The molecular basis of substrate channeling

Journal of Biological Chemistry

Volumn 274, Issue 18, 1999, Pages 12193-12196

  Miles, Edith Wilson ^a,b   Rhee, Sangkee ^b   Davies, David R ^b  

^a Department of Dermatopathology   (United States)

^b NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME ACTIVE SITE; ENZYME SUBSTRATE COMPLEX; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; SALMONELLA TYPHIMURIUM; SHORT SURVEY;

AMIDOPHOSPHORIBOSYLTRANSFERASE; CARBAMOYL-PHOSPHATE SYNTHASE (GLUTAMINE-HYDROLYZING); ELECTROSTATICS; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY; TETRAHYDROFOLATE DEHYDROGENASE; THYMIDYLATE SYNTHASE; TRYPTOPHAN SYNTHASE;

SALMONELLA TYPHIMURIUM; TYPHIMURIUM;

EID: 0033617187     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.18.12193     Document Type: Short Survey

References (50)

1. Srere, P. A. (1987) Complexes of sequential metabolic enzymes. Annu. Rev. Biochem. 56, 89-124
2. Ovadi, J. (1991) Physiological significance of metabolite channeling. J. Theor. Biol. 152, 1-22
3. Davis, B. D. (1958) On the importance of being ionized. Arch. Biochem. Biophys. 78, 497-509
4. Manney, T. R. (1970) Physiological advantage of the mechanism of the tryptophan synthetase reaction. J. Bacteriol. 102, 483-488
5. Knowles, J. R. (1991) Calmer waters in the channel. J. Theor. Biol. 152, 53-56
6. Ovadi, J. (1991) Physiological significance of metabolite channeling: author's response to commentaries. J. Theor. Biol. 162, 135-141
7. 2 multienzyme complex from Salmonella typhimurium. J. Biol. Chem. 263, 17857-17871
8. Thoden, J. B., Holden, H. M., Wesenberg, G., Raushel, F. M., and Rayment, I. (1997) Structure of carbamoyl phosphate synthetase: a journey of 96 Å from substrate to product. Biochemistry 36, 6305-6316
9. Krahn, J. M., Kim, J. H., Burns, M. R., Parry, R. J., Zalkin, H., and Smith, J. L. (1997) Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site. Biochemistry 36, 11061-11068
10. Knighton, D. R., Kan, C. C., Howland, E., Janson, C. A., Hostomska, Z., Welsh, K. M., and Matthews, D. A. (1994) Structure of and kinetic channeling in bifunctional dihydrofolate reductase-thymidylate synthase. Nat. Struct. Biol. 1, 186-194
11. Stroud, R. M. (1994) An electrostatic highway. Nat. Struct. Biol. 1, 131-134
12. 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. 268, 8020-8033
13. Kim, J. H., Krahn, J. M., Tomchick, D. R., Smith, J. L., and Zalkin, H. (1996) Structure and function of the glutamine phosphoribosylpyrophosphate amidotransferase glutamine site and communication with the phosphoribosylpyrophosphate site. J. Biol. Chem. 271, 15549-15557
14. Pan, P., Woehl, E., and Dunn, M. F. (1997) Protein architecture, dynamics and allostery in tryptophan synthase channeling. Trends Biochem. Sci. 22, 22-27
15. Liang, P. H., and Anderson, K. S. (1998) Substrate channeling and domain-domain interactions in bifunctional thymidylate synthase-dihydrofolate reductase. Biochemistry 37, 12195-12205
16. Miles, B. W., Banzon, J. A., and Raushel, F. M. (1998) Regulatory control of the amidotransferase domain of carbamoyl phosphate synthetase. Biochemistry 37, 16773-16779
17. Yanofsky, C., and Crawford, I. P. (1972) in The Enzymes (Boyer, P. D., ed) Vol. 7, pp. 1-31, Academic Press, New York
18. Miles, E. W. (1991) Structural basis for catalysis by tryptophan synthase. Adv. Enzymol. Relat. Areas Mol. Biol. 64, 93-172
19. Miles, E. W. (1995) Tryptophan synthase: structure, function, and protein engineering. In Subcellular Biochemistry, Proteins: Structure, Function, and Protein Engineering (Biswas, B. B., and Roy, S., eds) Vol. 24, pp. 207-254, Plenum Press, New York
20. Yanofsky, C., and Rachmeler, M. (1958) The exclusion of free indole as an intermediate in the biosynthesis of tryptophan in Neurospora crassa. Biochim. Biophys. Acta 28, 641-642
21. DeMoss, J. A. (1962) Studies on the mechanism of the tryptophan synthetase reaction. Biochim. Biophys. Acta 62, 279-293
22. Creighton, T. E. (1970) A steady-state kinetic investigation of the reaction mechanism of the tryptophan synthetase of Escherichia coli. Eur. J. Biochem. 13, 1-10
23. Matchett, W. H. (1974) Indole channeling by tryptophan synthase of Neurospora. J. Biol. Chem. 249, 4041-4049
24. 22 complex. Biochemistry 35, 4211-4221
25. 2 complex with ligands bound to the active sites of the α and β subunits reveal ligand-induced conformational changes. Biochemistry 36, 7664-7680
26. 2 complex reveals the correct orientation of active site αGlu49. J. Biol. Chem. 273, 8553-8555
27. Rhee, S., Miles, E. W., Mozzarelli, A., and Davies, D. R. (1998) Cryo-crystallography and microspectrophotometry of a mutant (αD60N) tryptophan synthase azß2 complex reveals allosteric roles of αAsp-60. Biochemistry 37, 10653-10659
28. Schneider, T. R., Gerhardt, E., Lee, M., Liang, P.-H., Anderson, K. S., and Schlichting, I. (1998) Loop closure and intersubunit communication in tryptophan synthase. Biochemistry 37, 5394-5406
29. Dunn, M. F., Aguilar, V., Brzovic', P. S., Drewe, W. F. J., Houben, K. F., Leja, C. A., and Roy, M. (1990) The tryptophan synthase bienzyme complex transfers indole between the α- and β-sites via a 25-30 Å long tunnel. Biochemistry 29, 8598-8607
30. Lane, A. N., and Kirschner, K. (1991) Mechanism of the physiological reaction catalyzed by tryptophan synthase from Escherichia coli. Biochemistry 30, 479-484
31. Anderson, K. S., Kim, A. Y., Quillen, J. M., Sayers, E., Yang, X.-J., and Miles, E. W. (1995) Kinetic characterization of channel impaired mutants of tryptophan synthase. J. Biol. Chem. 270, 29936-29944
32. Brzovic', P. S., Ngo, K., and Dunn, M. F. (1992) Allosteric interactions coordinate catalytic activity between successive metabolic enzymes in the tryptophan synthase bienzyme complex. Biochemistry 31, 3831-3839
33. 2 complex: kinetic studies with a mutant enzyme (βK87T) provide evidence for allosteric activation by an aminoacrylate intermediate. Biochemistry 34, 12704-12711
34. Zalkin, H., and Smith, J. L. (1998) Enzymes utilizing glutamine as an amide donor. Adv. Enzymol. Relat. Areas Mol. Biol. 72, 87-144
35. Raushel, F. M., Thoden, J. B., Reinhart, G. D., and Holden, H. M. (1998) Carbamoyl phosphate synthetase: a crooked path from substrates to products. Curr. Opin. Chem. Biol. 2, 624-632
36. Holden, H. M., Thoden, J. B., and Raushel, F. M. (1998) Carbamoyl phosphate synthetase: a tunnel runs through it. Curr. Opin. Struct. Biol. 8, 679-685
37. Anderson, P. M., and Meister, A. (1966) Bicarbonate-dependent cleavage of adenosine triphosphate and other reactions catalyzed by Escherichia coli carbamyl phosphate synthetase. Biochemistry 5, 3157-3163
38. Raushel, F. M., Mullins, L. S., and Gibson, G. E. (1998) A stringent test for the nucleotide switch mechanism of carbamoyl phosphate synthetase. Biochemistry 37, 10272-10278
39. Messenger, L. J., and Zalkin, H. (1979) Glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli. Purification and properties. J. Biol. Chem. 254, 3382-3392
40. Muchmore, C. R., Krahn, J. M., Kim, J. H., Zalkin, H., and Smith, J. L. (1998) Crystal structure of glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli. Protein Sci. 7, 39-51
41. Elcock, A. H., Potter, M. J., Matthews, D. A., Knighton, D. R., and McCammon, J. A. (1996) Electrostatic channeling in the bifunctional enzyme dihydrofolate reductase-thymidylate synthase. J. Mol. Biol. 262, 370-374
42. Elcock, A. H., Huber, G. A., and McCammon, J. A. (1997) Electrostatic channeling of substrates between enzyme active sites: comparison of simulation and experiment. Biochemistry 36, 16049-16058
43. Meek, T. D., Garvey, E. P., and Santi, D. V. (1985) Purification and characterization of the bifunctional thymidylate synthetase-dihydrofolate reductase from methotrexate-resistant Leishmania tropica. Biochemistry 24, 678-686
44. Trujillo, M., Donald, R. G., Roos, D. S., Greene, P. J., and Santi, D. V. (1996) Heterologous expression and characterization of the bifunctional dihydrofolate reductase-thymidylate synthase enzyme of Toxoplasma gondii. Biochemistry 35, 6366-6374
45. Kisliuk, R. L., Gaumont, Y., and Baugh, C. M. (1974) Polyglutamyl derivatives of folate as substrates and inhibitors of thymidylate synthetase. J. Biol. Chem. 249, 4100-4103
46. Rudolph, J., and Stubbe, J. (1995) Investigation of the mechanism of phospho-ribosylamine transfer from glutamine phosphoribosylpyrophosphate amidotransferase to glycinamide ribonucleotide synthetase. Biochemistry 34, 2241-2250
47. Wang, W., Kappock, T. J., Stubbe, J., and Ealick, S. E. (1998) X-ray crystal structure of glycinamide ribonucleotide synthetase from Escherichia coli. Biochemistry 37, 15647-15662
48. Irvine, H. S., Shaw, S. M., Paton, A., and Carrey, E. A. (1997) A reciprocal allosteric mechanism for efficient transfer of labile intermediates between active sites in CAD, the mammalian pyrimidine-biosynthetic multienzyme polypeptide. Eur. J. Biochem. 247, 1063-1073
49. Penverne, B., Belkaid, M., and Herve, G. (1994) In situ behavior of the pyrim-idine pathway enzymes in Saccharomyces cerevisiae. 4. The channeling of carbamylphosphate to aspartate transcarbamylase and its partition in the pyrimidine and arginine pathways. Arch. Biochem. Biophys. 309, 85-93
50. Thoden, J. B., Raushel, F. M., Benning, M. M., Rayment, I., and Holden, H. M. (1999) The structure of carbamoyl phosphate synthetase determined to 2.1 Å resolution. Acta Crystallogr. Sec. D 55, 8-24