Identification of lysine 153 as a functionally important residue in UDP-galactose 4-epimerase from Escherichia coli

The role of lysine 153 in the action of UDP-galactose 4-epimerase from Escherichia coli has been investigated by site specific mutagenesis and kinetic and spectrophotometric analysis of the mutant enzymes. The crystal structure of UDP-galactose 4-epimerase shows that the binding of NAD+ to the coenz...

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Veröffentlicht in:	Biochemistry (Easton) 1993-12, Vol.32 (48), p.13231-13236
Hauptverfasser:	Swanson, Barbara A., Frey, Perry A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Binding Sites Biological and medical sciences Enzymes and enzyme inhibitors Escherichia coli Escherichia coli - enzymology Fundamental and applied biological sciences. Psychology Isomerases Kinetics Lysine - chemistry Models, Molecular Mutagenesis, Site-Directed NAD - metabolism Recombinant Proteins Spectrometry, Fluorescence Spectrophotometry, Ultraviolet Structure-Activity Relationship UDPglucose 4-Epimerase - chemistry Uridine Monophosphate - metabolism
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