Residues C123 and D58 of the 2-methylisocitrate lyase (PrpB) enzyme of Salmonella enterica are essential for catalysis

Journal of Bacteriology

Volumn 185, Issue 16, 2003, Pages 4837-4843

  Grimek, T L ^a   Holden, H ^a   Rayment, I ^a   Escalante Semerena, J C ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

2 METHYLISOCITRATE LYASE; ALANINE; BACTERIAL ENZYME; DITHIOTHREITOL; GLUTATHIONE; ISOCITRATE LYASE; LYSINE; MAGNESIUM ION; MANGANESE; MUTANT PROTEIN; MUTASE; PHOSPHINE DERIVATIVE; PHOSPHOENOLPYRUVATE MUTASE; PROPIONIC ACID; PYRUVIC ACID; SUCCINIC ACID; TRIS(2 CARBOXYETHYL)PHOSPHINE; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL GENE; CATALYSIS; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; DISULFIDE BOND; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME ISOLATION; ENZYME SUBUNIT; GENETIC CODE; HUMAN; MOLECULAR WEIGHT; PRIORITY JOURNAL; PROTEIN DEGRADATION; SALMONELLA ENTERICA; SEROTYPE; SITE DIRECTED MUTAGENESIS; WILD TYPE;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; CARBON-CARBON LYASES; ISOCITRATES; KINETICS; MOLECULAR SEQUENCE DATA; MUTATION; SALMONELLA TYPHIMURIUM; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); NEGIBACTERIA; PROKARYOTA; SALMONELLA; SALMONELLA ENTERICA; SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR TYPHIMURIUM;

EID: 0041559746     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.16.4837-4843.2003     Document Type: Article

References (45)

1. Altschul, S. F., W. Gish, W. Miller, and E. W. Myers. 1990. Basic local alignment search tool. J. Mol. Biol. 215:403-410.
2. Altschul, S. F., T. L. Madden, A. A. Schaffer, J. Zhang, W. Miller, and D. J. Lipmann. 1997. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25:3389-3402.
3. Berkowitz, D., J. M. Hushon, H. J. Whitfield, J. Roth, and B. N. Ames. 1968. Procedure for identifying nonsense mutations. J. Bacteriol. 96:215-220.
4. Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-255.
5. Britton, K., S. Langridge, P. J. Baker, K. Weeradechapon, S. E. Sedelnikova, J. R. De Lucas, D. W. Rice, and G. Turner. 2000. The crystal structure and active site location of isocitrate lyase from the fungus Aspergillus nidulans. Struct. Fold Des. 8:349-362.
6. Britton, K. L., I. S. Abeysinghe, P. J. Baker, V. Barynin, P. Diehl, S. J. Langridge, B. A. McFadden, S. E. Sedelnikova, T. J. Stillman, K. Weeradechapon, and D. W. Rice. 2001. The structure and domain organization of Escherichia coli isocitrate lyase. Acta Crystallogr. D Biol. Crystallogr. 57:1209-1218.
7. Brock, M., D. Darley, S. Textor, and W. Buckel. 2001. 2-Methylisocitrate lyases from the bacterium Escherichia coli and the filamentous fungus Aspergillus nidulans characterization and comparison of both enzymes. Eur. J. Biochem. 268:3577-3586.
8. Brock, M., C. Maerker, A. Schutz, U. Volker, and W. Buckel. 2002. Oxidation of propionate to pyruvate in Escherichia coli. Involvement of methylcitrate dehydratase and aconitase. Eur. J. Biochem. 269:6184-6194.
9. Burns, J. A., J. C. Butler, J. Moran, and G. M. Whitesides. 1991. Selective reduction of disulfides by Tris(2-caboxyethyl)phosphine. J. Org. Chem. 56:2648-2650.
10. Dawson, R. M. C., D. C. Elliott, W. H. Elliott, and K. M. Jones. 1986. Data for biochemical research, 3rd ed. Oxford University Press, Oxford, United Kingdom.
11. Grimm, C., A. Evers, M. Brock, C. Maerker, G. Klehe, W. Buckel, and K. Reuter. 2003. Crystal structure of 2-methylisocitrate lyase (PrpB) from Escherichia coli and modelling of its ligand bound active centre. J. Mol. Biol. 328:609-621.
12. BAD promoter. J. Bacteriol. 177:4121-4130.
13. Hidaka, T., S. Imai, O. Hara, H. Anzai, T. Murakami, K. Nagaoka, and H. Seto. 1990. Carboxyphosphoenolpyruvate phosphomutase, a novel enzyme catalyzing C-P bond formation. J. Bacteriol. 172:3066-3072.
14. Horswill, A. R., and J. C. Escalante-Semerena. 2002. Characterization of the propionyl-CoA synthetase (PrpE) enzyme of Salmonella enterica: residue Lys592 is required for propionyl-AMP synthesis. Biochemistry 41:2379-2387.
15. Horswill, A. R., and J. C. Escalante-Semerena. 2001. In vitro conversion of propionate to pyruvate by Salmonella enterica enzymes: 2-methylcitrate dehydratase (PrpD) and aconitase enzymes catalyze the conversion of 2-methylcitrate to 2-methylisocitrate. Biochemistry 40:4703-4713.
16. Horswill, A. R., and J. C. Escalante-Semerena. 1997. Propionate catabolism in Salmonella typhimurium LT2: two divergently transcribed units comprise the prp locus at 8.5 centisomes, prpR encodes a member of the sigma-54 family of activators, and the prpBCDE genes constitute an operon. J. Bacteriol. 179:928-940.
17. Horswill, A. R., and J. C. Escalante-Semerena. 1999. The prpE gene of Salmonella typhimurium LT2 encodes propionyl-CoA synthetase. Microbiology 145:1381-1388.
18. Horswill, A. R., and J. C. Escalante-Semerena. 1999. Salmonella typhimurium LT2 catabolizes propionate via the 2-methylcitric acid cycle. J. Bacteriol. 181:5615-5623.
19. 2+-oxalate. Struct. Fold Des. 7:539-548.
20. Jia, Y., Z. Lu, K. Huang, O. Herzberg, and D. Dunaway-Mariano. 1999. Insight into the mechanism of phosphoenolpyruvate mutase catalysis derived from site-directed mutagenesis studies of active site residues. Biochemistry 38:14165-14173.
21. Ko, Y. H., and B. A. McFadden. 1990. Alkylation of isocitrate lyase from Escherichia coli by 3-bromopyruvate. Arch. Biochem. Biophys. 278:373-380.
22. Laemmli, U. K. 1970. Cleavage and structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
23. Liu, S., Z. Lu, Y. Jia, D. Dunaway-Mariano, and O. Herzberg. 2002. Dissociative phosphoryl transfer in PEP mutase catalysis: structure of the enzyme/ sulfopyruvate complex and kinetic properties of mutants. Biochemistry 41:10270-10276.
24. Luttik, M. A., P. Kotter, F. A. Salomons, I. J. van Der Klei, J. P. van Dijken, and J. T. Pronk. 2000. The Saccharomyces cerevisiae ICL2 gene encodes a mitochondrial 2-methylisocitrate lyase involved in propionyl-coenzyme A metabolism. J. Bacteriol. 182:7007-7113.
25. Michael, S. F. 1994. Mutagenesis by incorporation of a phosphorylated oligo during PCR amplification. BioTechniques 16:410-414.
26. Nimmo, H. G., F. Douglas, C. Kleanthous, D. G. Campbell, and C. Mackintosh. 1989. Identification of a cysteine residue at the active site of Escherichia coli isocitrate lyase. Biochem. J. 261:431-435.
27. Ogawa, Y., T. Tsuruoka, S. Inoue, and T. Niida. 1973. Studies on a new antibiotic SF-1293. II. Chemical structure of antibiotic SF-1293. Sci. Rep. Meijii Kaisha 13:42-48.
28. Rehman, A., and B. A. McFadden. 1997. Cysteine 195 has a critical functional role in catalysis by isocitrate lyase from Escherichia coli. Curr Microbiol. 35:267-269.
29. Ryu, J.-I., and R. J. Hartin. 1990. Quick transformation of Salmonella typhimurium LT2. BioTechniques 8:43-45.
30. Sasse, J. 1991. Detection of proteins, p. 10.6.1-10.6.8. In F. A. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.), Current protocols in molecular biology, vol. 1. Wiley Interscience, New York, N.Y.
31. Schloss, J. V., and W. W. Cleland. 1982. Inhibition of isocitrate lyase by 3-nitropropionate, a reaction intermediate analogue. Biochemistry 21:4420-4427.
32. Seidel, H. M., and J. R. Knowles. 1994. Interaction of inhibitors with phosphoenolpyruvate mutase: implications for the reaction mechanism and the nature of the active site. Biochemistry 33:5641-5646.
33. Seidman, C. G., K. Struhl, J. Sheen, and T. Jessen. 1997. Introduction of plasmid DNA into cells, p. 1.8.-1.8.10. In F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.), Current protocols in molecular biology, vol. 1. Wiley Interscience, New York, N.Y.
34. Sharma, V., S. Sharma, K. Hoener zu Bentrup, J. D. McKinney, D. G. Russell, W. R. Jacobs, Jr., and J. C. Sacchettini. 2000. Structure of isocitrate lyase, a persistence factor of Mycobacterium tuberculosis. Nat. Struct. Biol. 7:663-668.
35. Tabor, S. 1990. Expression using the T7 RNA polymerase/promoter system., p. 16.2.1.-16.2.11. In F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.), Current protocols in molecular biology, vol. 2. Wiley Interscience, New York, N.Y.
36. Tabuchi, T., and S. Hara. 1974. Production of 2-methylcitric acid from n-paraffins by mutants of Candida lipolytica. Agric. Biol. Chem. 38:1105-1106.
37. Tabuchi, T., and N. Serizawa. 1975. The production of 2-methylisocitric acid from odd-carbon n-alkanes by a mutant of Candida lipolytica. Agric. Biol. Chem. 39:1049-1054.
38. Tabuchi, T., H. Umetsu, H. Aoki, and H. Uchiyama. 1995. Characteristics of 2-methylisocitrate dehydratase, isolated from Yarrowia lipolytica, in comparison with aconitase. Biosci. Biotechnol. Biochem. 59:2013-2017.
39. Textor, S., V. F. Wendisch, A. A. De Graaf, U. Müller, M. I. Linder, D. Linder, and W. Buckel. 1997. Propionate oxidation in Escherichia coli: evidence for operation of a methylcitrate cycle in bacteria. Arch. Microbiol. 168:428-436.
40. Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acid Res. 22:4673-4680.
41. Tsai, S. P., R. J. Hartin, and J. Ryu. 1989. Transformation in restriction-deficient Salmonella typhimurium LT2. J. Gen. Microbiol. 135:2561-2567.
42. Tsang, A. W., A. R. Horswill, and J. C. Escalante-Semerena. 1998. Studies of regulation of expression of the propionate (prpBCDE) operon provide insights into how Salmonella typhimurium LT2 integrates its 1,2-propanediol and propionate catabolic pathways. J. Bacteriol. 180:6511-6518.
43. Vanni, P., E. Giachetti, G. Pinzauti, and B. A. McFadden. 1990. Comparative structure, function and regulation of isocitrate lyase, an important assimilatory enzyme. Comp. Biochem. Physiol. 95:431-458.
44. Way, J. C., M. A. Davis, D. Morisato, D. E. Roberts, and N. Kleckner. 1984. New Tn10 derivatives for transposon mutagenesis and for construction of lacZ operon fusions by transposition. Gene 32:369-379.
45. Winston, S. E., S. A. Fuller, and J. G. R. Hurrell. 1990. Western blotting, p. 10.8.1-10.8.6. In F. A. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.), Current protocols in molecular biology, vol. 1. Wiley Interscience, New York, N.Y.