Purification and characterization of anthranilate synthase component I (TrpE) from Mycobacterium tuberculosis H37Rv

Protein Expression and Purification

Volumn 64, Issue 1, 2009, Pages 8-15

  Lin, Xiaohua ^a   Xu, Shengfeng ^a   Yang, Yanping ^a   Wu, Junchen ^a   Wang, Hongjun ^a   Shen, Hongbo ^a   Wang, Honghai ^a  

^a FUDAN UNIVERSITY   (China)

Author keywords

Anthranilate synthase component I; Mycobacterium tuberculosis H37Rv; Protein expression; Rv1609; Tuberculosis

Indexed keywords

ANTHRANILATE SYNTHASE; ANTIINFECTIVE AGENT; RECOMBINANT PROTEIN; TUBERCULOSTATIC AGENT;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL GENE; CHEMICAL STRUCTURE; CHEMISTRY; DRUG DESIGN; DRUG EFFECT; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR GENETICS; MOLECULAR WEIGHT; MULTIDRUG RESISTANCE; MULTIDRUG RESISTANT TUBERCULOSIS; MYCOBACTERIUM TUBERCULOSIS; NUCLEOTIDE SEQUENCE; PROTEIN CONFORMATION; PROTEIN MOTIF; PROTEIN SECONDARY STRUCTURE; SEQUENCE HOMOLOGY; TUBERCULOSIS;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANTHRANILATE SYNTHASE; ANTI-BACTERIAL AGENTS; ANTITUBERCULAR AGENTS; CONSERVED SEQUENCE; DRUG DESIGN; DRUG RESISTANCE, MULTIPLE, BACTERIAL; ESCHERICHIA COLI; GENES, BACTERIAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; MYCOBACTERIUM TUBERCULOSIS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; TUBERCULOSIS; TUBERCULOSIS, MULTIDRUG-RESISTANT;

ESCHERICHIA COLI; MAMMALIA; MYCOBACTERIUM TUBERCULOSIS;

EID: 57649112190     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2008.09.020     Document Type: Article

References (31)

1. World Health Organization, Tuberculosis fact sheet no. 104, World Health Organization, Geneva. Available from: .
2. Corbett E.L., Watt C.J., Walker N., Maher D., Williams B.G., Raviglione M.C., and Dye C. The growing burden of tuberculosis: global trends and interactions with the HIV epidemic. Arch. Intern. Med. 163 (2003) 1009-1021
3. World Health Organization, Anti-tuberculosis drug resistance in the world: The Global Report (2004).
4. Parish T., and Stoker N.G. The common aromatic amino acid biosynthesis pathway is essential in Mycobacterium tuberculosis. Microbiology 148 (2002) 3069-3077
5. Sassetti C.M., Boyd D.H., and Rubin E.J. Genes required for mycobacterial growth defined by high density mutagenesis. Mol. Microbiol. 48 (2003) 77-84
6. Xie G., Keyhani N.O., Bonner C.A., and Jensen R.A. Ancient origin of the tryptophan operon and the dynamics of evolutionary change. Microbiol. Mol. Biol. R. 67 (2003) 303-342
7. Morollo A.A., and Eck M.J. Structure of the cooperative allosteric anthranilate synthase from Salmonella typhimurium. Nat. Struct. Biol. 8 (2001) 243-247
8. Spraggon G., Kim C., Nguyen-Huu X., Yee M.-C., Yanofsky C., and Mills S.E. The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan. PNAS 98 (2001) 6021-6026
9. Knochel T., Ivens A., Hester G., Gonzalez A., Bauerle R., Wilmanns M., Kirschner K., and Jansnius J.N. The crystal structure of anthranilate synthase from Sulfolobus solfataricus: Functional implications(X-ray structure analysisy/glutamine amidotransferasey/tryptophan biosynthesis). Proc. Natl. Acad. Sci. USA 96 (1999) 9479-9484
10. Bauerle R., Hess J., and French S. Anthranilate synthase-anthranilate phosphoribosyltransferase complex and subunits of Salmonella typhimurium. Methods Enzymol. 142 (1987) 366-386
11. Zalkin H., and Kling D. Anthranilate synthetase: purification and properties of component I from Salmonella typhimurium. Biochemistry 7 (1968) 3566-3573
12. Ito J., Cox E.C., and Yanofsky C. Anthranilate synthetase, an enzyme specified by the tryptophan operon of Escherichia coli: purification and characterization of component I. J. Bacteriol. 97 (1969) 725-733
13. Hankins C.N., and Mills S.E. Anthranilate synthase-amidotransferase (combined). A novel from of antrhanilate synthase from Euglena gracilis. J. Biol. Chem. 251 (1976) 7774-7778
14. Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C., Harris D., Gordon S.V., Eiglmeier K., Gas S., Barry Jr. C.E., Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R., Devlin K., Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., and Barrell B.G. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393 (1998) 537-544
15. Braford M.M., McRorie R.A., and Williams W.L. 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
16. Baker T.I., and Crawford I.P. Anthranilate synthetase: partical purification and some kinetic studies on the enzyme from Escherichia Ecoli. J. Biol. Chem. 241 (1966) 5577-5584
17. Egan A.F., and Gibson F. Anthiranilate synthase/anthranilate 5-phosphoribosyl 1-pyrophosphate phosphoribosyltransferase from Aerobacter aerogenes. Biochem. J. 130 (1972) 847-859
18. Gison F. Chorismic acid: purification and some chemical and physical studies. Biochem. J. 90 (1964) 256-261
19. Tang X.-F., Ezaki S., Atomi H., and Imanaka T. Anthranilate synthase without an LLES motif from a Hyperthermophilic Archaeon is inhibited by tryptophan Biochem. Biophys. Res. Co. 281 (2001) 858-865
20. Yang J.T., Wu C.S., and Martinez H.M. Calculation of protein conformation from circular dichroism. Methods Enzymol. 130 (1986) 208-269
21. Higgins D., Thompson J., Gibson T., Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
22. Villaverde A., and Carrio M.M. Protein aggregation in recombinant bacteria: biological role of inclusion bodies. Biotechnol. Lett. 25 (2003) 1358-1395
23. Loughran S.T., Loughran N.B., Ryan B.J., D'Souza B.N., and Walls D. Modified His-tag fusion vector for enhanced protein purification by immobilized metal affinity chromatography. Anal. Biochem. 355 (2006) 148-150
24. Arnau J., Lauritzen C., Petersen G.E., and Pedersen J. Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins. Protein Expres. Purif. 48 (2006) 1-13
25. Patel M.P., and Blanchard J.S. Mycobacterium tuberculosis mycothione reductase: pH dependence of the kinetic parameters and kinetic isotope effects. Biochemistry 40 (2001) 5119-5126
26. Zheng R., and Blanchard J.S. Kinetic and mechanistic analysis of the E. coli panE-encoded ketopantoate reductase. Biochemistry 39 (2000) 3708-3717
27. Graf R., Mehmann B., and Braus G.H. Analysis of feedback-resistant anthranilate synthases from Saccharomyces cerevisiae. J. Bacteriol. 175 (1993) 1061-1068
28. Caligiuri M.G., and Bauerle R. Identification of amino acid residues involved in feedback regulation of the anthranilate synthase complex from Salmonella typhimurium. Evidence for an amino-terminal regulatory site. J. Biol. Chem. 266 (1991) 8328-8335
29. Tutino M.L., Tosco A., Marino G., and Sannia G. Expression of Sulfolobus solfataricus trpE and trpG genes in E. coli. Biochem. Biophys. Res. Commun. 230 (1997) 306-310
30. Caligiuri M.G., and Bauerle R. Subunit communication in the anthranilate synthase complex from Salmonella typhimurium. Science 252 (1991) 1845-1848
31. Bohlmann J., DeLuca V., Eilert U., and Martin W. Purification and cDNA cloning of anthranilate synthase from Ruta graveolens: modes of expression and properties of native and recombinant enzymes. Plant J. 7 (1995) 491-501