Active site residues in Mycobacterium tuberculosis pantothenate synthetase required in the formation and stabilization of the adenylate intermediate

Biochemistry

Volumn 43, Issue 22, 2004, Pages 7171-7178

  Zheng, Renjian ^a   Dam, Tarum K ^a   Brewer, C Fred ^a   Blanchard, John S ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALKYLATION; BIOCHEMISTRY; CALORIMETRY; CATALYSIS; ENZYMES; STRUCTURE (COMPOSITION);

MICROCALORIMETRY; MYOBACTERIUM TUBERCULOSIS;

BACTERIA;

ACYL CARRIER PROTEIN; BACTERIAL ENZYME; COENZYME A; PANTOTHENATE SYNTHETASE; PANTOTHENIC ACID; SYNTHETASE; UNCLASSIFIED DRUG;

ARTICLE; ENZYME ACTIVE SITE; ENZYME ASSAY; ENZYME KINETICS; GENE; GENE EXPRESSION; GENE MUTATION; MICHAELIS CONSTANT; MICROCALORIMETRY; MOLECULAR CLONING; MYCOBACTERIUM; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PANC GENE; PRIORITY JOURNAL; SPECTROPHOTOMETRY; THERMODYNAMICS;

ADENOSINE MONOPHOSPHATE; AMINO ACIDS; BINDING SITES; CONSERVED SEQUENCE; MYCOBACTERIUM TUBERCULOSIS; PANTOTHENIC ACID; PEPTIDE SYNTHASES;

BACTERIA (MICROORGANISMS); MYCOBACTERIUM; MYCOBACTERIUM TUBERCULOSIS;

EID: 2642541703     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049676n     Document Type: Article

References (31)

1. Neidhardt, F. (1996) Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, 2nd ed., pp 687-694, American Society for Microbiology, Washington, DC.
2. Abiko, Y. (1975) Metabolism of coenzyme A, In Metabolic Pathways (Greenburg, D. M., Ed.), pp 1-25, Academic Press, Inc., New York.
3. Dreier, J., Shah, A. N., and Khosla, C. (1999) Kinetic analysis of the actinorhodin aromatic polyketide synthase, J. Biol. Chem. 274, 25108-25112.
4. Lambalot, R. H., Gehring, A. M., Flugel, R. S., Zuber, P., LaCelle, M., Marahiel, M. A., Reid, R., Khosla, C., and Walsh, C. T. (1996) A new enzyme superfamily-the phosphopantetheinyl transferases, Chem. Biol. 3, 923-936.
5. Maas, W. K., and Vogel, H. J. (1953) α-Ketoisovaleric acid, a precursor of pantothenic acid in Escherichia coli, J. Bacteriol. 65, 388-393.
6. Brown, G. M., and Williamson, J. M. (1982) Biosynthesis of riboflavin, folic acid, thiamine, and pantothenic acid, Adv. Enzymol. 53, 345-381.
7. Cronan, J. E., Jr., Littel, K. J., and Jackowski, S. (1982) Genetic and biochemical analyses of pantothenate biosynthesis in Escherichia coli and Salmonella typhimurium, J. Bacteriol. 149, 916-922.
8. Brown, G. M., and Williamson, J. M. (1987) In Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology (Neidhardt, F., Ingraham, J. L., Low, K. B., Magasanik, B., Schaechter, M., and Umbarger, H. E., Eds.) pp 521-538, American Society for Microbiology, Washington, DC.
9. Sambandamurthy, V. K., Wang, X., Chen, B., Russell, R. G., Rerick, S., Collins, F. M., Morris, S. L., and Jacobs, W. R. (2002) A pantothenate auxotroph of Mycobacterium tuberculosis is highly attenuated and protects mice against tuberculosis. Nat. Med. 8, 1171-1174.
10. Miyatake, K., Nakano, Y., and Kitaoka, S. (1979) Pantothenate synthetase from Escherichia coli [D-pantoate: β-alanine ligase (AMP-forming), EC 6.3.2.1], Methods Enzymol. 62, 215-219.
11. Zheng, R., and Blanchard, J. S. (2001) Steady-state and pre-steady-state kinetic analysis of Mycobacterium tuberculosis pantothenate synthetase, Biochemistry 40, 12904-12912.
12. Miyatake, K., Nakano, Y., and Kitaoka, S. (1978) Enzymological properties of pantothenate synthetase from Escherichia coli B, J. Nutr. Sci. Vitaminol. 24, 243-253.
13. Genschel, U., Powell, C. A., Abell, C., and Smith, A. G. (1999) The final step of pantothenate biosynthesis in higher plants: cloning and characterization of pantothenate synthetase from Lotus japonicus and Oryza sativum (rice), Biochem. J. 341, 669-678.
14. von Delft, F., Lewendon, A., Dhanaraj, V., Blundell, T. L., Abell, C., and Smith, A. G. (2001) The crystal structure of E. coli pantothenate synthetase confirms it as a member of the cytidylyl-transferase superfamily, Structure 9, 439-450.
15. Wang, S., and Eisenberg, D. (2003) Crystal structures of a pantothenate synthetase from M. tuberculosis and its complexes with substrates and a reaction intermediate, Protein Sci. 12, 1097-1108.
16. Williams, L., Zheng, R., Blanchard, J. S., and Raushel, F. M. (2003) Positional isotope exchange analysis of the pantothenate synthetase reaction, Biochemistry 42, 5108-5113.
17. Kim, Y. S., and Kang, S. W. (1994) Steady-state kinetics of malonyl-CoA synthetase from Bradyrhizobium japonicum and evidence for malonyl-AMP formation in the reaction, Biochem. J. 297, 327-333.
18. Kisselev, L. L., and Favorova, O. O. (1974) Aminoacyl-tRNA synthetases: sone recent results and achievements, Adv. Enzymol. 40, 141-238.
19. King, H. L., Jr., Dyar, R. E., and Wilken, D. R. (1974) Ketopantoyl lactone and ketopantoic acid reductases. Characterization of the reactions and purification of two forms of ketopantoyl lactone reductase, J. Biol. Chem. 249, 4689-4695.
20. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
21. Piotrowski, J., Beal, R., Hoffman, L., Wilkinson, K. D., Cohen, R. E., and Pickart, C. M. (1997) Inhibition of the 26S proteasome by polyubiquitin chains synthesized to have defined lengths, J. Biol. Chem. 272, 23712-23721.
22. Cleland, W. W. (1979) Statistical analysis of enzyme kinetic data, Methods Enzymol. 63, 103-138.
23. Johnson, K. A. (1992) Transient-State Kinetic Analysis of Enzyme Reaction Pathways, in The Enzymes, 3rd ed., (Sigman, D. S., Ed.) Vol. 20, pp 1-60, Academic Press: New York.
24. An, J. H., Lee, G. Y., Jung, J. W., Lee, W., and Kim, Y. S. (1999) Identification of residues essential for a two-step reaction by malonyl-CoA synthetase from Rhizobium trifolii, Biochem. J. 344, 159-166.
25. Pfleiderer, G., Kreiling, A., and Wieland, T. (1960) On pantothenic acid synthetase from E. coli. I. Concentration with the aid of an optical test, Biochem. Z. 333, 302-307.
26. Leatherbarrow, R. J., and Fersht, A. R. (1987) Investigation of transition-state stabilization by residues histidine-45 and threonine-40 in the tyrosyl-tRNA synthetase, Biochemistry 26, 8524-8528.
27. Kim, I. Y., Veres, Z., and Stadtman, T. C. (1993) Biochemical analysis of Escherichia coli selenophosphate synthetase mutants. Lysine 20 is essential for catalytic activity and cysteine 17/19 for 8-azido-ATP derivatization, J. Biol. Chem. 268, 27020-27025.
28. Saraste, M., Sibbald, P. R., and Wittinghofer, A. (1990) The P-loop-a common motif in ATP- and GTP-binding proteins, Trends Biochem. Sci. 15, 430-434.
29. Chang, K., Xiang, H., and Dunaway-Mariano, D. (1997) Acyl-adenylate motif of the acyl-adenylate/thioester-forming enzyme superfamily: A site-directed mutagenesis study with the Pseudomonas p. strain CBS3 4-chlorobenzoate: Coenzyme A ligase, Biochemistry 36, 15650-15659.
30. Hawkes, R., Grutter, M. G., and Schellman, J. (1984) Thermodynamic stability and point mutations of bacteriophage T4 lysozyme, J. Mol. Biol. 175, 195-212.
31. Shortle, D., Meeker, A. K., and Freire, E. (1988) Stability mutants of staphylococcal nuclease: large compensating enthalpy-entropy changes for the reversible denaturation reaction, Biochemistry 27, 4761-4768.