Corrigendum to "Kinetic characterization and quaternary structure of glutamate racemase from the periodontal anaerobe Fusobacterium nucleatum" [Archives of Biochemistry and Biophysics 491 (2009) 16-24] (DOI:10.1016/j.abb.2009.09.009);Kinetic characterization and quaternary structure of glutamate racemase from the periodontal anaerobe Fusobacterium nucleatum

Archives of Biochemistry and Biophysics

Volumn 491, Issue 1-2, 2009, Pages 16-24

  Potrykus, Joanna ^a   Flemming, Janette ^a   Bearne, Stephen L ^a,b  

^a DALHOUSIE UNIVERSITY   (Canada)

^b DALHOUSIE UNIVERSITY   (Canada)

Author keywords

Bacillus subtilis; Fusobacterium nucleatum; Glutamate racemase; Kinetics; Mutagenesis; pH activity; Pseudosymmetry; Quaternary structure; Substrate specificity

Indexed keywords

ALANINE; DIMER; GLUTAMATE RACEMASE; RACEMASE; UNCLASSIFIED DRUG; VALINE;

AMINO ACID SEQUENCE; ARTICLE; BACILLUS SUBTILIS; CATALYSIS; CONTROLLED STUDY; ENANTIOMER; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME LOCALIZATION; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SYNTHESIS; FUSOBACTERIUM NUCLEATUM; MOUTH FLORA; MUTATIONAL ANALYSIS; NONHUMAN; OPEN READING FRAME; PERIODONTAL DISEASE; PH; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN CROSS LINKING; PROTEIN QUATERNARY STRUCTURE; RACEMIZATION; SPECIES COMPARISON;

BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS); FUSOBACTERIUM NUCLEATUM; NEGIBACTERIA;

ALANINE; AMINO ACID ISOMERASES; AMINO ACID SEQUENCE; BIOCATALYSIS; BIOFILMS; CLONING, MOLECULAR; DRUG DISCOVERY; FUSOBACTERIUM NUCLEATUM; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR SEQUENCE DATA; OPEN READING FRAMES; PERIODONTAL DISEASES; PROTEIN STRUCTURE, QUATERNARY; SUBSTRATE SPECIFICITY;

EID: 70350321289     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2009.12.006     Document Type: Erratum

References (78)

1. Cohen M.L. Science 257 (1992) 1050-1055
2. Ochman H., Lawrence J.G., and Groisman E.A. Nature 405 (2000) 299-304
3. Finch R. J. Antimicrob. Chemother. 60 Suppl. 1 (2007) i79-i82
4. Höltje J.V. Microbiol. Mol. Biol. Rev. 62 (1998) 181-203
5. Ju J., Misono H., and Ohnishi K. J. Biosci. Bioeng. 100 (2005) 246-254
6. Schleifer K.H., and Kandler O. Bacteriol. Rev. 36 (1972) 407-477
7. van Heijenoort J. Nat. Prod. Rep. 18 (2001) 503-519
8. Pucci M.J., Thanassi J.A., Ho H.T., Falk P.J., and Dougherty T.J. J. Bacteriol. 177 (1995) 336-342
9. Song J.H., Ko K.S., Lee J.Y., Baek J.Y., Oh W.S., Yoon H.S., Jeong J.Y., and Chun J. Mol. Cells 19 (2005) 365-374
10. Tanner M.E. Acc. Chem. Res. 35 (2002) 237-246
11. Gallo K.A., and Knowles J.R. Biochemistry 32 (1993) 3981-3990
12. Gallo K.A., Tanner M.E., and Knowles J.R. Biochemistry 32 (1993) 3991-3997
13. Tanner M.E., Gallo K.A., and Knowles J.R. Biochemistry 32 (1993) 3998-4006
14. Hwang K.Y., Cho C.S., Kim S.S., Sung H.C., Yu Y.G., and Cho Y. Nat. Struct. Biol. 6 (1999) 422-426
15. Kim K.H., Bong Y.J., Park J.K., Shin K.J., Hwang K.Y., and Kim E.E. J. Mol. Biol. 372 (2007) 434-443
16. Lundqvist T., Fisher S.L., Kern G., Folmer R.H., Xue Y., Newton D.T., Keating T.A., Alm R.A., and de Jonge B.L. Nature 447 (2007) 817-822
17. May M., Mehboob S., Mulhearn D.C., Wang Z., Yu H., Thatcher G.R., Santarsiero B.D., Johnson M.E., and Mesecar A.D. J. Mol. Biol. 371 (2007) 1219-1237
18. Ruzheinikov S.N., Taal M.A., Sedelnikova S.E., Baker P.J., and Rice D.W. Structure 13 (2005) 1707-1713
19. de Dios A., Prieto L., Martin J.A., Rubio A., Ezquerra J., Tebbe M., Lopez de Uralde B., Martin J., Sanchez A., LeTourneau D.L., McGee J.E., Boylan C., Parr T.R., and Smith M.C. J. Med. Chem. 45 (2002) 4559-4570
20. Doublet P., van Heijenoort J., Bohin J.P., and Mengin-Lecreulx D. J. Bacteriol. 175 (1993) 2970-2979
21. Kim W.C., Rhee H.I., Park B.K., Suk K.H., and Cha S.H. J. Biomol. Screen. 5 (2000) 435-440
22. de Almeida Leone P., Carroll A.R., Towerzey L., King G., McArdle B.M., Kern G., Fisher S., Hooper J.N., and Quinn R.J. Org. Lett. 10 (2008) 2585-2588
23. de Jonge B.L., Kutschke A., Uria-Nickelsen M., Kamp H.D., and Mills S.D. Antimicrob. Agents Chemother. (2009) (E-pub, ahead of print)
24. Geng B., Basarab G., Comita-Prevoir J., Gowravaram M., Hill P., Kiely A., Loch J., MacPherson L., Morningstar M., Mullen G., Osimboni E., Satz A., Eyermann C., and Lundqvist T. Bioorg. Med. Chem. Lett. 19 (2009) 930-936
25. Breault G.A., Comita-Prevoir J., Eyermann C.J., Geng B., Petrichko R., Doig P., Gorseth E., and Noonan B. Bioorg. Med. Chem. Lett. 18 (2008) 6100-6103
26. Spies M.A., Reese J.G., Dodd D., Pankow K.L., Blanke S.R., and Baudry J. J. Am. Chem. Soc. 131 (2009) 5274-5284
27. Tanner M.E., and Miao S. Tetrahedron Lett. 35 (1994) 4073-7076
28. Glavas S., and Tanner M.E. Bioorg. Med. Chem. Lett. 7 (1997) 2265-2270
29. Taal M.A., Sedelnikova S.E., Ruzheinikov S.N., Baker P.J., and Rice D.W. Acta Crystallogr. D Biol. Crystallogr. 60 (2004) 2031-2034
30. Yagasaki M., Iwata K., Ishino S., Azuma M., and Ozaki A. Biosci. Biotechnol. Biochem. 59 (1995) 610-614
31. Liu L., Yoshimura T., Endo K., Esaki N., and Soda K. J. Biochem. (Tokyo) 121 (1997) 1155-1161
32. Doublet P., van Heijenoort J., and Mengin-Lecreulx D. Biochemistry 33 (1994) 5285-5290
33. Doublet P., van Heijenoort J., and Mengin-Lecreulx D. Microb. Drug Resist. 2 (1996) 43-49
34. Pucci M.J., Novotny J., Discotto L.F., and Dougherty T.J. J. Bacteriol. 176 (1994) 528-530
35. Yoshimura T., Ashiuchi M., Esaki N., Kobatake C., Choi S.Y., and Soda K. J. Biol. Chem. 268 (1993) 24242-24246
36. Ho H.T., Falk P.J., Ervin K.M., Krishnan B.S., Discotto L.F., Dougherty T.J., and Pucci M.J. Biochemistry 34 (1995) 2464-2470
37. Kim S.S., Choi I.G., Kim S.H., and Yu Y.G. Extremophiles 3 (1999) 175-183
38. Dodd D., Reese J.G., Louer C.R., Ballard J.D., Spies M.A., and Blanke S.R. J. Bacteriol. 189 (2007) 5265-5275
39. Piovano S. Anaerobe 5 (1999) 221-227
40. W.H. Organization, the World Oral Health Report 2003, Continuous Improvement in Oral Health in the 21st Century - the Approach of the WHO Global Oral Health Programme, 2003.
41. Bartold P.M., Gully N.J., Zilm P.S., and Rogers A.H. J. Periodontal Res. 26 (1991) 314-322
42. Singer R.E., and Buckner B.A. Infect. Immun. 32 (1981) 458-463
43. Kolenbrander P.E., Andersen R.N., and Moore L.V. Appl. Environ. Microbiol. 56 (1990) 3890-3894
44. Kolenbrander P.E., and London J. J. Bacteriol. 175 (1993) 3247-3252
45. J. Sambrook, E.F. Fritsch, T. Maniatis, in: Molecular Cloning, Cold Spring Harbor Laboratory Press, Plainview, New York, pp. 1.21-1.52.
46. Potrykus J., Mahaney B., White R.L., and Bearne S.L. Proteomics 7 (2007) 1839-1853
47. Hanahan D. J. Mol. Biol. 166 (1983) 557-580
48. Studier F.W., and Moffatt B.A. J. Mol. Biol. 189 (1986) 113-130
49. Braman J., Papworth C., and Greener A. Methods Mol. Biol. 57 (1996) 31-44
50. Novagen, pET System Manual, seventh ed., TB055, 1997, pp. 18-64.
51. Niepmann M., and Zheng J. Electrophoresis 27 (2006) 3949-3951
52. Ferguson K.A. Metabolism 13 (1964) 985-1002
53. Kluger R., and Alagic A. Bioorg. Chem. 32 (2004) 451-472
54. Ashiuchi M., Kuwana E., Komatsu K., Soda K., and Misono H. FEMS Microbiol. Lett. 223 (2003) 221-225
55. Ashiuchi M., Kuwana E., Yamamoto T., Komatsu K., Soda K., and Misono H. J. Biol. Chem. 277 (2002) 39070-39073
56. Sengupta S., Shah M., and Nagaraja V. Nucleic Acids Res. 34 (2006) 5567-5576
57. Doublet P., van Heijenoort J., and Mengin-Lecreulx D. J. Bacteriol. 174 (1992) 5772-5779
58. Ashiuchi M., and Misono H. Appl. Microbiol. Biotechnol. 59 (2002) 9-14
59. Kada S., Nanamiya H., Kawamura F., and Horinouchi S. FEMS Microbiol. Lett. 236 (2004) 13-20
60. Kimura K., Tran L.S., and Itoh Y. Microbiology 150 (2004) 2911-2920
61. Segel I.H. Enzyme Kinetics (1975), John Wiley and Sons Inc., New York
62. Horiike K., Tojo H., Yamano T., and Nozaki M. J. Biochem. (Tokyo) 93 (1983) 99-106
63. le Maire M., Viel A., and Moller J.V. Anal. Biochem. 177 (1989) 50-56
64. Schagger H., and von Jagow G. Anal. Biochem. 199 (1991) 223-231
65. Wittig I., Braun H.P., and Schagger H. Nat. Protoc. 1 (2006) 418-428
66. Camacho-Carvajal M.M., Wollscheid B., Aebersold R., Steimle V., and Schamel W.W. Mol. Cell. Proteomics 3 (2004) 176-182
67. Wittig I., and Schagger H. Proteomics 5 (2005) 4338-4346
68. Green N.S., Reisler E., and Houk K.N. Protein Sci. 10 (2001) 1293-1304
69. K. Kobayashi, S.D. Ehrlich, A. Albertini, G. Amati, K.K. Andersen, M. Arnaud, K. Asai, S. Ashikaga, S. Aymerich, P. Bessieres, F. Boland, S.C. Brignell, S. Bron, K. Bunai, J. Chapuis, L.C. Christiansen, A. Danchin, M. Debarbouille, E. Dervyn, E. Deuerling, K. Devine, S.K. Devine, O. Dreesen, J. Errington, S. Fillinger, S.J. Foster, Y. Fujita, A. Galizzi, R. Gardan, C. Eschevins, T. Fukushima, K. Haga, C.R. Harwood, M. Hecker, D. Hosoya, M.F. Hullo, H. Kakeshita, D. Karamata, Y. Kasahara, F. Kawamura, K. Koga, P. Koski, R. Kuwana, D. Imamura, M. Ishimaru, S. Ishikawa, I. Ishio, D. Le Coq, A. Masson, C. Mauel, R. Meima, R.P. Mellado, A. Moir, S. Moriya, E. Nagakawa, H. Nanamiya, S. Nakai, P. Nygaard, M. Ogura, T. Ohanan, M. O'Reilly, M. O'Rourke, Z. Pragai, H.M. Pooley, G. Rapoport, J.P. Rawlins, L.A. Rivas, C. Rivolta, A. Sadaie, Y. Sadaie, M. Sarvas, T. Sato, H.H. Saxild, E. Scanlan, W. Schumann, J.F. Seegers, J. Sekiguchi, A. Sekowska, S.J. Seror, M. Simon, P. Stragier, R. Studer, H. Takamatsu, T. Tanaka, M. Takeuchi, H.B. Thomaides, V. Vagner, J.M. van Dijl, K. Watabe, A. Wipat, H. Yamamoto, M. Yamamoto, Y. Yamamoto, K. Yamane, K. Yata, K. Yoshida, H. Yoshikawa, U. Zuber, N. Ogasawara, Proc. Natl. Acad. Sci. USA 100 (2003) 4678-4683.
70. Kumar P.S., Griffen A.L., Barton J.A., Paster B.J., Moeschberger M.L., and Leys E.J. J. Dent. Res. 82 (2003) 338-344
71. Liebana J., Castillo A.M., and Alvarez M. Med. Oral Patol. Oral Cir. Bucal 9 Suppl. (2004) S75-S91
72. Mehboob S., Guo L., Fu W., Mittal A., Yau T., Truong K., Johlfs M., Long F., Fung L.W., and Johnson M.E. Biochemistry 48 (2009) 7045-7055
73. W.P. Jencks, J. Regenstein, Ionization constants of acids and bases, in: H.A. Sober (Ed.), Handbook of Biochemistry, The Chemical Rubber Co., Cleveland, Ohio, pp. J150-J189.
74. Glavas S., and Tanner M.E. Biochemistry 38 (1999) 4106-4113
75. Sims P.A., Larsen T.M., Poyner R.R., Cleland W.W., and Reed G.H. Biochemistry 42 (2003) 8298-8306
76. Kallarakal A.T., Mitra B., Kozarich J.W., Gerlt J.A., Clifton J.G., Petsko G.A., and Kenyon G.L. Biochemistry 34 (1995) 2788-2797
77. Larkin M.A., Blackshields G., Brown N., Chenna R., McGettigan P.A., McWilliam H., Valentin F., Wallace I.M., Wilm A., Lopez R., Thompson J.D., Gibson T.J., and Higgins D.G. Bioinformatics 23 (2007) 2947-2948
78. W.L. DeLano, MacPyMOL: A PyMOL-based Molecular Graphics Application for MacOS X, DeLano Scientific LLC, Palo Alto, CA, USA, 2007. Available from: .