One-step purification and characterization of a fully active histidine-tagged Class II fructose-1,6-bisphosphate aldolase from Mycobacterium tuberculosis

Enzyme and Microbial Technology

Volumn 43, Issue 7, 2008, Pages 500-506

  Rukseree, Kamolchanok ^a,b   Thammarongtham, Chinae ^a   Palittapongarnpim, Prasit ^a,b  

^a NATIONAL SCIENCE AND TECHNOLOGY DEVELOPMENT AGENCY   (Thailand)

^b Mahidol University ^*  (Thailand)

Author keywords

Aldolase assay; Fructose 1,6 bisphosphate aldolase; Immobilized metal affinity chromatography; Mycobacterium tuberculosis

Indexed keywords

AFFINITY CHROMATOGRAPHY; CHROMATOGRAPHIC ANALYSIS; CHROMATOGRAPHY; ENZYMES; ESCHERICHIA COLI; FRUCTOSE; GENE ENCODING; METAL REFINING; PASSENGER CARS; PORT TERMINALS; PURIFICATION; WATER POLLUTION;

ALDOLASE; ALDOLASE ASSAY; BIOCHEMICAL PROPERTIES; BISPHOSPHATE; E. COLI; ENZYME OVERPRODUCTIONS; EXPRESSION SYSTEMS; GENE SETS; HIGH-THROUGHPUT SCREENINGS; IMMOBILIZED METAL AFFINITY CHROMATOGRAPHIES; IMMOBILIZED METAL AFFINITY CHROMATOGRAPHY; MYCOBACTERIUM TUBERCULOSIS; NATIVE ENZYMES; POTENTIAL DRUGS;

BACKPROPAGATION ALGORITHMS;

FRUCTOSE BISPHOSPHATE ALDOLASE;

ARTICLE; ENZYME KINETICS; ENZYME PURIFICATION; ENZYME STABILITY; FBA GENE; GENE; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PH; PROTEIN EXPRESSION;

MYCOBACTERIUM TUBERCULOSIS;

EID: 55949108361     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2008.08.009     Document Type: Article

References (31)

1. Aziz M.A., and Wright A. The World Health Organization/International Union against tuberculosis and lung disease global project on surveillance for anti-tuberculosis drug resistance: a model for other infectious diseases. Clin Infect Dis 41 Suppl 4 (2005) S258-S262
2. World Health Organization (WHO). Global tuberculosis control: surveillance, planning, financing. WHO report 2007. Geneva: World Health Organization (WHO/HTM/TB/2007.376); 2007.
3. O'Brien R.J., and Nunn P.P. The need for new drugs against tuberculosis. Obstacles, opportunities, and next steps. Am J Respir Crit Care Med 163 5 (2001) 1055-1058
4. Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C., Harris D., et al. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393 6685 (1998) 537-544
5. Mushegian A.R., and Koonin E.V. A minimal gene set for cellular life derived by comparison of complete bacterial genomes. Proc Natl Acad Sci USA 93 19 (1996) 10268-10273
6. Koonin E.V. How many genes can make a cell: the minimal-gene-set concept. Annu Rev Genomics Hum Genet 1 (2000) 99-116
7. Thammarongtham C., and Palittapongarnpim P. In silico searching for drug targets in Mycobacterium tuberculosis genome. The international conference on bioinformatics: north-south networking, 6-8 February 2002. Le Royal Meridien, Bangkok, Thailand (2002)
8. Rutter W.J. Evolution of aldolase. Fed Proc 23 (1964) 1248-1257
9. Blom N.S., Tetreault S., Coulombe R., and Sygusch J. Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase. Nat Struct Biol 3 10 (1996) 856-862
10. Blonski C., Gefflaut T., and Perie J. Effects of chirality and substituents at carbon 3 in dihydroxyacetone-phosphate analogues on their binding to rabbit muscle aldolase. Bioorg Med Chem 3 9 (1995) 1247-1253
11. Gefflaut T., Blonski C., Perie J., and Willson M. Class I aldolases: substrate specificity, mechanism, inhibitors and structural aspects. Prog Biophys Mol Biol 63 3 (1995) 301-340
12. Perham R.N. The fructose-1,6-bisphosphate aldolases: same reaction, different enzymes. Biochem Soc Trans 18 2 (1990) 185-187
13. Bock A., and Neidhardt F.C. Properties of a mutant of Escherichia coli with a temperature-sensitive fructose-1,6-diphosphate aldolase. J Bacteriol 92 2 (1966) 470-476
14. Bock A., and Neidhardt F.C. Isolation of a mutant of Escherichia coli with a temperature-sensitive fructose-1,6-diphosphate aldolase activity. J Bacteriol 92 2 (1966) 464-469
15. Liebke H.H., and Speyer J.F. A new gene in E. coli RNA synthesis. Mol Gen Genet 189 2 (1983) 314-320
16. Mitchell C., Morris P.W., Lum L., Spiegelman G., and Vary J.C. The amino acid sequence of a Bacillus subtilis phosphoprotein that matches an orfY-tsr coding sequence. Mol Microbiol 6 10 (1992) 1345-1349
17. Trach K., Chapman J.W., Piggot P., LeCoq D., and Hoch J.A. Complete sequence and transcriptional analysis of the spo0F region of the Bacillus subtilis chromosome. J Bacteriol 170 9 (1988) 4194-4208
18. Wehmeier U.F. Molecular cloning, nucleotide sequence and structural analysis of the Streptomyces galbus DSM40480 fda gene: the S. galbus fructose-1,6-bisphosphate aldolase is a member of the class II aldolases. FEMS Microbiol Lett 197 1 (2001) 53-58
19. Ramsaywak P.C., Labbe G., Siemann S., Dmitrienko G.I., and Guillemette J.G. Molecular cloning, expression, purification, and characterization of fructose 1,6-bisphosphate aldolase from Mycobacterium tuberculosis-a novel Class II A tetramer. Protein Expr Purif 37 1 (2004) 220-228
20. van Soolingen D., de Haas P.E., Hermans P.W., and van Embden J.D. DNA fingerprinting of Mycobacterium tuberculosis. Methods Enzymol 235 (1994) 196-205
21. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 (1976) 248-254
22. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 5259 (1970) 680-685
23. Blostein R., and Rutter W.J. Comparative studies of liver and muscle aldolase. II. Immunochemical and chromatographic differentiation. J Biol Chem 238 (1963) 3280-3285
24. Sibley J.A., and Lehninger A.L. Determination of aldolase in animal tissues. J Biol Chem 177 2 (1949) 859-872
25. Stribling D., and Perham R.N. Purification and characterization of two fructose diphosphate aldolases from Escherichia coli (Crookes' strain). Biochem J 131 4 (1973) 833-841
26. Bai N.J., Pai M.R., Murthy P.S., and Venkitasubramanian T.A. Fructose-bisphosphate aldolases from mycobacteria. Methods Enzymol 90PtE (1982) 241-250
27. Bai N.J., Pai M.R., Murthy P.S., and Venkitasubramanian T.A. Fructose-1,6-diphosphate aldolase of Mycobacterium tuberculosis H37Rv. Indian J Biochem Biophys 12 2 (1975) 181-183
28. Hongmanee P., Rukseree K., Buabut B., Somsri B., and Palittapongarnpim P. In vitro activities of cloxyquin (5-chloroquinolin-8-ol) against Mycobacterium tuberculosis. Antimicrob Agents Chemother 51 3 (2007) 105-106
29. Bai N.J., Pai M.R., Murthy P.S., and Venkitasubramanian T.A. Effect of oxygen tension on the aldolases of Mycobacterium tuberculosis H37Rv. FEBS Lett 45 1 (1974) 68-70
30. Sauve V., and Sygusch J. Molecular cloning, expression, purification, and characterization of fructose-1,6-bisphosphate aldolase from Thermus aquaticus. Protein Expr Purif 21 2 (2001) 293-302
31. Lowry O.H., Roberts N.R., Wu M.L., Hixon W.S., and Crawford E.J. The quantitative histochemistry of brain. II. Enzyme measurements. J Biol Chem 207 1 (1954) 19-37