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- W1972144893 abstract "Escherichia coli uronate isomerase and mannonate dehydrogenase were overexpressed in E. coli BL21(DE3)pLysS cells and purified to near-homogeneity. The kinetic properties of the two enzymes were investigated. The isomerase was found to be inhibited by EDTA and to be stimulated by Zn2+, Co2+, and Mn2+, but not by Mg2+ or Ca2+. Both enzymes were used to develop a sensitive spectrophotometric assay, in which d-glucuronate is converted to d-mannonate with concomitant oxidation of NADH to NAD+. The sensitivity of this assay permits the detection of less than 1 nmol d-glucuronate. This assay can also be used to determine the concentration of β-glucuronides and glucuronate 1-phosphate after enzymatic hydrolysis of these compounds with β-glucuronidase or alkaline phosphatase." @default.
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- W1972144893 date "2004-10-01" @default.
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- W1972144893 title "A spectrophotometric assay of d-glucuronate based on Escherichia coli uronate isomerase and mannonate dehydrogenase" @default.
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- W1972144893 doi "https://doi.org/10.1016/j.pep.2004.06.015" @default.
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