首页> 外文学位 >A kinetic and synthetic study of 2-keto-3-deoxy-6-phosphogluconate aldolase toward the synthesis of 4,5-dihydroxy-D-threo-L-norvaline, 4-cis-hydroxyproline, bulgecinine and 4,5-dihydroxypipecolinc acid.
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A kinetic and synthetic study of 2-keto-3-deoxy-6-phosphogluconate aldolase toward the synthesis of 4,5-dihydroxy-D-threo-L-norvaline, 4-cis-hydroxyproline, bulgecinine and 4,5-dihydroxypipecolinc acid.

机译:动力学和合成研究2-酮-3-脱氧-6-磷酸葡糖醛酸醛缩酶对4,5-二羟基-D-苏-L-正缬氨酸,4-顺羟基脯氨酸,球蛋白和4,5-二羟基哌咯酸的合成。

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摘要

2-Keto-3-deoxy-6-phosphogluconate (KDPG) aldolase from Pseudomonas putida is examined for its utility as a biocatalyst in the stereoselective aldol condensation between pyruvate and aldehydes of varying steric and electronic structure. KDPG aldolase has been used to prepare stereospecific aldol condensation products with a C4-C5 erythro conformation. This class I aldolase is a representative member of the largest group of aldolases that utilize pyruvic acid as its nucleophilic substrate. Pyruvate forms a Schiff base with Lysine 144 in the active site and condenses with D-glyceraldehyde-3-phosphate (G-3-P) to yield the biological product, KDPG. This study demonstrates that aldehydes of varying size and substitution patterns including its natural substrate, G-3-P, are used as substrates and found to react at different rates in the presence of KDPG aldolase. In order to assess the substrate specificity of KDPG aldolase, kinetic constants,
机译:研究了恶臭假单胞菌的2-酮-3-脱氧-6-磷酸葡萄糖酸(KDPG)醛缩酶作为生物催化剂在丙酮酸与不同空间和电子结构的醛之间的立体选择性醛醇缩合中的生物催化剂的用途。 KDPG醛缩酶已用于制备具有C4-C5赤型构象的立体特异性醛醇缩合产物。此类I类醛缩酶是利用丙酮酸作为其亲核底物的最大醛缩酶类的代表成员。丙酮酸在活性位点与赖氨酸144形成席夫碱,并与D-甘油醛-3-磷酸酯(G-3-P)缩合,生成生物产物KDPG。这项研究表明,使用各种大小和取代方式的醛(包括其天然底物G-3-P)作为底物,发现在KDPG醛缩酶存在下,醛的反应速率不同。为了评估KDPG醛缩酶的底物特异性,动力学常数,

著录项

  • 作者

    Lewis, Ronald D., II.;

  • 作者单位

    Wesleyan University.;

  • 授予单位 Wesleyan University.;
  • 学科 Chemistry Organic.;Biology Molecular.
  • 学位 Ph.D.
  • 年度 1997
  • 页码 246 p.
  • 总页数 246
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

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