Glucose-1-phosphate thymidylyltransferase () is an enzyme that catalyzes the chemical reaction
The enzyme characterised from Pseudomonas aeruginosa and Streptococcus faecalis combines thymidine triphosphate and glucose 1-phosphate to give thymidine diphosphate glucose, with pyrophosphate (PPi) as a byproduct. The mechanism of the reaction has been studied in Escherichia coli, where it is part of the biosynthetic pathway to L-rhamnose.
Nomenclature This enzyme is a transferase, specifically one transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is dTTP:alpha-D-glucose-1-phosphate thymidylyltransferase. Other names in common use include: glucose 1-phosphate thymidylyltransferase, dTDP-glucose synthase, dTDP-glucose pyrophosphorylase, thymidine diphosphoglucose pyrophosphorylase, thymidine diphosphate glucose pyrophosphorylase, and TDP-glucose pyrophosphorylase.
Structural studies As of late 2007, 19 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , , , and .
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