Modification of a catalytically important residue of indoleglycerol-phosphate synthase from Escherichia coli

FEBS Letters
M Eberhard, K Kirschner

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.

References

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Citations

May 30, 1998·Protein Science : a Publication of the Protein Society·B DarimontK Kirschner
Sep 29, 2004·Proceedings of the National Academy of Sciences of the United States of America·Devleena Mazumder-Shivakumar, Thomas C Bruice
Dec 12, 2012·Biochemistry·Sandra SchleeReinhard Sterner

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