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Characterization of Early Enzymes Involved in TDP‐Aminodideoxypentose Biosynthesis en Route to Indolocarbazole AT2433
Author(s) -
PeltierPain Pauline,
Singh Shanteri,
Thorson Jon S.
Publication year - 2015
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201500365
Subject(s) - calicheamicin , biosynthesis , biochemistry , dehydratase , xylose , enzyme , chemistry , secondary metabolism , nucleotide sugar , sugar , nucleotide , biology , fermentation , myeloid leukemia , gene , immunology
The characterization of TDP‐α‐ d ‐glucose dehydrogenase (AtmS8), TDP‐α‐ d ‐glucuronic acid decarboxylase (AtmS9), and TDP‐4‐keto‐α‐ d ‐xylose 2,3‐dehydratase (AtmS14), involved in Actinomadura melliaura AT2433 aminodideoxypentose biosynthesis, is reported. This study provides the first biochemical evidence that both deoxypentose and deoxyhexose biosynthetic pathways share common strategies for sugar 2,3‐dehydration/reduction and implicates the sugar nucleotide base specificity of AtmS14 as a potential mechanism for sugar nucleotide commitment to secondary metabolism. In addition, a re‐evaluation of the AtmS9 homologue involved in calicheamicin aminodeoxypentose biosynthesis (CalS9) reveals that CalS9 catalyzes UDP‐4‐keto‐α‐ d ‐xylose as the predominant product, rather than UDP‐α‐ d ‐xylose as previously reported. Cumulatively, this work provides additional fundamental insights regarding the biosynthesis of novel pentoses attached to complex bacterial secondary metabolites.