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Literature summary extracted from

  • Thoden, J.B.; Ruzicka, F.J.; Frey, P.A.; Rayment, I.; Holden, H.M.
    Structural analysis of the H166G site-directed mutant of galactose 1-phosphate uridylyltransferase complexed with either UDP-glucose or UDP-galactose: detailed description of the nucleotide sugar binding site (1997), Biochemistry, 36, 1212-1222.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.7.12 H166G mutant enzyme/UDP-glucose or UDP-galactose complexes, X-ray diffraction structure determination and analysis Escherichia coli
2.7.7.12 uridyl/enzyme complex, X-ray diffraction structure determination and analysis Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.12 H166G
-
 Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.12 Escherichia coli P09148
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.7.12 UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose active site nucleophil H166 Escherichia coli
a
2.7.7.12 UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose amino acid residues of both subunits contribute to the active site Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.12 UDP-glucose + alpha-D-galactose 1-phosphate
-
 Escherichia coli alpha-D-glucose 1-phosphate + UDP-galactose
-
 r