PMID: 6412746Jul 19, 1983Paper

L-serine binds to arginine-148 of the beta 2 subunit of Escherichia coli tryptophan synthase

Biochemistry
K Tanizawa, E W Miles

Abstract

Inactivation of the beta 2 subunit and of the alpha 2 beta 2 complex of tryptophan synthase of Escherichia coli by the arginine-specific dicarbonyl reagent phenylglyoxal results from modification of one arginyl residue per beta monomer. The substrate L-serine protects the holo beta 2 subunit and the holo alpha 2 beta 2 complex from both inactivation and arginine modification but has no effect on the inactivation or modification of the apo forms of the enzyme. This result and the finding that phenylglyoxal competes with L-serine in reactions catalyzed by both the holo beta 2 subunit and the holo alpha 2 beta 2 complex indicate that L-serine and phenylglyoxal both bind to the same essential arginyl residue in the holo beta 2 subunit. The apo beta 2 subunit is protected from phenylglyoxal inactivation much more effectively by phosphopyridoxyl-L-serine than by either pyridoxal phosphate or pyridoxine phosphate, both of which lack the L-serine moiety. The phenylglyoxal-modified apo beta 2 subunit binds pyridoxal phosphate and the alpha subunit but cannot bind L-serine or L-tryptophan. We conclude that the alpha-carboxyl group of L-serine and not the phosphate of pyridoxal phosphate binds to the essential arginyl residue in the beta ...Continue Reading

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Citations

Oct 1, 1988·Archives of Biochemistry and Biophysics·S R PadgetteG M Kishore
Jun 1, 1989·Proceedings of the National Academy of Sciences of the United States of America·M B BerlynG R Fink
Feb 25, 2003·Bioscience, Biotechnology, and Biochemistry·Nobuyoshi NakajimaHideaki Tsuji
Jun 4, 1993·Biochimica Et Biophysica Acta·P J White, K E Kendrick
May 1, 1985·Archives of Biochemistry and Biophysics·B TanciniC B Voltattorni
May 16, 2002·The Journal of Biological Chemistry·Christine Fehlner-GardinerGrant McClarty
Mar 15, 2002·Chemical Record : an Official Publication of the Chemical Society of Japan ... [et Al.]·E W Miles

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