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首页> 外文期刊>Biochemistry >Characterization of TDP-4-Keto-6-deoxy-D-glucose-3,4-ketoisomerase from the D-Mycaminose Biosynthetic Pathway of Streptomyces fradiae:In Vitro Activity and Substrate Specificity Studies1,
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Characterization of TDP-4-Keto-6-deoxy-D-glucose-3,4-ketoisomerase from the D-Mycaminose Biosynthetic Pathway of Streptomyces fradiae:In Vitro Activity and Substrate Specificity Studies1,

机译：从链霉菌的D-Mycaminose生物合成途径表征TDP-4-Keto-6-脱氧-D-葡萄糖-3,4-酮异构酶：体外活性和底物特异性研究1，

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Deoxysugars are critical structural elements for the bioactivity of many natural products.Ongoing work on elucidating a variety of deoxysugar biosynthetic pathways has paved the way for manipulation of these pathways for the generation of structurally diverse glycosylated natural products.In the course of this work,the biosynthesis of D-mycaminose in the tylosin pathway of Streptomyces fradiae was investigated.Attempts to reconstitute the entire mycaminose biosynthetic machinery in a heterologous host led to the discovery of a previously overlooked gene,tylla,encoding an enzyme thought to convert TDP-4-keto-6-deoxy-D-glucose to TDP-3-keto-6-deoxy-D-glucose,a 3,4-ketoisomerization reaction in the pathway.Tyl1a has now been overexpressed,purified,and assayed,and its activity has been verified by product analysis.Incubation of Tylla and the C-3 aminotransferase TylB,the next enzyme in the pathway,produced TDP-3-amino-3,6-dideoxy-D-glucose,confirming that these two enzymes act sequentially.Steady state kinetic parameters of the Tyl1a-catalyzed reaction were determined,and the ability of Tylla and TylB to process a C-2 deoxygenated substrate and a CDP-linked substrate was also demonstrated.Enzymes catalyzing 3,4-ketoisomerization of hexoses represent a new class of enzymes involved in unusual sugar biosynthesis.The fact that Tyl1a exhibits a relaxed substrate specificity holds potential for future deoxysugar biosynthetic engineering endeavors.
机译：脱氧糖是许多天然产物生物活性的关键结构要素。正在进行的阐明多种脱氧糖生物合成途径的工作为操纵这些途径以产生结构多样的糖基化天然产物铺平了道路。研究了链霉菌泰乐菌素途径中D-mycaminose的生物合成。试图在异源宿主中重建整个mycaminose生物合成机制的尝试导致发现了一个先前被忽视的基因tylla，该基因编码一种被认为可以转化TDP-4-keto的酶-6-脱氧-D-葡萄糖转化为TDP-3-酮-6-脱氧-D-葡萄糖，该途径中的3,4-酮异构化反应。现已过表达，纯化和测定Tyl1a，其活性已得到证实。 Tylla和该途径中的下一个酶C-3氨基转移酶TylB的温育产生了TDP-3-amino-3,6-dideoxy-D-glucose，证实这两种酶顺序起作用确定了Tyl1a催化反应的稳态动力学参数，并证明了Tylla和TylB处理C-2脱氧底物和CDP连接的底物的能力。催化己糖3,4-酮异构化的酶代表Tyl1a具有轻松的底物特异性这一事实为将来的脱氧糖生物合成工程研究提供了潜力。

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