Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Ellen W Moomaw"'
Publikováno v:
PLoS ONE, Vol 12, Iss 5, p e0177164 (2017)
Oxalate oxidase is a manganese containing enzyme that catalyzes the oxidation of oxalate to carbon dioxide in a reaction that is coupled with the reduction of oxygen to hydrogen peroxide. Oxalate oxidase from Ceriporiopsis subvermispora (CsOxOx) is t
Externí odkaz:
https://doaj.org/article/f8847a2066ab437bb06efc0d499e59ce
Autor:
Ellen W Moomaw, Eric Hoffer, Patricia Moussatche, John C Salerno, Morgan Grant, Bridget Immelman, Richard Uberto, Andrew Ozarowski, Alexander Angerhofer
Publikováno v:
PLoS ONE, Vol 8, Iss 3, p e57933 (2013)
Ceriporiopsis subvermispora oxalate oxidase (CsOxOx) is the first bicupin enzyme identified that catalyzes manganese-dependent oxidation of oxalate. In previous work, we have shown that the dominant contribution to catalysis comes from the monoproton
Externí odkaz:
https://doaj.org/article/5f6b15c15673425392c4385fb5def7c4
Autor:
Richard Uberto, Ellen W Moomaw
Publikováno v:
PLoS ONE, Vol 8, Iss 9, p e74477 (2013)
The cupin superfamily is extremely diverse and includes catalytically inactive seed storage proteins, sugar-binding metal-independent epimerases, and metal-dependent enzymes possessing dioxygenase, decarboxylase, and other activities. Although numero
Externí odkaz:
https://doaj.org/article/d57ee09b6260408d8bba94f3485f8155
Autor:
Marc A Shuler, Maurizio Affer, Ellen W. Moomaw, Manu O. Platt, Meghan C. Ferrall-Fairbanks, Zachary T. Barry
Publikováno v:
Protein Science. 26:880-890
Multiple proteases in a system hydrolyze target substrates, but recent evidence indicates that some proteases will degrade other proteases as well. Cathepsin S hydrolysis of cathepsin K is one such example. These interactions may be uni- or bi-direct
Autor:
Lis Souza Rocha, Ellen W. Moomaw, Sofiene Abdellaoui, Patricia Moussatche, Hassan Rana, Shelley D. Minteer
Publikováno v:
Biochemistry and Biophysics Reports, Vol 5, Iss C, Pp 396-400 (2016)
Isothermal titration calorimetry (ITC) may be used to determine the kinetic parameters of enzyme-catalyzed reactions when neither products nor reactants are spectrophotometrically visible and when the reaction products are unknown. We report here the
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1747
Membrane inlet mass spectrometry (MIMS) is a reproducible and reliable method for the measurement of nitric oxide in aqueous solution with a lower limit of detection of 10 nM and a linear response to 50 μM. MIMS utilizes a semipermeable membrane to
Publikováno v:
Methods in Molecular Biology ISBN: 9781493976942
Membrane inlet mass spectrometry (MIMS) is a reproducible and reliable method for the measurement of nitric oxide in aqueous solution with a lower limit of detection of 10 nM and a linear response to 50 μM. MIMS utilizes a semipermeable membrane to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::00e31e78b03061c9bff98a283f05e0b6
https://doi.org/10.1007/978-1-4939-7695-9_4
https://doi.org/10.1007/978-1-4939-7695-9_4
Publikováno v:
Molecular Plant Pathology. 16:825-836
Summary Sclerotinia sclerotiorum pathogenesis requires the accumulation of high levels of oxalic acid (OA). To better understand the factors affecting OA accumulation, two putative oxalate decarboxylase (OxDC) genes (Ss-odc1 and Ss-odc2) were charact
Publikováno v:
Biochemical and Biophysical Research Communications. 450:750-754
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 proper
Characterization of Ceriporiopsis subvermispora bicupin oxalate oxidase expressed in Pichia pastoris
Autor:
Witcha Imaram, Eric Hoffer, Patricia Moussatche, Kelsey Uberto, Daniel Sledge, Crystal Bruce, Alexander Angerhofer, Ellen W. Moomaw, Nigel G. J. Richards, Christopher Brooks
Publikováno v:
Archives of Biochemistry and Biophysics. 509:100-107
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 ox