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首页> 外文期刊>The FEBS journal >From feedback inhibition to allostery: the enduringexample of aspartate transcarbamoylase
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From feedback inhibition to allostery: the enduringexample of aspartate transcarbamoylase

机译：从反馈抑制到变构：天冬氨酸转氨甲酰酶的持久例子

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Aspartate transcarbamoylase (ATCase) of Escherichia coli, the first enzymeof the pyrimidine biosynthetic pathway, is inhibited by CTP and UTP, thenucleotide end-products of the pathway. First discovered by Yates andPardee in 1956 [Yates R & Pardee AB (1956) J Biol Chem 221, 743–756;Yates RA & Pardee AB (1956) J Biol Chem 221, 757–770], these interactionsestablish feedback inhibition in vivo, a key means of metabolic regulationby which end-product production by the pathway is adjusted to endproductusage in macromolecule synthesis. Activation of the enzyme by thepurine nucleotide ATP may also have regulatory significance. ATCase andthreonine deaminase of E. coli were the first enzymes to be characterizedwith regard to their allosteric properties, namely, sigmoidal saturation withregard to substrates, reflecting cooperative ligand binding at the active site,and inhibition and activation by nucleotides of very different chemicalstructure from the substrates. In the case of ATCase, the nucleotides bindat regulatory sites located on protein subunits different from those bearingthe active sites. The early characterization of ATCase proved useful in the1965 conceptualization of the allosteric transition by Monod, Wyman, andChangeux [Monod J et al. (1965) J Mol Biol 12, 88–118], and the proteinin subsequent years has proved useful in the experimental analysis of theinteractions of sites and of conformational changes in allosteric proteins.This is an account of the early years of work on ATCase, up to 1965.
机译：大肠杆菌的天冬氨酸转氨甲酰酶（ATCase）是嘧啶生物合成途径的首个酶，被该途径的核苷酸终产物CTP和UTP抑制。 Yates andPardee于1956年首次发现[Yates R＆Pardee AB（1956）J Biol Chem 221，743–756; Yates RA＆Pardee AB（1956）J Biol Chem 221，757–770]，这些相互作用在体内建立了反馈抑制作用，代谢调节的关键手段，通过该途径可以将通过途径产生的最终产物调整为大分子合成中的最终产物。嘌呤核苷酸ATP对酶的激活也可能具有调节意义。大肠杆菌的ATCase和苏氨酸脱氨酶是第一个因其变构特性而被表征的酶，即相对于底物呈S型饱和，反映了活性位点上的配合配体结合，以及与底物化学结构非常不同的核苷酸对核苷酸的抑制和激活。就ATCase而言，核苷酸结合位于蛋白质亚基上的调节位点，而该蛋白质亚基不同于具有活性位点的那些。 AnoCase的早期表征在Monod，Wyman和Changeux的1965年变构构想的概念化中被证明是有用的[Monod J et al。 （1965）J Mol Biol 12，88–118]，随后的蛋白质被证明可用于变构蛋白质的位点相互作用和构象变化的实验分析。这是对ATCase的早期研究的证明，直到1965年。

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