|Matsuhashi, M.; Strominger, J.L.
|Thymidine diphosphate 4-acetamido-2,6-dideoxyhexoses. 3. Purification and properties of thymidine diphosphate 4-keto-6-deoxy-D-glucose transaminase from Escherichia coli strain B.
|J Biol Chem
|A pyridoxal phosphate-requiring transaminase which catalyzes a reversible reaction between thymidine diphosphate 4-keto-6-deoxy-n-glucose and L-glutamate to form
TDP-4-amino-4,6-dideoxy-u-glucose and cY-ketoglutarate
has been purified 28-fold from an extract of Escherichia coli strain B. Some properties of the enzyme are reported.
Transaminase activity is widely distributed among strains of
E. coli, Salmonella, and Pasteurella pseudofuberculosis,
but among the organisms studied only E. coli strain B has a
transaminase which catalyzes the synthesis of TDP-4-
amino-4,6-dideoxy-n-glucose. The other organisms have
an enzyme which catalyzes the synthesis of the nucleotide
containing the sugar with the n-galacto configuration.