转酮醇酶的结构和功能机制,Biochimica et Biophysica Acta (BBA) |
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硫胺素二磷酸依赖性酶的研究似乎始于1937年,分离了酵母丙酮酸脱羧酶的辅酶,事实证明该酶是硫胺素的二磷酸酯。长期以来,这些研究主要集中在使α-酮酸脱羧的酶上,例如丙酮酸脱羧酶和丙酮酸脱氢酶复合物。转酮酶由Racker和Horecker于1953年独立发现(并由Racker命名)[1],直到1992年才受到关注,当时对酿酒酵母的酶进行了晶体X射线结构分析。被执行[2]。这些数据,以及定点诱变的结果,使得有可能详细了解硫胺素二磷酸依赖的催化机制。在转酮醇酶功能特性的研究中也取得了一些进展。关于转酮醇酶的最后一次综述相当完整,发表于1998年[3]。因此,本文的发表似乎还为时过早。
"点击查看英文标题和摘要" Structure and functioning mechanism of transketolase
Studies of thiamine diphosphate-dependent enzymes appear to have commenced in 1937, with the isolation of the coenzyme of yeast pyruvate decarboxylase, which was demonstrated to be a diphosphoric ester of thiamine. For quite a long time, these studies were largely focused on enzymes decarboxylating α-keto acids, such as pyruvate decarboxylase and pyruvate dehydrogenase complexes. Transketolase, discovered independently by Racker and Horecker in 1953 (and named by Racker) [1], did not receive much attention until 1992, when crystal X-ray structure analysis of the enzyme from Saccharomyces cerevisiae was performed [2]. These data, together with the results of site-directed mutagenesis, made it possible to understand in detail the mechanism of thiamine diphosphate-dependent catalysis. Some progress was also made in studies of the functional properties of transketolase. The last review on transketolase, which was fairly complete, appeared in 1998 [3]. Therefore, the publication of this paper should not seem premature. |
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