PMID:2494074
| Citation |
Eberhard, M and Kirschner, K (1989) Modification of a catalytically important residue of indoleglycerol-phosphate synthase from Escherichia coli. FEBS Lett. 245:219-22 |
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| Abstract |
The active-site residues of indoleglycerol-phosphate synthase from Escherichia coli were tentatively localized by comparing crystallographic data with the amino acid identities among the known indoleglycerol-phosphate synthase sequences. To test the validity of the resulting model of catalysis one of the residues in the presumptive active site, Lys 55, was changed to serine using oligonucleotide-directed mutagenesis. The specificity constant kcat/Km of the mutant is 3 x 10(4)-times lower than that of the wild-type enzyme, due to a 60-fold decrease in kcat and a 450-fold increase in Km. This finding shows that Lys 55 is important for both catalysis and substrate binding. |
| Links | |
| Keywords |
Amino Acid Sequence; Binding Sites; Carboxy-Lyases/metabolism; Catalysis; Escherichia coli/enzymology; Indole-3-Glycerol-Phosphate Synthase/genetics; Indole-3-Glycerol-Phosphate Synthase/metabolism; Lysine; Mutation; Serine; Structure-Activity Relationship |
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