A hybrid proteolytic fragment of Escherichia coli aspartokinase I-homoserine dehydrogenase I. Structure, inhibition pattern, dissociation properties, and generation of two homodimers.
作者： A Fazel , Y Guillou , G N Cohen
DOI: 10.1016/S0021-9258(17)43952-4
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摘要: A hybrid dimeric fragment of Escherichia coli aspartokinase I-homoserine dehydrogenase I (Fazel, A., Muller, K., Le Bras, G., Garel, J.-R., Veron, M., and Cohen, G. N. (1983) Biochemistry 22, 158-165) has been purified shown to possess both homoserine activities is rather stable in the presence L-threonine. Its two are still inhibited by threonine, but noncooperatively contrast native protein. The activity found be more sensitive threonine than activity. In absence different chains (Mr = 89,000 + 59,000) dissociate first into monomers, this being followed pairing homologous form homodimers. L-threonine, homodimers do not re-form fragment. NH2-terminal analysis shows that correspond, respectively, dimer protein 2 X 89,000) a already described (Veron, Falcoz-Kelly, F., (1972) Eur. J. Biochem. 28, 520-527).
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sci-hub.st 参考文章(19)
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