Synthesis of P(1)-Citronellyl-P(2)-alpha-D-pyranosyl pyrophosphates as potential substrates for the E. coli undecaprenyl-pyrophosphoryl-N-acetylglucoseaminyl transferase MurG.
P(1)-Citronellyl-P(2)-alpha-D-pyranosyl pyrophosphates containing alpha-D-N-acetylglucoseaminyl, alpha-D-glucosyl, and alpha-D-N-acetylmuramyl carbohydrates were synthesized and used in substrate specificity studies of the Escherichia coli MurG enzyme. Oxalyl chloride activation of citronellyl phosphate for coupling to alpha-D-pyranose-1-phosphates resulted in markedly improved yields over traditional Khorana-Moffatt and diphenyl chlorophosphate activation strategies.
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Johnson Research Foundation and the Department of Biochemistry and Biophysics, The University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6059, USA.
Behenna
D C
DC
Yu
M K
MK
Kruger
R G
RG
Szewczuk
L M
LM
McCafferty
D G
DG
D001425:Bacterial Outer Membrane Proteins; D011756:Diphosphates / Q000138:chemical synthesis* / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology*; D009682:Magnetic Resonance Spectroscopy; D017351:N-Acetylglucosaminyltransferases / Q000378:metabolism*; D021241:Spectrometry, Mass, Electrospray Ionization; D013379:Substrate Specificity
D001425:Bacterial Outer Membrane Proteins; D011756:Diphosphates; D017351:N-Acetylglucosaminyltransferases; C064057:UDP-N-acetylglucosamine-N-acetylmuramyl-(pentapeptide)pyrophosphoryl-undecaprenol N-acetylglucosamine transferase