Development of a continuous assay and steady-state characterization of Escherichia coli threonine synthase

Analytical Biochemistry

Volumn 423, Issue 1, 2012, Pages 78-85

  Morneau, Dominique J K ^a   Abouassaf, Edgar ^a   Skanes, Jennifer E ^a   Aitken, Susan M ^a  

^a CARLETON UNIVERSITY   (Canada)

Author keywords

Hydroxyisocaproate dehydrogenase; Pyridoxal 5 phosphate; Threonine and methionine biosynthesis; Threonine deaminase

Indexed keywords

BIOCHEMISTRY; ENZYMES; ESCHERICHIA COLI;

CONCOMITANT OXIDATION; ENZYME CONCENTRATIONS; HYDROXYISOCAPROATE DEHYDROGENASE; LACTOBACILLUS DELBRUECKII; METHIONINE BIOSYNTHESIS; NICOTINAMIDE ADENINE DINUCLEOTIDES; PURIFICATION PROTOCOL; THREONINE DEAMINASE;

AMINO ACIDS;

HYDROXYISOCAPROATE DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SYNTHETASE; THREONINE DEHYDRATASE; THREONINE SYNTHETASE; UNCLASSIFIED DRUG;

ARTICLE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME KINETICS; ENZYME PURIFICATION; ENZYME SUBSTRATE; ESCHERICHIA COLI; LACTOBACILLUS DELBRUECKII; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; SPECTROPHOTOMETRY;

ESCHERICHIA COLI; LACTOBACILLUS DELBRUECKII;

EID: 84857314428     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2012.01.004     Document Type: Article

References (45)

1. C. Ramos, I.L. Calderon, Biochemical evidence that the Saccharomyces cerevisiae THR4 gene encodes threonine synthetase, FEBS Lett. 351 (1994) 357-359.
2. M.T. Skarstedt, S.B. Greer, Threonine synthetase of Bacillus subtilis, J. Biol. Chem. 248 (1973) 1032-1044.
3. A.S. Covarrubias, M. Hogbom, T. Bergfors, P. Carroll, K. Mannerstedt, S. Oscarson, T. Parish, T.A. Jones, S.L. Mowbray, Structural, biochemical, and in vivo investigations of the threonine synthase from Mycobacterium tuberculosis, J. Mol. Biol. 381 (2008) 622-633.
4. J.M. Kingsbury, J.H. McCusker, Threonine biosynthetic genes are essential in Cryptococcus neoformans, Microbiology 154 (2008) 2767-2775.
5. T. Murakawa, Y. Machida, H. Hayashi, Product-assisted catalysis as the basis of the reaction specificity of threonine synthase, J. Biol. Chem. 286 (2011) 2774-2784.
6. G.N. Cohen, M-L. Hirsch, Threonine synthase, a system for synthesizing Lthreonine from L-homoserine, J. Bacteriol. 67 (1954) 182-190.
7. Y. Watanabe, K. Shimura, Biosynthesis of threonine from homoserine, J. Biochem. 42 (1955) 181-192.
8. E.H. Wormser, A.B. Pardee, Regulation of threonine biosynthesis in Escherichia coli, Arch. Biochem. Biophys. 78 (1958) 416-432.
9. M. Szczesiul, D.E. Wampler, Regulation of metabolic system in vitro: synthesis of threonine from aspartic acid, Biochemistry 15 (1976) 2236-2244.
10. G.K. Farrington, A. Kumar, S.L. Shames, J.I. Ewaskiewicz, D.E. Ash, F.C. Wedler, Threonine synthase of Escherichia coli: inhibition by classical and slow-binding analogues of homoserine phosphate, Arch. Biochem. Biophys. 307 (1993) 165-174. (Pubitemid 23333989)
11. B. Laber, K.-P. Gerbling, C. Harde, K.-H. Neff, H.-D. Nordhoff, E. Pohlenz, Mechanisms of interaction of Escherichia coli threonine synthase with substrates and inhibitors, Biochemistry 33 (1994) 3413-3423. (Pubitemid 24112656)
12. B. Laber, S.D. Lindell, H.-D. Pohlenz, Inactivation of Escherichia coli threonine synthase by DL-Z-2-amino-5-phosphono-3-pentoic acid, Arch. Microbiol. 161 (1994) 400-403. (Pubitemid 24167205)
13. C. Chassagnole, B. Rais, E. Quentin, D.A. Fell, J.-P. Mazat, An integrated study of threonine-pathway enzyme kinetics in Escherichia coli, Biochem. J. 356 (2001) 415-423. (Pubitemid 32532352)
14. B. Rais, C. Chassagnole, T. Letellier, D.A. Fell, J.-P. Mazat, Threonine synthesis from aspartate in Escherichia coli cell-free extracts: pathway dynamics, Biochem. J. 356 (2001) 425-432. (Pubitemid 32532353)
15. J.T. Madison, J.F. Thompson, Threonine synthetase from higher plants: stimulation by S-adenosylmethionine and inhibition by cysteine, Biochem. Biophys. Res. Commun. 71 (1976) 684-691.
16. A. Thoen, S.E. Rognes, H. Aarnes, Biosynthesis of threonine from homoserine in pea seedlings: II. Threonine synthase, Plant Sci. Lett. 13 (1978) 113-119.
17. J. Giovanelli, K. Veluthambi, G.A. Thompson, S.H. Mudd, A.H. Datko, Threonine synthase of Lemna paucicostata Hegelm.6746, Plant Physiol. 76 (1984) 285-292.
18. G. Curien, R. Dumas, S. Ravanel, R. Douce, Characterization of an Arabidopsis thaliana cDNA encoding and S-adenosylmethionine-sensitive threonine synthase: threonine synthase from higher plants, FEBS Lett. 390 (1996) 85-90. (Pubitemid 26233273)
19. G. Curien, D. Job, R. Douce, R. Dumas, Allosteric activation of Arabidopsis thaliana threonine synthase by S-adenosylmethionine, Biochemistry 37 (1998) 13212-13221. (Pubitemid 28449565)
20. B. Laber, W. Maurer, C. Hanke, S. Grafe, S. Ehlert, A. Messerschmidt, T. Clausen, Characterization of recombinant Arabidopsis thaliana threonine synthase, Eur. J. Biochem. 263 (1999) 212-221. (Pubitemid 29313857)
21. K. Thomazeau, G. Curien, R. Dumas, V. Biou, Crystal structure of threonine synthase from Arabidopsis thaliana, Protein Sci. 10 (2001) 638-648. (Pubitemid 32221152)
22. M. Flavin, C. Slaughter, Threonine synthetase mechanism: studies using isotopic hydrogen, J. Biol. Chem. 235 (1960) 1112-1118.
23. A.H. Datko, J. Giovanelli, S.H. Mudd, Homocysteine biosynthesis in green plants, J. Biol. Chem. 249 (1974) 1139-1155.
24. S. Ravanel, M. Droux, R. Douce, Methionine biosynthesis in higher plants: I. Purification and characterization of cystathionine γ-synthase from spinach chloroplasts, Arch. Biochem. Biophys. 316 (1995) 572-584.
25. G. Curien, S. Ravanel, R. Dumas, A kinetic model of the branch-point between the methionine and threonine biosynthetic pathways in Arabidopsis thaliana, Eur. J. Biochem. 270 (2003) 4615-4627. (Pubitemid 37487230)
26. M. Lee, M.N. Martin, A.O. Hudson, J. Lee, M.J. Muhitch, T. Leustek, Methionine and threonine synthesis are limited by homoserine kinase availability and not the activity of homoserine kinase in Arabidopsis thaliana, Plant J. 41 (2005) 685-696. (Pubitemid 40336000)
27. S.M. Aitken, D.H. Kim, J.F. Kirsch, Escherichia coli cystathionine γ-synthase does not obey ping-pong kinetics: novel continuous assays for the elimination and substitution reactions, Biochemistry 42 (2003) 11297-11306. (Pubitemid 37158897)
28. E. Eisenstein, Cloning, expression, purification, and characterization of biosynthetic threonine deaminase from Escherichia coli, J. Biol. Chem. 266 (1991) 5801-5807.
29. E. Eisenstein, H.D. Yu, K.E. Fisher, D.A. Iacuzio, K.R. Ducote, F.P. Schwarz, An expanded two-state model accounts for homotropic cooperativity in biosynthetic threonine deaminase from Escherichia coli, Biochemistry 34 (1995) 9403-9412.
30. A. Farsi, P.H. Lodha, J.E. Skanes, H. Los, N. Kalidindi, S.M. Aitken, Interconversion of a pair of active-site residues in Escherichia coli cystathionine γ-synthase, E. coli cystathionine β-lyase, and Saccharomyces cerevisiae cystathionine γ-lyase and development of tools for the investigation of their mechanisms and reaction specificity, Biochem. Cell Biol. 87 (2009) 445-457.
31. M.M. Bradford, A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72 (1976) 248-254.
32. P.A. Lanzetta, L.J. Alvarez, P.S. Reinach, O.A. Candia, An improved assay for nanomole amounts of inorganic phosphate, Anal. Biochem. 100 (1979) 95-97. (Pubitemid 10157636)
33. P.P. Van Veldhoven, G.P. Mannaerts, Inorganic and organic phosphate measurements in the nanomolar range, Anal. Biochem. 161 (1987) 45-48. (Pubitemid 17036687)
34. J. Theze, L. Kleidman, I. Saint Girons, Homoserine kinase from Escherichia coli K-12: properties, inhibition by L-threonine, and regulation of biosynthesis, J. Bacteriol. 118 (1974) 577-581.
35. A. Peracchi, S. Bettati, A. Mozzarelli, G.L. Rossi, E.W. Miles, M.F. Dunn, Allosteric regulation of tryptophan synthase: effects of pH, temperature, and α-subunit ligands on the equilibrium distribution of pyridoxal 5′-phosphate-L-homoserine intermediates, Biochemistry 35 (1996) 1872-1880.
36. S.L. Shames, F.C. Wedler, Homoserine kinase of Escherichia coli: Kinetic mechanism and inhibition by L-aspartate semialdehyde, Arch. Biochem. Biophys. 235 (1984) 359-370.
37. +-dependent d-2-hydroxyisocaproate dehydrogenase of Lactobacillus delbrueckii subsp. bulgaricus: gene cloning and enzyme characterization, Eur. J. Biochem. 224 (1994) 439-446.
38. S. Ravanel, B. Gakiere, D. Job, R. Douce, The specific features of methionine biosynthesis and metabolism in plants, Proc. Natl. Acad. Sci. 95 (1998) 7805-7812. (Pubitemid 28293335)
39. J. Schnyder, M. Rottenberg, Improved synthesis of O-phosphohomoserine, Helv. Chim. Acta 58 (1975) 518-521.
40. I. Schildkraut, S.B. Greer, Threonine synthetase-catalyzed conversion of phosphohomoserine to α-ketobutyrate in Bacillus subtilis, J. Bacteriol. 115 (1973) 777-785.
41. P. Laloi, D. Atlan, B. Blanc, C. Gilbert, R. Portalier, Cell-wall-associated proteinase of Lactobacillus delbrueckii subsp. bulgaricus CNRZ 397: differential extraction, purification, and properties of the enzyme, Appl. Microbiol. Biotechnol. 36 (1991) 196-204.
42. W. Bockelmann, H.P. Beuck, S. Lick, K. Heller, Purification and characterization of a new tripeptidase from Lactobacillus delbrueckii ssp. bulgaricus B14, Int. Dairy J. 5 (1995) 493-502.
43. A.A. Bourniquel, B. Mollet, Purification and characterization of the 3-phosphoglycerate kinase from the thermophile Lactobacillus delbrueckii subsp. lactis, Int. Dairy J. 12 (2002) 723-728.
44. B. Burr, J. Walker, P. Truffa-Bachi, G.N. Cohen, Homoserine kinase from Escherichia coli K12, Eur. J. Biochem. 62 (1976) 519-526.
45. C. Parsot, P. Cossart, I. Saint-Girons, G.N. Cohen, Nucleotide sequence of thrC and of the transcription termination region of the threonine operon in Escherichia coli K12, Nucleic Acids Res. 11 (1983) 7331-7345.