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- W2021402187 abstract "Tyr-240 of the catalytic chain of aspartate transcarbamylase from E. coli has been substituted by Phe using site-directed mutagenesis. The regulatory mechanisms of the mutant enzyme have been shown to be slightly less effective than the wild-type enzyme [1]. A study of the structural consequences of the mutation using solution X-ray scattering and computer simulations is reported here. No significant change from the wild-type enzyme is detectable in the quaternary structure. Simulations suggest that the only effect of the mutation is an increased mobility of the mutated side chain." @default.
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- W2021402187 date "1989-04-24" @default.
- W2021402187 modified "2023-09-25" @default.
- W2021402187 title "Structural consequences of a one atom mutation on aspartate transcarbamylase from <i>E. coli</i>" @default.
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- W2021402187 doi "https://doi.org/10.1016/0014-5793(89)81371-7" @default.
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