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Full-Text Articles in Physical Sciences and Mathematics
Characterization Of Ceriporiopsis Subvermispora Bicupin Oxalate Oxidase Expressed In Pichia Pastoris, Patricia Moussatche, Alexander Angerhofer, Witcha Imaram, Eric Hoffer, Kelsey Uberto, Christopher Brooks, Crystal Bruce, Daniel Sledge, Nigel G. J. Richards, Ellen W. Moomaw
Characterization Of Ceriporiopsis Subvermispora Bicupin Oxalate Oxidase Expressed In Pichia Pastoris, Patricia Moussatche, Alexander Angerhofer, Witcha Imaram, Eric Hoffer, Kelsey Uberto, Christopher Brooks, Crystal Bruce, Daniel Sledge, Nigel G. J. Richards, Ellen W. Moomaw
Ellen Moomaw
Oxalate oxidase (E.C. 1.2.3.4) catalyzes the oxygen-dependent oxidation of oxalate to carbon dioxide in a reaction that is coupled with the formation of hydrogen peroxide. Although there is currently no structural information available for oxalate oxidase fromCeriporiopsis subvermispora (CsOxOx), sequence data and homology modeling indicate that it is the first manganese-containing bicupin enzyme identified that catalyzes this reaction. Interestingly, CsOxOx shares greatest sequence homology with bicupin microbial oxalate decarboxylases (OxDC). We show that CsOxOx activity directly correlates with Mn content and other metals do not appear to be able to support catalysis. EPR spectra indicate that the Mn is present …
Membrane Inlet Mass Spectrometry Reveals That Ceriporiopsis Subvermispora Bicupin Oxalate Oxidase Is Inhibited By Nitric Oxide, Ellen Moomaw, Richard Uberto, Chingkuang Tu
Membrane Inlet Mass Spectrometry Reveals That Ceriporiopsis Subvermispora Bicupin Oxalate Oxidase Is Inhibited By Nitric Oxide, Ellen Moomaw, Richard Uberto, Chingkuang Tu
Ellen Moomaw
Membrane inlet mass spectrometry (MIMS) uses a semipermeable membrane as an inlet to a mass spectrometer for the measurement of the concentration of small uncharged molecules in solution. We report the use of MIMS to characterize the catalytic properties of oxalate oxidase (E.C. 1.2.3.4) fromCeriporiopsis subvermispora (CsOxOx). Oxalate oxidase is a manganese dependent enzyme that catalyzes the oxygen-dependent oxidation of oxalate to carbon dioxide in a reaction that is coupled with the formation of hydrogen peroxide. CsOxOx is the first bicupin enzyme identified that catalyzes this reaction. The MIMS method of measuring OxOx activity involves continuous, real-time direct detection of …
Characterization Of Ceriporiopsis Subvermispora Bicupin Oxalate Oxidase Expressed In Pichia Pastoris, Patricia Moussatche, Eric Hoffer, Ellen W. Moomaw, Et Al.
Characterization Of Ceriporiopsis Subvermispora Bicupin Oxalate Oxidase Expressed In Pichia Pastoris, Patricia Moussatche, Eric Hoffer, Ellen W. Moomaw, Et Al.
Ellen Moomaw
Oxalate oxidase (E.C. 1.2.3.4) catalyzes the oxygen-dependent oxidation of oxalate to carbon dioxide in a reaction that is coupled with the formation of hydrogen peroxide. Although there is currently no structural information available for oxalate oxidase from Ceriporiopsis subvermispora (CsOxOx), sequence data and homology modeling indicate that it is the first manganese-containing bicupin enzyme identified that catalyzes this reaction. Interestingly, CsOxOx shares greatest sequence homology with bicupin microbial oxalate decarboxylases (OxDC). We show that CsOxOx activity directly correlates with Mn content and other metals do not appear to be able to support catalysis. EPR spectra indicate that the Mn is …
Membrane Inlet Mass Spectrometry Reveals That Ceriporiopsis Subvermispora Bicupin Oxalate Oxidase Is Inhibited By Nitric Oxide, Ellen Moomaw, Richard Uberto, Chingkuang Tu
Membrane Inlet Mass Spectrometry Reveals That Ceriporiopsis Subvermispora Bicupin Oxalate Oxidase Is Inhibited By Nitric Oxide, Ellen Moomaw, Richard Uberto, Chingkuang Tu
Ellen Moomaw
Membrane inlet mass spectrometry (MIMS) uses a semipermeable membrane as an inlet to a mass spectrometer for the measurement of the concentration of small uncharged molecules in solution. We report the use of MIMS to characterize the catalytic properties of oxalate oxidase (E.C. 1.2.3.4) fromCeriporiopsis subvermispora (CsOxOx). Oxalate oxidase is a manganese dependent enzyme that catalyzes the oxygen-dependent oxidation of oxalate to carbon dioxide in a reaction that is coupled with the formation of hydrogen peroxide. CsOxOx is the first bicupin enzyme identified that catalyzes this reaction. The MIMS method of measuring OxOx activity involves continuous, real-time direct detection of …
Characterization Of Ceriporiopsis Subvermispora Bicupin Oxalate Oxidase Expressed In Pichia Pastoris, Patricia Moussatche, Eric Hoffer, Ellen W. Moomaw, Et Al.
Characterization Of Ceriporiopsis Subvermispora Bicupin Oxalate Oxidase Expressed In Pichia Pastoris, Patricia Moussatche, Eric Hoffer, Ellen W. Moomaw, Et Al.
Ellen Moomaw
Oxalate oxidase (E.C. 1.2.3.4) catalyzes the oxygen-dependent oxidation of oxalate to carbon dioxide in a reaction that is coupled with the formation of hydrogen peroxide. Although there is currently no structural information available for oxalate oxidase from Ceriporiopsis subvermispora (CsOxOx), sequence data and homology modeling indicate that it is the first manganese-containing bicupin enzyme identified that catalyzes this reaction. Interestingly, CsOxOx shares greatest sequence homology with bicupin microbial oxalate decarboxylases (OxDC). We show that CsOxOx activity directly correlates with Mn content and other metals do not appear to be able to support catalysis. EPR spectra indicate that the Mn is …