information
-
additional information
-
transient-state inhibition constants
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.01
-
-
specific MnP activity recovered from solid-state culture after 1h and 10C, U/mg of fugal biomass, pH 6.0; specific MnP activity recovered from solid-state culture after 1h and 25C, U/mg of fugal biomass, pH 6.0
0.04
-
-
effect of dialysis on MnP recovered from solid-state culture at 10C, dialyzed extract, extraction conducted for 3h at 100 rpm, U/mg of fugal biomass, pH 4.0
0.1
-
-
specific MnP activity recovered from solid-state culture after 3h and 10C, U/mg of fugal biomass, pH 6.0
0.12
-
-
specific MnP activity recovered from solid-state culture after 3h and 25C, U/mg of fugal biomass, pH 6.0
0.16
-
-
effect of dialysis on MnP recovered from solid-state culture at 10C, dialyzed extract, extraction conducted for 1h without agitation, U/mg of fugal biomass, pH 5.0
0.2
-
-
specific MnP activity recovered from solid-state culture after 1h and 25C, U/mg of fugal biomass, pH 4.0
0.21
-
-
effect of dialysis on MnP recovered from solid-state culture at 10C, dialyzed extract, extraction conducted for 3h at 100 rpm, U/mg of fugal biomass, pH 5.0
0.27
-
-
effect of dialysis on MnP recovered from solid-state culture at 10C, dialyzed extract, extraction conducted for 1h without agitation, U/mg of fugal biomass, pH 4.0
0.31
-
-
effect of dialysis on MnP recovered from solid-state culture at 10C, crude extract, extraction conducted for 3h at 100 rpm, U/mg of fugal biomass, pH 4.0; specific MnP activity recovered from solid-state culture after 3h and 10C, U/mg of fugal biomass, pH 4.0
0.35
-
-
effect of dialysis on MnP recovered from solid-state culture at 10C, crude extract, extraction conducted for 1h without agitation, U/mg of fugal biomass, pH 4.0; effect of dialysis on MnP recovered from solid-state culture at 10C, crude extract, extraction conducted for 1h without agitation, U/mg of fugal biomass, pH 5.0; specific MnP activity recovered from solid-state culture after 1h and 10C, U/mg of fugal biomass, pH 4.0; specific MnP activity recovered from solid-state culture after 1h and 10C, U/mg of fugal biomass, pH 5.0
0.41
-
-
effect of dialysis on MnP recovered from solid-state culture at 10C, crude extract, extraction conducted for 3h at 100 rpm, U/mg of fugal biomass, pH 5.0; specific MnP activity recovered from solid-state culture after 3h and 10C, U/mg of fugal biomass, pH 5.0
0.45
-
-
specific MnP activity recovered from solid-state culture after 1h and 25C, U/mg of fugal biomass, pH 5.0
0.48
-
-
specific MnP activity recovered from solid-state culture after 3h and 25C, U/mg of fugal biomass, pH 4.0
0.7
-
-
specific MnP activity recovered from solid-state culture after 3h and 25C, U/mg of fugal biomass, pH 5.0
10.2
-
-
oxidation of 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate in presence of Mn2+ and H2O2
23
-
-
isoenzyme H5
40
-
-
culture supernatant, pH 5.5, 45C; purification step culture supernatant
41
-
-
purification step ultrafiltration
65
134
-
depending on culture age
107
-
-
isoenzyme H4
169
-
-
purification step chromatography on a concanavalin-A Sepharose column
180
-
-
Mn3+-lactate complex formation
185
-
-
purification step crude medium
288
-
-
after 7.2fold purification, pH 5.5, 45C; purification step gel filtration
506
-
-
pH 5.0, 25C
660
-
-
o-toluidine as substrate for Mn3+-oxidation
733
-
-
purification step DEAE Sepharose
870
-
-
purification step Mono Q1
1230
-
-
purification step CIM QA disk 3, chromatographic MnP form 3, CIM3
2250
-
-
purification step Mono Q2
2480
-
-
purification step CIM QA disk 1, chromatographic MnP form 1, CIM1
3430
-
-
purification step CIM QA disk 2, chromatographic MnP form 2, CIM2
additional information
-
-
216-467, 1 unit: initial increase in absorbance of 1.0 per min at 465 nm
additional information
-
-
284-422: 5 isozymes, expressed as spectral change in DELTAA per min and mg of heme-containing protein
additional information
-
-
216-467, 1 unit: initial increase in absorbance of 1.0 per min at 465 nm
additional information
-
-
66.6, 1 unit: oxidation of 3,3,5,5-tetramethylbenzidine so that the change in A650 is 0.01 per min
additional information
-
-
-
additional information
-
-
-
additional information
-
Deuteromycotina sp., Phanerochaete chrysosporium
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
340-350 U/l
additional information
-
-
0.055 U/ml, R42A mutant, in the presence of 2,6-dimethoxyphenol; 0.069 U/ml, N131D mutant, in the presence of 2,6-dimethoxyphenol; 0.076 U/ml, wild-type enzyme, in the presence of 2,6-dimethoxyphenol
additional information
-
-
enzyme yield is species-dependent and strain-dependent, the carbon source and lignocellulosic substrate play a crucial role in enzyme production
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2.5
-
-
oxidation of 2,6-dimethoxyphenol in absence of Mn2+
3
-
-
Mn2+-independent peroxidase activity
3
-
-
oxidation of 2,6-dimethoxyphenol and veratryl alcohol in absence of Mn2+
3
-
-
oxidation of 2,6-dimethoxyphenol and veratryl alcohol in absence of Mn2+
3
-
-
decolorization of bromophenol blue
3
-
-
optimal pH for the Mn-dependent oxidation of veratryl alcohol; optimum pH for the Mn2+-dependent oxidation of veratryl alehyde
3.5
4.5
-
decolorization of bromocresol purple
3.5
4.5
-
pH optimum for Mn2+-independent DMOP oxidation
3.5
5.5
-
-
3.5
-
-
oxidation of NAD(P)H
3.5
-
-
oxidation of NAD(P)H
4
4.5
-
pH optimum for Mn2+-dependent DMOP oxidation
4
-
-
oxidation of NADH
4
-
-
oxidation of Mn2+
4
-
-
oxidation of 2,6-dimethoxyphenol in presence of Mn2+
4
-
-
decolorization of bromocresol green, bromophenol red, bromothymol blue, o-cresol red, m-cresol purple, phenol red and thymol blue
4
-
-
pH optimum for Mn2+ oxidation, chromatographic MnP form 1, 2 and 3
4
-
B5U990
activity assay
4.5
-
-
oxidation of 2,2-azino-bis-3-ethyl-6-benzothiazolinesulfonate
4.5
-
-
Mn2+ oxidation
4.5
-
-
oxidation of 2,6-dimethoxyphenol in presence of Mn2+
4.5
-
-
MnP1 in 50 mM malonate
4.5
-
-
oxidation of 2,6-dimethoxyphenol in presence of Mn2+
4.5
-
-
activity assay
4.8
-
-
Mn3+-tartrate and Mn3+-malate formation
5
-
-
Mn3+-lactate complex formation
5
-
-
Mn2+-dependent peroxidase activity
5
-
-
MnP2 in 50 mM malonate
5
-
-
oxidation of Mn2+
5
-
-
oxidation of Mn2+
6
-
-
optimal pH for MnP production in submerged culture
6.8
-
Schizophyllum sp.
-
oxidation of 2,6-dimethoxyphenol
additional information
-
-
pI: 3.8
additional information
-
-
5 isozymes, pI: 2.9-3.2
additional information
-
-
isozyme H5: pI 4.2, isoenzyme H4: pI 4.5, isoenzyme H3: pI 4.9; pI: 4.9
additional information
-
-
pI: 4.9
additional information
-
-
pI: 3.2
additional information
-
-
pI: 4.9
additional information
-
-
pI: 3.5
additional information
-
-
MnP1: pI 3.25, MnP2: pI 3.3
additional information
-
-
MnP2: pI 3.7, MnP3: pI 3.5
additional information
-
-
pI: 3.5
additional information
-
-
-
additional information
-
-
MnP1: pI 4.1, MnP2: pI 3.9
additional information
-
-
pI: 3.8
additional information
-
-
MnPI: pI 5.3, MnPII: pI 4.2, MnPIII: pI 3.3
additional information
-
Deuteromycotina sp.
-
4 isoenzymes: pI 5.1, 4.9, 4.5 and 3.7
additional information
-
-
-
additional information
-
-
2 isozymes: pI 3.8 and 3.7
additional information
-
-
-
additional information
-
-
2 isoenzymes: pI 6.3-7.0
additional information
-
-
MnP1: pI 6.3-7.1, MnP2: 3.5-3.7, MnP3: 5.1
additional information
-
-
-
additional information
-
Bjerkandera sp.
-
BOS1: pI 3.45, BOS2: pI 3.4
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2
6
-
active in the range, below pH 2 and above pH 6: completely inactive
3
3.5
-
pH 3.5: decrease of 95% of oxidation of Mn2+, pH 3: nearly no oxidation of Mn2+
3
5
-
oxidation of veratryl alcohol decreases more than 95% when the pH is increased from 3 to 4.5 and nearly absent at pH 5
3.1
6.1
-
veratryl alcohol oxidation, activity increases with increasing pH
3.1
8.3
-
in presence of H2O2 the formation of enzyme compound I is independent of pH over the range
3.5
4.5
-
optima for Mn2+-independent 2,6-dimethoxyphenol oxidation
3.5
6
-
pH 3.5: about 30% of maximal activity, pH 4.0: about 70% of maximal activity, pH 6.0: about 45% of maximal activity
3.5
6.5
-
Mn2+ oxidation shows an optimum in the range 5.5-5.75 and negligible activity at pH values below 3.5 and above 6.5
4
4.5
-
optima for Mn2+-dependent 2,6-dimethoxyphenol oxidation
4
5.5
-
about half-maximal activity at pH 4.0 and 5.5, 2,2-azino-bis-3-ethyl-6-benzothiazolinesulfonate-oxidation
4.5
5.7
-
about 65% of maximal activity at pH 4.5 and about 50% at pH 5.7, Mn(III)-lactate formation
5.5
5.8
-
the pH-activity profile for Mn2+ oxidation shows an optimum in the range 5.5 - 5.75 and negligible activity at pHs below 3.5 and above 6.5
additional information
-
-
MnP is active in a broad pH-range
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
25
-
Clitocybula dusenii, Nematoloma frowardii
-
assay at
25
-
-
activity assay
30
-
Deuteromycotina sp., Phanerochaete chrysosporium
-
assay at
30
-
B5U990
activity assay
35
-
Schizophyllum sp.
-
oxidation of 2,6-dimethoxyphenol
37
-
-
assay at
40
-
-
assay at
45
-
-
; optimum temperature for the oxidation of Mn2+ and DMOP
60
-
-
highest Mn2+ oxidation rate over 1 min
additional information
-
-
assay at room temperature
additional information
-
-
assay at room temperature
additional information
-
-
assay at room temperature
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
10
60
-
the enzyme shows relative activities of 34, 50, and 47% at 10, 40, and 60C, respectively
20
65
-
progressive enhancement of activity from 20C to 65C
25
45
-
25C: about 80% of maximal activity, 45C: about 60% of maximal activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.5
-
-
chromatographic MnP form 1 and 2
3.6
-
Schizophyllum sp.
-
isoelectric focusing
3.77
-
-
isoelectric focusing
3.98
-
B5U990
theoretical
4.06
-
-
isoelectric focusing
4.1
-
-
isoelectric focusing
4.2
-
-
isoenzyme MnP4, isoelectrofocusing
4.6
-
-
isoenzyme MnP2, isoelectrofocusing
4.9
-
-
isoenzyme MnP1, isoelectrofocusing
6.2
-
-
isoelectric focusing
8.2
-
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
shallow stationary culture growing on N-limited medium
Manually annotated by BRENDA team
-
higher concentrations of foam and lower levels of spore inoculums result in the formation of scattered mycelial pellets, increased autolysis of chlamydospore-like cells (a reservoir of MnP), and a higher activity of MnP. Even though MnP is a secondary metabolite, the addition of 5times more glucose and diammonium tartrate, as carbon and nitrogen sources, results in a 4fold increase in the dry cell mass. MnP activity decreases under these conditions to less than half, due to the formation of increasingly dense pellets and the inhibited lysis of chlamydospore-like cells
Manually annotated by BRENDA team
Schizophyllum sp.
-
-
Manually annotated by BRENDA team
Phanerochaete chrysosporium MZKI B-223, Schizophyllum sp. F17
-
-
-
Manually annotated by BRENDA team
Abortiporus biennis, Agaricus sp., Agrocybe aegerita, Agrocybe sp. 1, Agrocybe sp. 2, Clitocybe sp., Coprinopsis atramentaria, Cortinarius sp. 1, Cortinarius sp. 2, Ganoderma carnosum, Inocybe lacera, Inocybe longicystis, Lactarius deliciosus, Lepiota naucina, Lepiota sp. 1, Lepiota sp. 2, Lepista nuda, Leptonia lazunila, Lyophyllum subglobisporium, Parasola plicatilis, Pleurotus ostreatus, Ramaria stricta, Rhizopogon luteolus, Russula rosacea, Russula sp., Trametes hirsuta, Trametes versicolor, Volvariella sp.
-
-
Manually annotated by BRENDA team
Abortiporus biennis ECN 100601, Cortinarius sp. 2 ECN 100602, Ganoderma carnosum ECN 100603, Lactarius deliciosus ECN 100604, Lepista nuda ECN 100605, Lyophyllum subglobisporium ECN 100606, Pleurotus ostreatus ECN 100607, Ramaria stricta ECN 100608, Trametes versicolor ECN 100609
-
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
appears to be closely related to mycelium
-
Manually annotated by BRENDA team
Clitocybula dusenii
-
-
-
Manually annotated by BRENDA team
Deuteromycotina sp.
-
-
-
Manually annotated by BRENDA team
Nematoloma frowardii
-
-
-
Manually annotated by BRENDA team
Schizophyllum sp.
-
-
-
Manually annotated by BRENDA team
B5U990
secreted into the medium
-
Manually annotated by BRENDA team
Agrocybe praecox TM 70.84, Bjerkandera adusta UAMH, Clitocybula dusenii b11, Dichomitus squalens CBS 432.34
-
-
-
-
Manually annotated by BRENDA team
Lentinula edodes SR-1
-
secreted into the medium
-
-
Manually annotated by BRENDA team
Phanerochaete chrysosporium BKM-F 1767, Phanerochaete chrysosporium BKM-F-1767
-
appears to be closely related to mycelium
-
-
Manually annotated by BRENDA team
Phanerochaete chrysosporium ME446, Phanerochaete chrysosporium OGC101, Phanerochaete chrysosporium VKM F-1767, Phlebia radiata 79, Schizophyllum sp. F17, Stropharia coronilla TM 47-1
-
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37000
-
B5U990
theoretical
40000
45000
-
-
40000
-
-
around 40 kDa, gel filtration
41000
42000
-
-
41000
-
-
MnP2, gel filtration
42000
43000
Clitocybula dusenii
-
-
42000
45000
-
-
42000
50000
Nematoloma frowardii
-
-
43000
99000
-
-
43000
-
-
-
43000
-
-
determined by Western blot analysis
44000
45000
Bjerkandera sp.
-
-
44000
50000
-
-
44500
-
-
TvMP2
44600
59000
-
MnPs from different strains
44800
-
B5U990
determined by SDS-PAGE
45000
-
-
TvMP1
45000
-
-
gel filtration
47000
-
-
MnP3, gel filtration
48000
49000
-
-
48000
-
-
MnP1 and MnP2, gel filtration
48000
-
B5U990
determined by gel filtration
50000
-
-
determined by SDS-PAGE, chromatographic MnP form 1, 2 and 3
50500
-
-
determined by gel filtration and SDS-PAGE; gel filtration
660000
-
-
protein complex containing MnP, laccase and beta-glucosidase, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 45000-47000, SDS-PAGE
?
-
x * 49000, SDS-PAGE
?
-
x * 44000, isozyme TvMP4, x * 44500, isozyme TvMP2 and TvMP5, 1 * 45000, isozyme TvMP1 and TvMP3, SDS-PAGE
?
-
x * 44600, SDS-PAGE
?
-
x * 43000, isoelectrofocusing; x * 43000, SDS-PAGE
?
-
x * 46000, wild-type and mutants R177D, R177E, R177N and R177Q, SDS-PAGE
?
-
x * 36600, MALDI-TOF mass spectrometric analysis, more accurate reflection of the true molecular weight than by SDS-PAGE; x * 43000, SDS-PAGE
?
-
x * 45000, SDS-PAGE
?
Deuteromycotina sp.
-
x * 43000, SDS-PAGE
?
-
x * 43000, SDS-PAGE
?
-
x * 43000, SDS-PAGE
?
-
x * 42000, SDS-PAGE
?
-
x * 41000, MnP1 and MnP2, x * 43000, MnP3, SDS-PAGE
?
-
x * 42000, SDS-PAGE
?
-
x * 46000, SDS-PAGE
?
-
x * 42000, SDS-PAGE
?
-
x * 40000, SDS-PAGE
?
Schizophyllum sp.
-
x * 48700, SDS-PAGE
?
-
x * 43000, SDS-PAGE
?
-
x * 40000, SDS-PAGE
?
Agrocybe praecox TM 70.84
-
x * 42000, SDS-PAGE
-
?
Bjerkandera adusta 90-41
-
x * 43000, isoelectrofocusing; x * 43000, SDS-PAGE
-
?
Bjerkandera adusta UAMH
-
x * 36600, MALDI-TOF mass spectrometric analysis, more accurate reflection of the true molecular weight than by SDS-PAGE; x * 43000, SDS-PAGE
-
?
Phanerochaete chrysosporium BKM-F 1767, Phanerochaete chrysosporium BKM-F-1767
-
x * 45000-47000, SDS-PAGE
-
?
Phanerochaete chrysosporium ME446
-
-
-
?
Phanerochaete chrysosporium OGC101
-
x * 46000, SDS-PAGE; x * 46000, wild-type and mutants R177D, R177E, R177N and R177Q, SDS-PAGE
-
?
-
x * 49000, SDS-PAGE
-
?
Pleurotus ostreatus CBS 411.71
-
x * 43000, SDS-PAGE; x * 43000, SDS-PAGE
-
?
Schizophyllum commune IBL-06
-
x * 40000, SDS-PAGE
-
?
-
x * 48700, SDS-PAGE
-
?
Stropharia coronilla TM 47-1
-
x * 41000, MnP1 and MnP2, x * 43000, MnP3, SDS-PAGE
-
?
Trichophyton rubrum LSK-27
-
x * 42000, SDS-PAGE
-
monomer
-
1 * 41000, MnP2, 1 * 38000, MnP3, SDS-PAGE
monomer
-
1 * 48000, MnP1, 1 * 48900, MnP2, SDS-PAGE
monomer
Bjerkandera sp.
-
1 * 45000, BOS1, 1 * 44000, BOS2, SDS-PAGE
monomer
-
1 * 45000, PCH4 and PCH6, 1 * 43000, PCH5, SDS-PAGE
monomer
-
1 * 45000, SDS-PAGE
monomer
-
; 1 * 50500, SDS-PAGE
monomer
B5U990
-
monomer
Bjerkandera sp. BOS55
-
1 * 45000, BOS1, 1 * 44000, BOS2, SDS-PAGE
-
monomer
Dichomitus squalens CBS 432.34
-
1 * 48000, MnP1, 1 * 48900, MnP2, SDS-PAGE
-
monomer
Lentinula edodes SR-1
-
-
-
monomer
Lentinus tigrinus 577.79, Lentinus tigrinus CBS 577.79
-
; 1 * 50500, SDS-PAGE
-
monomer
Phanerochaete chrysosporium VKM F-1767
-
1 * 45000, PCH4 and PCH6, 1 * 43000, PCH5, SDS-PAGE
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
Bjerkandera adusta UAMH
-
-
-
glycoprotein
Bjerkandera sp.
-
2 isoenzymes differ in glycosylation degree, anthrone analysis: 5-7% total carbohydrate, SDS-PAGE after Endo-H treatment: 4.5% N-linked carbohydrate content in BOS1 and 2.3% in BOS2
glycoprotein
Bjerkandera sp.
-
-
glycoprotein
Bjerkandera sp. BOS55
-
2 isoenzymes differ in glycosylation degree, anthrone analysis: 5-7% total carbohydrate, SDS-PAGE after Endo-H treatment: 4.5% N-linked carbohydrate content in BOS1 and 2.3% in BOS2
-
glycoprotein
Deuteromycotina sp.
-
Asn-130 follows general rule of the N-glycosylation site
glycoprotein
Deuteromycotina sp.
-
-
proteolytic modification
Deuteromycotina sp.
-
leader sequence at the N-terminus: first 24 amino acids possess characteristics of signal peptides
glycoprotein
-
neutral carbohydrate content: MnP1: 8.5%, MnP2: 10.3%
glycoprotein
-
-
glycoprotein
Dichomitus squalens CBS 432.34
-
neutral carbohydrate content: MnP1: 8.5%, MnP2: 10.3%
-
glycoprotein
-
N-glycosylation of about 5.3% of the high-mannose type; the enzyme displays an extent of N-glycosylation of about 5.3% of the high-mannose type
glycoprotein
Lentinus tigrinus 577.79, Lentinus tigrinus CBS 577.79
-
N-glycosylation of about 5.3% of the high-mannose type; the enzyme displays an extent of N-glycosylation of about 5.3% of the high-mannose type
-
glycoprotein
-
17% carbohydrates
glycoprotein
-
glycoprotein with one recognition sequence for N-linked carbohydrate at Asp-217, residue at position 10 is a potential site for O-glycosylation
glycoprotein
Q02567
native MnP is glycosylated, but not recombinant MnP
glycoprotein
-
with 3 potential N-glycosylation sites, but only Asn-131 binds to carbohydrate
glycoprotein
-
glycosylation stabilizes MnP
glycoprotein
-
the recombinant enzyme produced by ZBMNP16 is hyperglycosylated
proteolytic modification
-
leader sequence at the N-terminus
glycoprotein
Phanerochaete chrysosporium BKM-F 1767
-
17% carbohydrates, glycoprotein with one recognition sequence for N-linked carbohydrate at Asp-217, residue at position 10 is a potential site for O-glycosylation
-
glycoprotein
Phanerochaete chrysosporium BKM-F-1767
-
17% carbohydrates
-
glycoprotein
Phanerochaete chrysosporium ME446
-
with 3 potential N-glycosylation sites, but only Asn-131 binds to carbohydrate
-
proteolytic modification
Phanerochaete chrysosporium ME446
-
leader sequence at the N-terminus
-
glycoprotein
Phanerochaete chrysosporium OGC101, Phanerochaete chrysosporium VKM F-1767
-
-
-
glycoprotein
-
-
glycoprotein
-
10% w/w carbohydrates
glycoprotein
-
-
glycoprotein
-
10% w/w carbohydrates
-
glycoprotein
-
5% carbohydrate content
glycoprotein
-
MP1: up to 5% carbohydrate, MP2: up to 7% carbohydrate
glycoprotein
-
presence of high-mannose-type glucans
glycoprotein
-
5% carbohydrate content
glycoprotein
Pleurotus ostreatus CBS 411.71
-
; 5% carbohydrate content
-
glycoprotein
Schizophyllum sp.
-
18% carbohydrate
glycoprotein
-
18% carbohydrate
-
glycoprotein
-
TvMnP1: 6% w/w carbohydrates, 0.6 mol glucose, 9.8 mol mannose and 6.7 mol glucosamine per mol protein, TvMnP2: 4% w/w carbohydrates, 0.8 mol glucose, 6.4 mol mannose and 3.6 mol glucosamine per mol protein, glucose may be from gel filtration on Sephadex
glycoprotein
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal structure
-
hanging drop vapor diffusion method, enzyme-Mn(II) structure at 1.45 A resolution, enzyme -Cd(II) structure, enzyme-Sm(III) structure, metal-free structure
-
manganese peroxidase crystallizes in the presence of Mn2+, where three homologous residues (Glu35, Glu39, and Asp179) participate in metal co-ordination, opening of the glutamate side-chains is not observed in manganese peroxidase crystals grown in the absence of Mn2+
-
crystal structure
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2.5
-
-
25C, 2 h, about 50% loss of activity
3
6
-
stable
3
-
-
25C, 2 h, about 40% loss of activity
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
4
-
Schizophyllum sp.
-
half-life: 19 h
4.5
6
-
25C, 2 h, stable
4.5
-
-
recombinant MnP, native MnP and A48C/A63C double mutant MnP are stable
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
5
-
Schizophyllum sp.
-
half-life: 23 h
6
-
-
native and A48C/A63C double mutant MnP: 1 h, less than 40% loss of activity
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
6
-
Schizophyllum sp.
-
half-life: 15 h
6.5
-
-
25C, 2 h, about 20% loss of activity
7
-
-
native MnP: 1 h, 80% loss of activity, A48C/A63C double mutant MnP: 1 h, 60% loss of activity
7
-
-
25C, 2 h, about 40% loss of activity
7
-
Schizophyllum sp.
-
half-life: 9 h
8
-
-
recombinant MnP: inactivation within 1 min, native MnP: inactivation within 15 min, A48C/A63C double mutant MnP: 1 h, 80% loss of activity
10
-
-
enzyme loses activity rapidly at pH 10
additional information
-
-
polyethylene glycol-modified enzyme shows greater stability to lower pH than native enzyme
additional information
-
-
recombinant MnP is more sensitive than native MnP as a result of lack of glycosylation
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
Schizophyllum sp.
-
stable for more than 1 months
25
-
Schizophyllum sp.
-
half-life: 24 h
30
-
Schizophyllum sp.
-
half-life: 13 h
35
-
-
pH 4.5, 1 h, stable up to
35
-
Schizophyllum sp.
-
half-life: 6 h
37
-
-
recombinant MnP: 5 min, 50% loss of activity, A48C/A63C double mutant MnP: relatively stable
40
-
-
stable below
40
-
-
60 min, stable
40
-
Schizophyllum sp.
-
half-life: 1 h
45
-
-
pH 4.5, 1 h, about 40% loss of activity
47
-
-
pH 4.5, 1 h, about 60% loss of activity
49
-
-
wild-type MnP, MnP F190Y and MnP F190L: 330 s, 50% loss of activity, MnP F190I: 30 s, 50% loss of activity, MnP F190A: 5 s, complete loss of activity
50
70
-
the enzyme is rather unstable at 50, 60, and 70C, resulting in half-lives of 660, 105, and 41 s, respectively
50
-
-
20% decrease of activity after 20 min, no further loss of activity after 60 min
50
-
-
stable up to
52
-
-
recombinant MnP: 20 s, 50% loss of activity, A48C/A63C double mutant MnP: 2 min, 50% loss of activity
55
-
-
more thermostable than MnP from Phanerochaete chrysosporium with half-lives 15-40fold longer at 55C, Mn2+, Cd2+ and Zn2+ enhances thermostability
55
-
-
pH 4.5, 1.4 min, 50% loss of activity, both Mn2+ and Cd2+ protect MnP from thermal denaturation more efficiently than Ca2+ at pH 4.5, extending the half-life more than 2fold at 1 mM, combination of 0.5 mM Mn2+ and 0.5 mM Cd2+ extends the half-life more than 10fold
55
-
-
pH 4.5, 3 min, wild-type enzyme loses about 75% of the initial activity, 50% loss of activity after 3 min in presence of 1 mM ferric chloride. pH 4.5, 2 min, recombinant enzyme loses about 90% of the initial activity, about 45% loss of activity in presence of 1 mM ferric chloride
60
-
-
80% loss of activity after 10 min, complete inactivation after 40 min
60
-
-
60 min, enzyme retains more than 60% of the initial activity
60
-
-
2 h, 45% loss of activity
65
-
-
pH 4.5, 1 h, complete loss of activity
70
-
-
complete inactivation after 5 min
100
-
-
complete inactivation after 5 min, 20% of original activity recovered after storage of heat-inactivated protein for 1 h at 0C, no reactivation possible after boiling for 20 min
100
-
-
complete inactivation after boiling for 5 min
additional information
-
-
Mn2+ protects against thermal inactivation, probably due to active site protection
additional information
-
-
polyethylene glycol-modified enzyme shows greater stability to higher temperatures than native enzyme
additional information
-
Q02567
very sensitive to thermal treatment
additional information
-
-
susceptible to thermal inactivation due to the loss of calcium, calcium content after thermal treatment at 37C for 15 min: 1.5 mol per mol of native MnP, 1 mol per mol of recombinant MnP and 1.3 mol per mol of A48C/A63C double mutant MnP, biphasic inactivation kinetics, recombinant MnP is more sensitive than native MnP as a result of the lack of glycosylation, calcium decreases the rate of thermal inactivation and reactivates MnP up to 50% of its original activity, while EGTA increases the rate of inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
enzyme retains more than 60% of the initial activity after exposure to 10 mM hydrogen peroxide for 5 min at 37C
-
calcium stabilizes
-
CHAPS stabilizes
-
complete loss of activity after 1 h in 2 mM KCN
-
enzyme is more stable in carbon-limited cultures than in nitrogen-limited cultures
-
heat-inactivated protein, 100C for 5 min, regains 80% of original activity by storage at 0C for 1 h
-
Mn2+ and bovine serum albumin stabilize
-
no inactivation after 5 h in 50 mM Na-tartrate buffer, pH 4.5, with 2 mM nitrilotriacetate, 0.5 mM iodoacetamide or 2 mM PMSF
-
prolonged dialysis inactivates
-
stable to lyophilization
-
enzyme is very stable when the molar concentration of H2O2 is 10times of the concentration of the enzyme. When the H2O2 concentration is 250fold and 1000fold of the MnP concentration, the MnP activity decreases by 14% and 45%, respectively, in the first 15 min and remains the same thereafter. When the H2O2 concentration is 5000times of the enzyme concentration, the enzyme activity rapidly decreases in 30 min and then continues to decrease, but at a slower rate
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
higher resistance to H2O2 than MnP from Phanerochaete chrysosporium
-
439847
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 10% decrease of activity after 3 months
-
-20C, concentrated preparation, 1 mg/ml, 3 months, stable
-
-20C, freeze-dried preparation, up to a year, stable
-
23C, crude, stable
-
4C, pH 4.5, purified enzyme in 50 mM Na-tartrate buffer is stable for 1 week
-
frozen, tartrate buffer, pH 4.5, 6 months, stable
-
4C, 72 h, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
MnP1 and MnP2
-
partial purification
-
24fold purification
-
2 isoenzymes: BOS1 and BOS2
Bjerkandera sp.
-
from Ceriporiopsis subvermispora by gel filtration and chromatography on a Mono-Q column
-
partial purification
-
-
Deuteromycotina sp.
-
148fold purification of MnP1 and 157fold purification of MnP2
-
extract is loaded onto a HiPREP26/10 desalting column followd by chromatography on a DEAE-Sepharose and a MonoQ HR5/5 column, finally the active fractions are applied to CIM QA Disks
-
purification of recombinant MnP, expressed in Phanerochaete chrysosporium
-
enzymes are extracted with 50 mM citrate-phosphate buffer at pH 4.0, 5.0 and 6.0 at 10C and 25C
-
MnP1: 19fold purification
-
purification of a protein complex containing MnP, laccase and beta-glucosidase activities
-
using a Toyopearl Butyl-650M, a Toyopearl DEAE-650 and a Superdex 75 HR 10/30 column
B5U990
purification scheme involves ultrafiltration, affinity chromatography on concanavalin-A Sepharose and gel filtration; ultrafiltration, Concanavalin-A Sepharose column chromatography and Superdex 75 gel filtration
-
from stem juice
-
-
Nematoloma frowardii
-
11.1fold purification
-
12fold purification; 3 isozymes
-
8.1-16fold purification
-
affinity chromatography on blue agarose: isozyme H4 95% pure, followed by preparative isoelectric focusing: isozymes H3 and H5 pure
-
isoenzyme H4; purification of recombinant A48C/A63C double mutant MnP, expressed in Escherichia coli
-
isoenzymes H4 and H5
-
partial purification
-
purification of MnPs from the mutants F190Y, F190L, F190I and F190A
-
purification of recombinant MnP, expressed in Escherichia coli
Q02567
purification of the mutant enzymes R177D, R177E, R177N and R177Q
-
MnPI, MnPII and MnPIII
-
partial purification
-
25fold purification; MnP1 and MnP2
-
MnP1 and MnP2
-
35.8fold purification
-
MnP2 and MnP3, purified from poplar culture
-
-
Schizophyllum sp.
-
partial purification, MnP2 and MnP3 are not separated
-
3 isoenzymes
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
isolation of the cDNAs encoding MnP isoenzymes: coding sequences of IZ-MnP1 cDNA with 1152 bp and IZ-MnP2 cDNA with 1155 bp in length, 2 copies of DNA encoding MnP isoenzymes exist in genomic DNA, 4 isoenzymes are generated as products of 2 genes by the difference of posttranslational modification
Deuteromycotina sp.
-
expression of mnp2 gene encoding MnP in Phanerochaete chrysosporium
-
MnP1 and MnP2 are encoded by different genes
-
lemnp2 is cloned by 3'-RACE using cDNA that is synthesized from mycelial RNA
B5U990
cDNA encoding MnP2 is cloned and expressed in Escherichia coli BL21(DE3)LysS
Q02567
cDNA sequence encoding a MnP isoenzyme is determined
-
cDNA sequences of several MnP-encoding genes, including mnp1, mnp2 and mnp3
-
expression in Pichia pastoris
-
expression in Pichia pastoris alphaMnP-1. Production of recombinant manganese peroxidase is highest at pH 6, with rMnP concentrations in the medium declining rapidly at pH less than 5.5, although cell growth rates are similar from pH 4-7
-
expression of A48C/A63C double mutant mnp gene in Escherichia coli XL-1 Blue
-
into the vector pET-22b, used for in vitro transcription and translation in a wheat germ extract system
-
isoenzymes H3, H4 and H5 are encoded by different genes and differentially regulated
-
mutant genes F190Y, F190L, F190I and F190A are subcloned and expressed in Escherichia coli XL-1 Blue and DH5alphaF
-
three differentexpression vectors are constructed: pZBMNP contains the native Phanerochaete chrysosporium fungal secretion signal, palphaAMNP contains an alpha-factor secretion signal derived from Saccharomyces cerevisiae, and pZBIMNP has no secretion signal and is used for intracellular expression
-
isoenzymes MnPI, MnPII and MnPIII are encoded by separate genes
-
cloning and sequencing of the gene encoding MnP2, promoter region is analyzed, nucleotide sequence of the cDNA encoding MnP1, mnp1 is located on chromosome IV, mnp2 on chromosome VI and mnp3 on chromosome V
-
isoenzymes are encoded by different genes
-
cloning of a full MnP cDNA from Trametes versicolor, and introducing an extra copy of the MnP gene under the control of a glyceraldehyde-3-phosphate dehydrogenase gene promoter from Aspergillus nidulans, into the genome of the wild type strain using a genetic transformation procedure. The gene is cloned and transferred into an expression vector (pBARGPE1) carrying a phosphinothricin resistance gene (bar) as a selectable marker to yield the expression vector, pBARTvMnP2. Transformants are generated through genetic transformation using pBARTvMnP2
Q6KB19
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
enyzme synthesis is species- and strain-dependent
-
copper increases the transcript levels of the manganese peroxidase genes mnp1 and mnp2
-
copper increases the transcript levels of the manganese peroxidase genes mnp1 and mnp2
Ceriporiopsis subvermispora FP-105752
-
-
the presence of laccase activity in the medium with sawdust probably depresses the expression of MnP
-
MnP is produced in media with sawdust
-
the presence of laccase activity in the medium with sawdust probably depresses the expression of MnP
Inocutis jamaicensis MVHC11379
-
-
MnP is produced in media with sawdust
Inocutis jamaicensis MVHC11379
-
-
the optimum temperature for MnP production is 37C. The amount of MnP registered at this temperature is 2.4 and 2.1times higher than that obtained in the treatments incubated at 30C
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
A48C/A63C
-
A48C and A63C double mutant with an engineered disulfide bond near the distal calcium binding site to restrict the movement of helix B upon loss of calcium and to stabilize against this loss, thermal and pH-stability is improved compared with that of native and recombinant MnP, thermally treated enzyme contains one calcium and retains a percentage of its activity
E35Q
-
engineered mutant
F190A
-
mutant MnP: apparent Km-value for ferrocyanide oxidation is 1/8 of that for wild-type MnP and kcat is 4fold greater than that for wild-type enzyme, mutant enzyme is significantly destabilized to thermal denaturation, unstable at 37C, rates of spontaneous reduction of the oxidized intermediates, compound I and II, are dramatically increased compared with those for the wild-type MnP
F190I
-
mutant enzyme is significantly destabilized to thermal denaturation, unstable at 37C, rates of spontaneous reduction of the oxidized intermediates, compound I and II, are 2fold greater than those for the wild-type MnP
F190L
-
rates of spontaneous reduction of the oxidized intermediates, compound I and II, are 2fold greater than those for the wild-type MnP
F190Y
-
engineered mutant
M237L
Q02567
engineered mutant
M273L
Q02567
mutant with high H2O2 resistance, i.e. 4.1fold higher than that of wild-type, Met-273 is located near the active site pocket and is converted to a non-oxidizable Leu
M67L
Q02567
engineered mutant
N131D
-
mutant displays a similar catalysis pattern to that of wild-type enzyme, Asn131 is the only potential glycosylation site
N81S
Q02567
mutant enzyme is not inhibited by 1 mM H2O2, H2O2-dependency is 5.5fold higher than that of wild-type, engineering of Asn-81, which might have conformational changes due to the environment of the pocket, to a non-bulky and non-oxidizable Ser
R177A
-
mutant with reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35
R177D
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
R177E
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
R177K
-
mutant with reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35
R177N
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
R177Q
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
R42A
-
mutant displays a similar catalysis pattern to that of wild-type enzyme, Arg42 is forming the peroxide binding pocket
S168W
-
mutant can oxidize both Mn2+ and typical lignin peroxidase substrates such as veratryl alcohol
F190A
Phanerochaete chrysosporium OGC101
-
mutant MnP: apparent Km-value for ferrocyanide oxidation is 1/8 of that for wild-type MnP and kcat is 4fold greater than that for wild-type enzyme, mutant enzyme is significantly destabilized to thermal denaturation, unstable at 37C, rates of spontaneous reduction of the oxidized intermediates, compound I and II, are dramatically increased compared with those for the wild-type MnP
-
F190I
Phanerochaete chrysosporium OGC101
-
mutant enzyme is significantly destabilized to thermal denaturation, unstable at 37C, rates of spontaneous reduction of the oxidized intermediates, compound I and II, are 2fold greater than those for the wild-type MnP
-
F190L
Phanerochaete chrysosporium OGC101
-
rates of spontaneous reduction of the oxidized intermediates, compound I and II, are 2fold greater than those for the wild-type MnP
-
F190Y
Phanerochaete chrysosporium OGC101
-
engineered mutant
-
R177A
Phanerochaete chrysosporium OGC101
-
mutant with reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35
-
R177D
Phanerochaete chrysosporium OGC101
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
-
R177E
Phanerochaete chrysosporium OGC101
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
-
R177K
Phanerochaete chrysosporium OGC101
-
mutant with reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35
-
R177N
Phanerochaete chrysosporium OGC101
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
industry
-
the ligninolytic enzymes of Basidiomycete are of fundamental importance for the efficient bioconversion of plant residues and they are prospective for the various biotechnological applications in pulp and paper, food, textile and dye industries, bioremediation, cosmetics, analytic biochemistry, and many others
degradation
-
various aspects of the biotechnological uses of these fungi have been studied regarding the nonspecific ligninolytic system of white-red fungi such as the degradation of industrial textile dye effluents and various xenobiotics
environmental protection
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polycyclic aromatic hydrocarbon degradation
industry
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the ligninolytic enzymes of Basidiomycete are of fundamental importance for the efficient bioconversion of plant residues and they are prospective for the various biotechnological applications in pulp and paper, food, textile and dye industries, bioremediation, cosmetics, analytic biochemistry, and many others
environmental protection
Bjerkandera adusta UAMH
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polycyclic aromatic hydrocarbon degradation
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paper production
Bjerkandera sp.
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bleaching of paper pulp
paper production
Bjerkandera sp.
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manganese peroxidase produced by the white-rot fungus Bjerkandera sp. strain BOS55 is used for lignin oxidation and bleaching of eucalyptus oxygen delignified kraft pulp
paper production
Bjerkandera sp. BOS55
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bleaching of paper pulp; manganese peroxidase produced by the white-rot fungus Bjerkandera sp. strain BOS55 is used for lignin oxidation and bleaching of eucalyptus oxygen delignified kraft pulp
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degradation
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biomimmetic decrosslinking with enzyme or metal complex-catalyzed reactions will enable the development of new devulcanizing strategies for the safe disposal and recycling of waste vulcanized rubber products
industry
-
the ligninolytic enzymes of Basidiomycete are of fundamental importance for the efficient bioconversion of plant residues and they are prospective for the various biotechnological applications in pulp and paper, food, textile and dye industries, bioremediation, cosmetics, analytic biochemistry, and many others
environmental protection
Deuteromycotina sp.
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degradation of recalcitrant high-molecular-mass compounds, such as nylon and melanin, degradation of xenobiotic compounds, bioremediation, decolorization of wastewater
paper production
Deuteromycotina sp.
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biobleaching of kraft pulp
industry
-
the ligninolytic enzymes of Basidiomycete are of fundamental importance for the efficient bioconversion of plant residues and they are prospective for the various biotechnological applications in pulp and paper, food, textile and dye industries, bioremediation, cosmetics, analytic biochemistry, and many others
degradation
B5U990
lingnin-degrading enzymes possess oxidative activity against phenolic compoundss, which can be used for bioremediation, biobleaching, and biofuel production
environmental protection
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key enzyme for degradation of environmentally persistent xenobiotics such as pentachlorophenol and dioxins
degradation
Lentinula edodes SR-1
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lingnin-degrading enzymes possess oxidative activity against phenolic compoundss, which can be used for bioremediation, biobleaching, and biofuel production
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biofuel production
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applications of recombinant enzyme in the pulp and paper industry and in the processing of lignocellulosic materials for ethanol and biofuels production
degradation
-
Mn peroxidases are of much interest biotechnologically because of their potentially applications in bioremdeial waste treatment and in catalyzing difficult chemical transfromations
environmental protection
-
degradation of recalcitrant pollutants
environmental protection
-
thiol-mediated degradation of dimeric model compounds and of polymeric lignin by MnP has potential applications in the degradation of industrial lignins
environmental protection
-
-
environmental protection
-
mediated system of degradation is potentially valuable for degradation of synthetic polymers and of environmental pollutants
paper production
-
bleaching of paper pulp
paper production
-
mediated system of degradation is potentially valuable for pulp and paper industries
paper production
-
applications of recombinant enzyme in the pulp and paper industry and in the processing of lignocellulosic materials for ethanol and biofuels production
environmental protection
Phanerochaete chrysosporium ME446
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-
-
paper production
Phanerochaete chrysosporium ME446
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-
-
environmental protection
Phanerochaete chrysosporium OGC101
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thiol-mediated degradation of dimeric model compounds and of polymeric lignin by MnP has potential applications in the degradation of industrial lignins
-
environmental protection
Phanerochaete chrysosporium VKM F-1767
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degradation of recalcitrant pollutants
-
paper production
Phanerochaete chrysosporium VKM F-1767
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bleaching of paper pulp
-
degradation
-
enzyme is able to detoxify aflatoxin B1. 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
degradation
Phanerochaete sordida YK-624
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enzyme is able to detoxify aflatoxin B1. 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
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nutrition
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biotechnological applications related to animal feeding
paper production
-
preferential degradation of lignin in wheat straw, an important property for biotechnological applications related to pulp and paper industry
paper production
-
-
nutrition
-
biotechnological applications related to animal feeding
paper production
-
preferential degradation of lignin in wheat straw, an important property for biotechnological applications related to pulp and paper industry
paper production
-
-
nutrition
Pleurotus ostreatus CBS 411.71
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biotechnological applications related to animal feeding
-
paper production
Pleurotus ostreatus CBS 411.71
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preferential degradation of lignin in wheat straw, an important property for biotechnological applications related to pulp and paper industry
-
industry
-
the ligninolytic enzymes of Basidiomycete are of fundamental importance for the efficient bioconversion of plant residues and they are prospective for the various biotechnological applications in pulp and paper, food, textile and dye industries, bioremediation, cosmetics, analytic biochemistry, and many others
biotechnology
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biotechnological applications require large amounts of low-cost enzymes, one of the appropriate approaches for this is to utilize the potential of lignocellulosic wastes, some of which may contain significant concentrations of soluble carbohydrates and inducers of enzyme synthesis, ensuring efficient production of ligninolytic enzymes
industry
-
the ligninolytic enzymes of Basidiomycete are of fundamental importance for the efficient bioconversion of plant residues and they are prospective for the various biotechnological applications in pulp and paper, food, textile and dye industries, bioremediation, cosmetics, analytic biochemistry, and many others