Summary
An overview of the recent results derived from X-ray crystallography, physical biochemical methods, rapid kinetic techniques and site-directed mutagenesis that have shaped current understanding of tryptophan synthase structure-function relationships is presented. An integrated mechanism relating the chemical transformations and metal ion activation to tunnel function and allosteric regulation is proposed.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Anderson, K. S., Miles, E. W. and Johnson, K A. (1991) Serine modulates substrate channeling in tryptophan synthase. A novel intersubunit triggering mechanism. J. Biol. Chem. 266: 8020–8033.
Bemasconi, C. (1976) Relaxation Kinetics, Academic Press, New York, Chapter 3.
Brzovic, P. S., Ngo, K., and Dunn, M. F. (1992a) Allosteric interactions coordinate catalytic activity between successive metabolic enzymes in the tryptophan synthase bienzyme complex. Biochemistry 31: 3831–3839.
Brzovic, P. S., Sawa, Y., Miles, E. W. and Dunn, M. F. (1992b) Evidence that mutations in a loop region of the a—subunit inhibit the transition from an open to a closed conformation in the tryptophan synthase bienzyme complex. J. Biol. Chem. 267: 13028–13038.
Brzovic, P. S., Kayastha, A. M., Miles, E. W. and Dunn, M. F. (1922c) Substitution of glutamic acid 109 by aspartic acid alters the substrate specificity and catalytic activity of the 13—subunit in the tryptophan synthase bienzyme complex from Salmonella typhimurium. Biochemistry 31: 1180–1190.
Brzovic, P. S., Hyde, C. C., Miles, E. W. and Dunn, M. F. (1993) Characterization of the functional role of a flexible loop in the the a—subunit of tryptophan synthase by rapid-scanning stopped-flow spectroscopy and site-directed mutagenesis. Biochemistry 32: 10404–10413.
Drewe, Jr., W. F. and Dunn, M. F. (1985) Detection and identification of intermediates in the reaction of L-serine with E. coli tryptophan synthase via rapid-scanning UV-visible spectroscopy. Biochemistry 24: 3977–3987.
Drewe, Jr., W. F. and Dunn, M. F. (1986) Characterization of the reaction of L-serine and indole with tryptophan synthase via rapid-scanning UV-visible spectroscopy. Biochemistry 25: 2494–2501.
Dunn, M. F., Aguilar, V., Brzovic, P. S., Drewe, W. F., Houben, K. F., Leja, C. A. and Roy, M. (1990) The tryptophan synthase bienzyme complex transfers indole between the a— and ß—sites via a 25–30 A-long tunnel. Biochemistry 29: 8598–8607.
Houben, K. F. and Dunn, M. F. (1990) Allosteric effects acting over a distance of 20–25 A in the E. coli tryptophan synthase bienzyme complex increase ligand affinity and cause redistribution of covalent intermediates. Biochemistry 29: 2421–2429. ßE109
Hyde, C. C., Ahmed, S. A., Padlan, E. A., Miles, E. W., and Davies, D. R. (1988) Three-dimensional structure of the tryptophan synthase a,ß, multienzyme complex from Salmonella typhimurium. J. Biol. Chem. 263: 17857–17871.
Kawasaki, H., Baurle, R., Zon, G., Ahmed, S., and Miles, E. W. (1987) Site-specific mutagenesis of the a—subunit of tryptophan synthase from Salmonella typhimurium. Changing arginine 179 to leucine alters the reciprocal transmission of substrate-induced conformational changes between the a and ß, subunits. J. Biol. Chem. 262: 10678–10683.
Kirschner, K., Lane, A. N. and Strasser, A. W. N. (1991) Reciprocal communication between the lyase and synthase active sites of the tryptophan synthase bienzyme complex. Biochemistry 30: 472–478.
Lane, A. N. and Kirschner, K. (1991) Mechanism of the physiological reaction catalyzed by tryptophan synthase from E. coli. Biochemistry 30: 479–484.
Miles, E. W. (1991) Structural basis for catalysis by tryptophan synthase. Adv. Enzymol. Relat. Areas Mol. Biol. 64: 93–172.
Nagata, S., Hyde. C. C. and Miles, E. W. (1989) The a—subunit of tryptophan synthase. Evidence that aspartic acid 60 is a catalytic residue and that the double alteration of residues 175 and 211 in a second-site revertant restores the proper geometry of the substrate binding site. J Biol. Chem. 264: 6288–6296.
Yang, X-J. and Miles, E. W. (1993) A novel intersubunit repair mechanism in the tryptophan synthase a.13, complex, -critical role of the 13—subunit lysine-167 in intersubunit communication. J Biol. Chem. 286: 22269–22272.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1994 Birkhäuser Verlag Basel/Switzerland
About this paper
Cite this paper
Dunn, M.F., Brzovic, P.S., Leja, C.A., Pan, P., Woehl, E.U. (1994). The Roles of Chemical Transformation, Loop Closure, Tunnel Function and Metal Ion Activation in the Tryptophan Synthase Mechanism. In: Marino, G., Sannia, G., Bossa, F. (eds) Biochemistry of Vitamin B6 and PQQ. Advances in Life Sciences. Birkhäuser Basel. https://doi.org/10.1007/978-3-0348-7393-2_19
Download citation
DOI: https://doi.org/10.1007/978-3-0348-7393-2_19
Publisher Name: Birkhäuser Basel
Print ISBN: 978-3-0348-7395-6
Online ISBN: 978-3-0348-7393-2
eBook Packages: Springer Book Archive