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B6db references: 15913355

type Journal Article
authors Zhao Z, Hong L, Liu HW.
title Characterization of protein encoded by spnR from the spinosyn gene cluster of Saccharopolyspora spinosa: mechanistic implications for forosamine biosynthesis
journal J Am Chem Soc
Activity 2.6.1.110
Family 2.6.1.110
sel selected
ui 15913355
year (2005)
volume 127
number 21
pages 7692-3
 
abstract d-Forosamine is a 4-N,N-(dimethylamino)-2,3,4,6-tetradeoxy-alpha-d-threo-hexopyranose found in spinosyn produced by Saccharopolyspora spinosa. Studies of spinosyn biosynthesis in S. spinosa led to the isolation of the entire biosynthetic gene cluster. Heterologous expression of spnR, one putative gene in forosamine biosynthesis, in E. coli and purification of the SpnR protein identified it as an aminotransferase catalyzing the conversion of the 4-keto-2,3,6-trideoxy sugar intermediate to the corresponding 4-amino sugar product. Identification of SpnR function relied on the use of a stable TMP-phosphonate sugar in place of TDP-sugar substrate to determine the function of SpnR. This strategy may find general applicability for designing probes to study enzymes which catalyze the transformation of labile deoxysugar intermediates.
last changed 2017/09/07 11:02

B6db references