Expression and functional characterization of prephenate dehydrogenase from Streptococcus mutans

Process Biochemistry

Volumn 45, Issue 4, 2010, Pages 607-612

  Ku, Hyung Keun ^a,b   Park, Sang Ryoul ^a,b   Yang, Inchul ^a,b   Kim, Sook Kyung ^a,b  

^a Korea Research Institute of Standards and Science   (South Korea)

^b University of Science and Technology (UST)   (South Korea)

Author keywords

MALDI TOF; Prephenate dehydrogenase; Site directed mutagenesis; Size exclusion chromatography; Streptococcus mutans; Tyrosine

Indexed keywords

CONSERVED RESIDUES; EFFECTS OF TEMPERATURE; EXPRESSION VECTORS; FUNCTIONAL CHARACTERIZATION; INHIBITORY EFFECT; ION CONCENTRATIONS; L-TYROSINE; MALDI-TOF; NICKEL COLUMN; ORAL CAVITY; PREPHENATE DEHYDROGENASE; PURIFIED ENZYME; REACTION CATALYZED; S. MUTANS; SITE DIRECTED MUTAGENESIS; SITE-DIRECTED MUTATION; STREPTOCOCCUS MUTANS;

AMINO ACIDS; CHROMATOGRAPHIC ANALYSIS; ENZYME ACTIVITY; ENZYMES; ESCHERICHIA COLI; GEL PERMEATION CHROMATOGRAPHY; GENE EXPRESSION; MUTAGENESIS; ORGANIC ACIDS; PH EFFECTS; PHOSPHATASES; PURIFICATION;

SIZE EXCLUSION CHROMATOGRAPHY;

ESCHERICHIA COLI; STREPTOCOCCUS MUTANS;

EID: 77649182177     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2009.12.006     Document Type: Article

References (30)

1. Loesche W.J. Role of Streptococcus mutans in human dental decay. Microbiol Rev 50 (1986) 353-380
2. Hanada N., and Kuramitsu H.K. Isolation and characterization of the gtfD gene, coding for primer-dependent soluble glucan synthesis. Infect Immun 57 (1989) 2079-2085
3. Okahashi N., Sasakawa C., Yoshikawa M., Hamada S., and Koga T. Molecular characterization of a surface protein antigen gene from serotype c Streptococcus mutans, implicated in dental caries. Mol Microbiol 3 (1989) 673-678
4. Marsh P.D. Dental plaque as a microbial biofilm. Caries Res 38 (2004) 204-211
5. Ajdic D., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., et al. Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen. Proc Natl Acad Sci USA 99 (2002) 14434-14439
6. Ajdic D., and Pham V.T. Global transcriptional analysis of Streptococcus mutans sugar transporters using microarrays. J Bacteriol 189 (2007) 5049-5059
7. Len A.C., Harty D.W., and Jacques N.A. Stress-responsive proteins are upregulated in Streptococcus mutans during acid tolerance. Microbiology 150 (2004) 1339-1351
8. Decker E.M., Maier G., Axmann D., Brecx M., and von Ohle C. Effect of xylitol/chlorhexidine versus xylitol or chlorhexidine as single rinses on initial biofilm formation of cariogenic streptococci. Quintessence Int 39 (2008) 17-22
9. Padilla C., Lobos O., Hubert E., Poblete F., Navarro A., and Nunez L. In vitro antibacterial activity of the peptide PsVP-10 against Streptococcus mutans and Streptococcus sobrinus with and without glycocalyx. Int J Antimicrob Agents 27 (2006) 212-216
10. Duarte S., Gregoire S., Singh A.P., Vorsa N., Schaich K., Bowen W.H., et al. Inhibitory effects of cranberry polyphenols on formation and acidogenicity of Streptococcus mutans biofilms. FEMS Microbiol Lett 257 (2006) 50-56
11. Ahmad S., Weisburg W.G., and Jensen R.A. Evolution of aromatic amino acid biosynthesis and application to the fine-tuned phylogenetic positioning of enteric bacteria. J Bacteriol 172 (1990) 1051-1061
12. Christopherson R.I. Chorismate mutase-prephenate dehydrogenase from Escherichia coli: cooperative effects and inhibition by l-tyrosine. Arch Biochem Biophys 240 (1985) 646-654
13. Koch G.L., Shaw D.C., and Gibson F. Characterisation of the subunits of chorismate mutase-prephenate dehydrogenase from Escherichia coli K12. Biochim Biophys Acta 229 (1971) 805-812
14. Dayan J., and Sprinson D.B. Enzyme alterations in tyrosine and phenylalanine auxotrophs of Salmonella typhimurium. J Bacteriol 108 (1971) 1174-1180
15. Cotton R.G., and Gibson F. The biosynthesis of phenylalanine and tyrosine; enzymes converting chorismic acid into prephenic acid and their relationships to prephenate dehydratase and prephenate dehydrogenase. Biochim Biophys Acta 100 (1965) 76-88
16. Chen S., Vincent S., Wilson D.B., and Ganem B. Mapping of chorismate mutase and prephenate dehydrogenase domains in the Escherichia coli T-protein. Eur J Biochem 270 (2003) 757-763
17. Xu S., Yang Y., Jin R., Zhang M., and Wang H. Purification and characterization of a functionally active Mycobacterium tuberculosis prephenate dehydrogenase. Protein Expr Purif 49 (2006) 151-158
18. Sun W., Shahinas D., Bonvin J., Hou W., Kimber M.S., Turnbull J., et al. The crystal structure of Aquifex aeolicus prephenate dehydrogenase reveals the mode of tyrosine inhibition. J Biol Chem 284 (2009) 13223-13232
19. Sun W., Singh S., Zhang R., Turnbull J.L., and Christendat D. Crystal structure of prephenate dehydrogenase from Aquifex aeolicus. Insights into the catalytic mechanism. J Biol Chem 281 (2006) 12919-12928
20. Davidson B.E., and Hudson G.S. Chorismate mutase-prephenate dehydrogenase from Escherichia coli. Methods Enzymol 142 (1987) 440-450
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. Bonvin J., Aponte R.A., Marcantonio M., Singh S., Christendat D., and Turnbull J.L. Biochemical characterization of prephenate dehydrogenase from the hyperthermophilic bacterium Aquifex aeolicus. Protein Sci 15 (2006) 1417-1432
23. Bonner C.A., Jensen R.A., Gander J.E., and Keyhani N.O. A core catalytic domain of the TyrA protein family: arogenate dehydrogenase from Synechocystis. Biochem J 382 (2004) 279-291
24. Xia T., Zhao G., Fischer R.S., and Jensen R.A. A monofunctional prephenate dehydrogenase created by cleavage of the 5′ 109 bp of the tyrA gene from Erwinia herbicola. J Gen Microbiol 138 (1992) 1309-1316
25. Koch G.L., Shaw D.C., and Gibson F. The purification and characterisation of chorismate mutase-prephenate dehydrogenase from Escherichia coli K12. Biochim Biophys Acta 229 (1971) 795-804
26. Champney W.S., and Jensen R.A. The enzymology of prephenate dehydrogenase in Bacillus subtilis. J Biol Chem 245 (1970) 3763-3770
27. Turnbull J., Morrison J.F., and Cleland W.W. Kinetic studies on chorismate mutase-prephenate dehydrogenase from Escherichia coli: models for the feedback inhibition of prephenate dehydrogenase by l-tyrosine. Biochemistry 30 (1991) 7783-7788
28. + to chorismate mutase/prephenate dehydrogenase from Escherichia coli K12 and the effects of these ligands on the activity and self-association of the enzyme. Analysis in terms of a model. J Biol Chem 258 (1983) 3114-3120
29. Christendat D., and Turnbull J.L. Identifying groups involved in the binding of prephenate to prephenate dehydrogenase from Escherichia coli. Biochemistry 38 (1999) 4782-4793
30. Christendat D., Saridakis V.C., and Turnbull J.L. Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by chorismate mutase-prephenate dehydrogenase from Escherichia coli. Biochemistry 37 (1998) 15703-15712