62012-79-7Relevant articles and documents
Substrate specificity of the macrolide-glycosylating enzyme pair DesVII/DesVIII: Opportunities, limitations, and mechanistic hypotheses
Borisova, Svetlana A.,Zhang, Changsheng,Takahashi, Haruko,Zhang, Hua,Wong, Alexander W.,Thorson, Jon S.,Liu, Hung-Wen
, p. 2748 - 2753 (2006)
(Chemical Equation Presented) Two's Company: DesVII, a glycosyltransferase involved in the biosynthesis of macrolide antibiotics, is unusual in that it requires an additional protein partner, DesVIII, for its full activity. The level of substrate tolerance of the DesVII/DesVIII pair was explored.
One-pot four-enzyme synthesis of thymidinediphosphate-l-rhamnose
Li, Siqiang,Wang, Hong,Ma, Juncai,Gu, Guofeng,Chen, Zonggang,Guo, Zhongwu
, p. 13995 - 13998 (2016/12/09)
A new, robust one-pot four-enzyme synthetic method was developed for thymidinediphosphate-l-rhamnose starting from d-glucose-1-phosphate. The enzymes, Glc-1-P thymidylyltransferase, dTDP-Glc-4,6-dehydratase, dTDP-4-keto-6-deoxy-Glc-3,5-epimerase and dTDP-4-keto-Rha reductase were derived from Streptococcus pneumonia serotype 23F, expressed in Escherichia coli, and studied in detail to provide the first direct evidence for their functions.
Cooperation of two bifunctional enzymes in the biosynthesis and attachment of deoxysugars of the antitumor antibiotic mithramycin
Wang, Guojun,Pahari, Pallab,Kharel, Madan K.,Chen, Jing,Zhu, Haining,Vanlanen, Steven G.,Rohr, Jürgen
supporting information, p. 10638 - 10642 (2013/01/15)
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