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substitution of ferric heme by MnIII protoporphyrin IX greatly diminishes the peroxidase activity, but has little effect on the cyclooxygenase activity
-
the MnIII2-tyrosyl radical cofactor, not the diferric-tyrosyl radical one, is the active metallocofactor in vivo
the enzyme uses a dimanganese-tyrosyl radical (Mn(III)2-Y(*)) cofactor in vivo
the enzyme uses a dimanganese-tyrosyl radical (Mn(III)2-Y(*)) cofactor in vivo
the enzyme uses a dimanganese-tyrosyl radical (Mn(III)2-Y(*)) cofactor in vivo
the enzyme uses a dimanganese-tyrosyl radical (Mn(III)2-Y(*)) cofactor in vivo
the enzyme uses a dimanganese-tyrosyl radical (Mn(III)2-Y(*)) cofactor in vivo
the enzyme uses a dimanganese-tyrosyl radical (Mn(III)2-Y(*)) cofactor in vivo
the enzyme uses a dimanganese-tyrosyl radical (Mn(III)2-Y(*)) cofactor in vivo
the enzyme uses a dimanganese-tyrosyl radical (Mn(III)2-Y(*)) cofactor in vivo
the MnIII2-tyrosyl radical cofactor, not the diferric-tyrosyl radical one, is the active metallocofactor in vivo
the MnIII2-tyrosyl radical cofactor, not the diferric-tyrosyl radical one, is the active metallocofactor in vivo
the MnIII2-tyrosyl radical cofactor, not the diferric-tyrosyl radical one, is the active metallocofactor in vivo
the enzyme uses a dimanganese-tyrosyl radical (Mn(III)2-Y(*)) cofactor in vivo
the MnIII2-tyrosyl radical cofactor, not the diferric-tyrosyl radical one, is the active metallocofactor in vivo
dimanganese(III)-tyrosyl radical cofactor
the MnIII2-tyrosyl radical cofactor, not the diferric-tyrosyl radical one, is the active metallocofactor in vivo
the MnIII2-tyrosyl radical cofactor, not the diferric-tyrosyl radical one, is the active metallocofactor in vivo
the MnIII2-tyrosyl radical cofactor, not the diferric-tyrosyl radical one, is the active metallocofactor in vivo
the MnIII2-tyrosyl radical cofactor, not the diferric-tyrosyl radical one, is the active metallocofactor in vivo
the MnIII2-tyrosyl radical cofactor, not the diferric-tyrosyl radical one, is the active metallocofactor in vivo
the MnIII2-tyrosyl radical cofactor, not the diferric-tyrosyl radical one, is the active metallocofactor in vivo
the MnIII2-tyrosyl radical cofactor, not the diferric-tyrosyl radical one, is the active metallocofactor in vivo
the MnIII2-tyrosyl radical cofactor, not the diferric-tyrosyl radical one, is the active metallocofactor in vivo
the MnIII2-tyrosyl radical cofactor, not the diferric-tyrosyl radical one, is the active metallocofactor in vivo
the MnIII2-tyrosyl radical cofactor, not the diferric-tyrosyl radical one, is the active metallocofactor in vivo
the MnIII2-tyrosyl radical cofactor, not the diferric-tyrosyl radical one, is the active metallocofactor in vivo
the MnIII2-tyrosyl radical cofactor, not the diferric-tyrosyl radical one, is the active metallocofactor in vivo
the enzyme uses a dimanganese-tyrosyl radical (Mn(III)2-Y(*)) cofactor in vivo
dimanganese(III)-tyrosyl radical cofactor
dimanganese(III)-tyrosyl radical cofactor
dimanganese(III)-tyrosyl radical cofactor
dimanganese(III)-tyrosyl radical cofactor
dimanganese(III)-tyrosyl radical cofactor
dimanganese(III)-tyrosyl radical cofactor
dimanganese(III)-tyrosyl radical cofactor
dimanganese(III)-tyrosyl radical cofactor
dimanganese(III)-tyrosyl radical cofactor
dimanganese(III)-tyrosyl radical cofactor
dimanganese(III)-tyrosyl radical cofactor
dimanganese(III)-tyrosyl radical cofactor
dimanganese(III)-tyrosyl radical cofactor
dimanganese(III)-tyrosyl radical cofactor
the enzyme uses a dimanganese-tyrosyl radical (Mn(III)2-Y(*)) cofactor in vivo
the enzyme uses a dimanganese-tyrosyl radical (Mn(III)2-Y(*)) cofactor in vivo
the enzyme uses a dimanganese-tyrosyl radical (Mn(III)2-Y(*)) cofactor in vivo
the enzyme uses a dimanganese-tyrosyl radical (Mn(III)2-Y(*)) cofactor in vivo
the enzyme uses a dimanganese-tyrosyl radical (Mn(III)2-Y(*)) cofactor in vivo
the enzyme uses a dimanganese-tyrosyl radical (Mn(III)2-Y(*)) cofactor in vivo
dimanganese(III)-tyrosyl radical cofactor
the enzyme uses a dimanganese-tyrosyl radical (Mn(III)2-Y(*)) cofactor in vivo
treatment of the periodate-oxidized enzyme with ascorbate results in a substantioal decrease in absorption, forming a complex that is spectroscopically identified as a Mn3+ species. Mn3+ form has a 5fold higher specific activity than native recombinant oxalate oxidase.
-
enzyme contains one atom of Mn(III) per 110000 Da enzyme
-
Mn3+ may play an important role on effective binding of phosphate and acceleration of hydrolysis of phosphomonoesters at pH 4-6
-
required for activity. Up to 16% of the electron paramagnetic resonance-visible manganese is in the +3 oxidation state at low pH in the presence of succinate buffer
-
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276
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1991
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Appl. Environ. Microbiol.
57
1453-1460
Characteristics and N-terminal amino acid sequence of a manganese peroxidase purified from Lentinula edodes cultures grown on a commercial wood substrate
1990
Forrester, I.T.; Grabski, A.C.; Mishra, C.; Kelley, B.D.; Strickland, W.N.; Leatham, G.F.; Burgess, R.R.
Appl. Microbiol. Biotechnol.
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Thiol-mediated oxidation of nonphenolic lignin model compounds by manganese peroxidase of Phanerochaete chrysosporium
1989
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-
Manganese peroxidase from Phanerochaete chrysosporium
1988
Gold, M.H.; Glenn, J.K.
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-
Manganese peroxidase from Phanerochaete chrysosporium: Purification
1988
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Methods Enzymol.
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Mn-peroxidase from Bjerkandera adusta 90-41. Purification and substrate specificity
2000
Dzedzyulya, E.I.; Becker, E.G.
Biochemistry
65
707-712
Characteristics and N-terminal amino acid sequence of manganese peroxidase from solid substrate cultures of Agaricus bisporus
2001
Lankinen, V.P.; Bonnen, A.M.; Anton, L.H.; Wood, D.A.; Kalkkinen, N.; Hatakka, A.; Thurston, C.F.
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55
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Heterologous expression of a thermostable manganese peroxidase from Dichomitus squalens in Phanerochaete chrysosporium
2001
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Arch. Biochem. Biophys.
385
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Lentinula edodes produces a multicomponent protein complex containing manganese (II)-dependent peroxidase, laccase and beta-glucosidase
2001
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200
175-179
Role of arginine 177 in the MnII binding site of manganese peroxidase. Studies with R177D, R177E, R177N, and R177Q mutants
2000
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267
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Manganese peroxidase isoenzymes produced by Pleurotus ostreatus grown on wood sadwust
2000
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Arch. Biochem. Biophys.
376
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Purification, characterization, and chemical modification of manganese peroxidase from Bjerkandera adusta UAMH 8258
2002
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45
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Purification and characterization of two manganese peroxidase isoenzymes from the white-rot basidiomycete Dichomitus squalens
1996
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Biochim. Biophys. Acta
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Engineering of the H2O2-binding pocket region of a recombinant manganese peroxidase to be resistant to H2O2
2001
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Biochemical and molecular characterization of a manganese peroxidase isoenzyme from Pleurotus ostreatus
1997
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Manganese peroxidases of the white rot fungus Phanerochaete sordida
1994
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Characterization of manganese peroxidases from the hyperlignolytic fungus IZU-154
1996
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Purification and catalytic properties of two manganese peroxidase isoenzymes from Pleurotus eryngii
1996
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Large scale production of manganese-peroxidase using agaric white-rot fungi
2002
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-
Purification and characterization of a manganese peroxidases from the litter-decomposing basidiomycetes Agrocybe praecox and Stropharia coronilla
2002
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-
Review: Lignin conversion by manganese peroxidase (MnP)
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1997
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Biochemistry
36
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Engineering a disulfide bond in recombinant manganese peroxidase results in increased thermostability
2000
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Effects of cadmium on manganese peroxidase. Competitive inhibition of MnII oxidation and thermal stabilization of the enzyme
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2.0 A structure of prostaglandin H2 synthase-1 reconstituted with a manganese porphyrin cofactor
2006
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62
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Burst kinetics and redox transformations of the active site manganese ion in oxalate oxidase: Implications for the catalytic mechanism
2007
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Active cystathionine beta-synthase can be expressed in heme-free systems in the presence of metal-substituted porphyrins or a chemical chaperone
2008
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50
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Direct identification of a bacterial manganese(II) oxidase, the multicopper oxidase MnxG, from spores of several different marine Bacillus species
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2015
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Biogenic manganese-oxide mineralization is enhanced by an oxidative priming mechanism for the multi-copper oxidase, MnxEFG
2017
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