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• W2097431044 startingPage "963" @default.
• W2097431044 abstract "Although many mutations in the ornithine transcarbamylase gene have been correlated with 'late onset' of hyperammonemia in patients, the effects of these mutations on enzyme function are largely unknown. Three recurrent mutations (R40H, R277W and R277Q) found in patients with 'late onset' disease were incorporated into 'mature' human ornithine transcarbamylase cDNA and overexpressed in Escherichia coli. The three recombinant mutant enzymes were purified to homogeneity on an affinity column and their biochemical characteristics were compared to the wild type enzyme. The R277W and R277Q mutants display markedly reduced affinity for L-ornithine, loss of substrate inhibition, alkaline shift of pH optimum, and reduced thermal stability compared to the wild type enzyme. These differences, particularly the reduced affinity for L-ornithine, are sufficient to account for their biochemical effects. In contrast, the 'mature' R40H mutant was biochemically indistinguishable from the wild type enzyme in vitro." @default.
• W2097431044 created "2016-06-24" @default.
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• W2097431044 date "1997-06-01" @default.
• W2097431044 modified "2023-09-25" @default.
• W2097431044 title "‘Late Onset’ Ornithine Transcarbamylase Deficiency: Function of Three Purified Recombinant Mutant Enzymes" @default.
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• W2097431044 doi "https://doi.org/10.1093/hmg/6.6.963" @default.
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