Enzyme-catalyzed synthesis of furanosyl nucleotides.
A bacterial alpha-d-glucopyranosyl-1-phosphate thymidylyltransferase was found to couple four hexofuranosyl-1-phosphates, as well as a pentofuranosyl-1-phosphate, with deoxythymidine 5'-triphosphate, providing access to furanosyl nucleotides. The enzymatic reaction mixtures were analyzed by electrospray ionization mass spectrometry and NMR spectroscopy to determine the anomeric stereochemistry of furanosyl nucleotide products. This is the first demonstration of a nucleotidylyltransferase discriminating between diastereomeric mixtures of sugar-1-phosphates to produce stereopure, biologically relevant furanosyl nucleotides.
Timmons
Shannon C
SC
Department of Chemistry, Dalhousie University, Halifax, Nova Scotia, Canada.
Hui
Joseph P M
JP
Pearson
Jessica L
JL
Peltier
Pauline
P
Daniellou
Richard
R
Nugier-Chauvin
Caroline
C
Soo
Evelyn C
EC
Syvitski
Ray T
RT
Ferrières
Vincent
V
Jakeman
David L
DL
D002384:Catalysis; D015394:Molecular Structure; D009711:Nucleotides / Q000138:chemical synthesis* / Q000737:chemistry; D009713:Nucleotidyltransferases / Q000378:metabolism*; D013237:Stereoisomerism; D013379:Substrate Specificity
D009711:Nucleotides; C523475:Glc-1-P thymidyltransferase, Streptomyces globisporus; D009713:Nucleotidyltransferases