Characterization of the putative tryptophan synthase β-subunit from Mycobacterium tuberculosis

Acta Biochimica et Biophysica Sinica

Volumn 41, Issue 5, 2009, Pages 379-388

  Shen, Hongbo ^a   Yang, Yanping ^a   Wang, Feifei ^a   Zhang, Ying ^b   Ye, Naihao ^c   Xu, Shengfeng ^a   Wang, Honghai ^a  

^a FUDAN UNIVERSITY   (China)

^b JOHNS HOPKINS BLOOMBERG SCHOOL OF PUBLIC HEALTH   (United States)

^c YELLOW SEA FISHERIES RESEARCH INSTITUTE   (China)

Author keywords

Active site; Enzyme activity; Mycobacterium tuberculosis; Site directed mutation; Tryptophan synthase

Indexed keywords

BACTERIAL PROTEIN; MAGNESIUM; PROTEIN SUBUNIT; PYRIDOXAL 5 PHOSPHATE; RECOMBINANT PROTEIN; SODIUM; TRYPTOPHAN SYNTHASE;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; DIMERIZATION; DRUG EFFECT; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; KINETICS; MASS SPECTROMETRY; METABOLISM; MOLECULAR GENETICS; MUTATION; MYCOBACTERIUM TUBERCULOSIS; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; TEMPERATURE;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; CATALYSIS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; DIMERIZATION; ENZYME STABILITY; ESCHERICHIA COLI; KINETICS; MAGNESIUM; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; MYCOBACTERIUM TUBERCULOSIS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; PYRIDOXAL PHOSPHATE; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SODIUM; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; SUBSTRATE SPECIFICITY; TEMPERATURE; TRYPTOPHAN SYNTHASE;

MYCOBACTERIUM TUBERCULOSIS;

EID: 66449084702     PISSN: 16729145     EISSN: 17457270     Source Type: Journal    
DOI: 10.1093/abbs/gmp017     Document Type: Article

References (32)

1. Anon. Global tuberculosis control. WHO report 2002. World Health Organization, Geneva, Switzerland, 2002: 181.
2. Dye C, Scheele S, Dolin P, Pathania V and Raviglione MC. Consensus statement. Global burden of tuberculosis: estimated incidence, prevalence, and mortality by country. WHO Global Surveillance and Monitoring Project. JAMA 1999, 282: 677-686. (Pubitemid 29384157)
3. Raviglione MC, Snider DE and Kochi A. Global epidemiology of tuberculosis. Morbidity and mortality of a worldwide epidemic. J AmMed Assoc 1995, 273: 220-226.
4. World Health Organization. Anti-tuberculosis drug resistance in the world. Third Global Report. 2004.
5. Smith DA, Parish T, Stoker NG and Bancroft GJ. Characterization of auxotrophic mutants of Mycobacterium tuberculosis and their potential as vaccine candidates. Infect Immun 2001, 69: 1142-1150. (Pubitemid 32109583)
6. Lee CE, Goodfellow C, Javid-Majd F, Baker EN and Lott JS. The crystal structure of TrpD, a metabolic enzyme essential for lung colonization by Mycobacterium tuberculosis, in complex with its substrate phosphoribosylpyrophosphate. J Mol Biol 2006, 355: 784-797. (Pubitemid 41817636)
7. Pouwels P and Van RJ. In vitro synthesis of enzymes of the tryptophan operon of Escherichia coli. Proc Natl Acad Sci USA 1972, 69: 1786-1790.
8. Yanofsky C. Using studies on tryptophan metabolism to answer basic biological questions. J Biol Chem 2003, 278: 10859-10878. (Pubitemid 36792631)
9. Truffa-Bachi P and Cohen G. Amino acid metabolism. Annu Rev Biochem 1973, 42: 113-134.
10. Aksoy S, Squires CL and Squires C. Translational coupling of the trpB and trpA genes in the Escherichia coli tryptophan operon. J Bacteriol 1984, 157: 363-367. (Pubitemid 14190405)
11. Amadasi A, Bertoldi M, Contestabile R, Bettati S, Cellini B, Salvo MLd and Borri-Voltattorni C, et al. Pyridoxal 5′-phosphate enzymes as targets for therapeutic agents. Curr Med Chem 2007, 14: 1291-1324. (Pubitemid 46746362)
12. Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D and Gordon SV, et al. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 1998, 393: 537-544. (Pubitemid 28319235)
13. Hurle M, Matthews C, Cohen F, Kuntz I, Toumadje A and Johnson WJ. Prediction of the tertiary structure of the a-subunit of tryptophan synthase. Proteins 1987, 2: 210-224. (Pubitemid 18105509)
14. Chang C, Wu C and Yang J. Circular dichroic analysis of protein conformation: inclusion of the beta-turns. Anal Biochem 1978, 91: 13-31. (Pubitemid 9066794)
15. Dettwiler M and Kirschner K. Tryptophan synthase from Saccharomyces cerevisiae is a dimer of two polypeptide chains of Mr 76000 each. Eur J Biochem 1979, 102: 159-165. (Pubitemid 10137587)
16. Marti-Renom MA, Stuart A, Fiser A, Sánchez R, Melo F and Sali A. Comparative protein structure modeling of genes and genomes. Annu Rev Biophys Biomol Struct 2000, 29: 291-325. (Pubitemid 30599596)
17. Miles E. Tryptophan synthetase : structure, function, and subunit interaction. Adv Enzymol 1979, 49: 127-186.
18. Miles E. The tryptophan synthase α2β2 complex. Cleavage of a flexible loop in the α subunit alters allosteric properties. J Biol Chem 1991, 266: 10715-10718. (Pubitemid 21906860)
19. Rhee S, Parris KD, Hyde CC, Ahmed SA, Miles EW and Davies DR. Crystal structures of a mutant (( K87T) tryptophan synthase 7alpha;2β2 complex with ligands bound to the active sites of the α- and β-subunits reveal ligand-induced conformational changes. Biochemistry 1997, 36: 7664-7680. (Pubitemid 27287176)
20. Hettwer S and Sterner R. A novel tryptophan synthase ( -subunit from the hyperthermophile Thermotoga maritime. J Biol Chem 2002, 277: 8194-8201.
21. Lu Z, Nagata S, McPhie P and Milese EW. Lysine 87 in the ( subunit of tryptophan synthase that forms an internal aldimine with pyridoxal phosphate serves critical roles in transimination, catalysis, and product release. J Biol Chem 1993, 268: 8727-8734. (Pubitemid 23118660)
22. Leopoldseder S, Hettwer S and Sterner R. Evolution of multi-enzyme complexes: the case of tryptophan synthase. Biochemistry 2006, 45: 14111-14119.
23. Hyde CC and Miles EW. The tryptophan synthase multienzyme complex: exploring structure-function relationships with X-ray crystallography and mutagenesis. Nat Biotech 1990, 8: 27-32. (Pubitemid 20028196)
24. KayasthaS AM, Sawaj Y, Nagatan S and Miles EW. Site-directed muta-genesis of the (subunit of tryptophan synthase from Salmonella typhi-murium, role of active site Glutamic acid 350. J Biol Chem 1991, 266: 7618-7625. (Pubitemid 21906410)
25. Stoll SW, Kansra S and Elder JT. Metalloproteinases stimulate ErbB-dependent ERK signaling in human skin organ culture. J Biol Chem 2002, 277: 26839-26845.
26. Caldwell H, Wood H, Crane D, Bailey R, Jones R, Mabey D and Maclean I, et al. Polymorphisms in Chlamydia trachomatis tryptophan synthase genes differentiate between genital and ocular isolates. J Clin Invest 2003, 111: 1757-1769. (Pubitemid 38057756)
27. Shen H, Wang F, Zhang Y, Huang Q, Xu S, Hu H and Yue J, et al. A novel inhibitor of indole-3-glycerol phosphate synthase with activity against multidrug-resistant Mycobacterium tuberculosis. FEBS J 2009, 276: 144-154.
28. Woehl E and Dunn MF. Mechanisms of monovalent cation action in enzyme catalysis: the tryptophan synthase α-, β-, and αβ- reactions. Biochemistry 1999, 38: 7131-7141. (Pubitemid 129515014)
29. Hyde CC, Ahmed SA, Padlan EA, Miles EW and Davies DR. Three-dimensional structure of the tryptophan synthase a2( 2 multien- zyme complex from Salmonella typhimurium. J Biol Chem 1988, 263: 17857-17871.
30. Banik U, Ahmed SA, McPhie P and Miles EW. Subunit assembly in the tryptophan synthase a2( 2 complex, stabilization by pyridoxal phosphate aldimine intermediates. J Biol Chem 1995, 270: 7944-7949.
31. Marabotti A, De Biase D, Tramonti A, Bettati S and Mozzarelli A. Allosteric communication of tryptophan synthase. Functional and regulatory properties of the βS178P mutant. J Biol Chem 2001, 276:17747-17753. (Pubitemid 37411329)
32. Peracchi A, Bettati S, Mozzarelli A, Rossi GL, Miles EW and Dunn MF. Allosteric regulation of tryptophan synthase: effects of pH, temperature, and a-subunit ligands on the equilibrium distribution of pyridoxal 5′-phosphate-L-serine intermediates. Biochemistry 1996, 35: 1872-1880. (Pubitemid 26062637)