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酵母丙酮酸羧化酶的序列和结构域结构。

Sequence and domain structure of yeast pyruvate carboxylase.

作者信息

Lim F, Morris C P, Occhiodoro F, Wallace J C

机构信息

Department of Biochemistry, University of Adelaide, Australia.

出版信息

J Biol Chem. 1988 Aug 15;263(23):11493-7.

PMID:3042770
Abstract

The nucleotide sequence of the yeast pyruvate carboxylase gene has been determined from a cloned fragment of yeast genomic DNA. The deduced translation product codes for a polypeptide of 1178 amino acids, having a calculated molecular weight of 130,100. The protein shows strong sequence homology to specific regions of other biotin carboxylases, lipoamide transferases, and carbamyl phosphate synthetases. The homologous regions suggest the presence of three subsites in the enzyme: a biotin attachment site, a keto acid-binding site, and an ATP-binding site. Partial proteolysis with a variety of proteases under nondenaturing conditions indicates the presence of structural domains corresponding to these subsites.

摘要

酵母丙酮酸羧化酶基因的核苷酸序列已从酵母基因组DNA的一个克隆片段中测定出来。推导的翻译产物编码一个由1178个氨基酸组成的多肽,计算分子量为130,100。该蛋白质与其他生物素羧化酶、硫辛酰胺转移酶和氨甲酰磷酸合成酶的特定区域显示出很强的序列同源性。这些同源区域表明该酶中存在三个亚位点:一个生物素附着位点、一个酮酸结合位点和一个ATP结合位点。在非变性条件下用多种蛋白酶进行部分蛋白水解表明存在与这些亚位点相对应的结构域。

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