메뉴 건너뛰기




Volumn 1804, Issue 9, 2010, Pages 1751-1759

Biochemical characterization of two thymidylate synthases in Corynebacterium glutamicum NCHU 87078

Author keywords

Corynebacterium glutamicum; FAD binding; Site based mutation; Thymidylate synthase A; Thymidylate synthase X

Indexed keywords

BACTERIAL PROTEIN; CORYNEBACTERIUM GLUTAMICUM THYMIDYLATE SYNTHASE A; CORYNEBACTERIUM GLUTAMICUM THYMIDYLATE SYNTHASE X; DIMER; FLAVINE ADENINE NUCLEOTIDE; TETRAMER; THYMIDYLATE SYNTHASE; UNCLASSIFIED DRUG; MESSENGER RNA; RECOMBINANT PROTEIN;

EID: 77955096031     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2010.05.006     Document Type: Article
Times cited : (6)

References (39)
  • 1
    • 0001744851 scopus 로고    scopus 로고
    • Escherichia and Salmonella: cellular and microbiology
    • Washington, DC, F.C. Neidhardt, R. Curtiss (Eds.)
    • Neuhard J., Kelln R.A. Escherichia and Salmonella: cellular and microbiology. Biosynthesis and conversion of pyrimidines 1996, 580-599. Washington, DC. F.C. Neidhardt, R. Curtiss (Eds.).
    • (1996) Biosynthesis and conversion of pyrimidines , pp. 580-599
    • Neuhard, J.1    Kelln, R.A.2
  • 3
    • 0037195380 scopus 로고    scopus 로고
    • Genetic evidence for a novel thymidylate synthase in the halophilic archaeon Halobacterium salinarum and in Campylobacter jejuni
    • Giladi M., Bitan-Banin G., Mevarech M., Ortenberg R. Genetic evidence for a novel thymidylate synthase in the halophilic archaeon Halobacterium salinarum and in Campylobacter jejuni. FEMS Microbiol. Lett. 2002, 216:105-109.
    • (2002) FEMS Microbiol. Lett. , vol.216 , pp. 105-109
    • Giladi, M.1    Bitan-Banin, G.2    Mevarech, M.3    Ortenberg, R.4
  • 4
    • 0029036377 scopus 로고
    • The catalytic mechanism and structure of thymidylate synthase
    • Carreras C.W., Santi D.V. The catalytic mechanism and structure of thymidylate synthase. Annu. Rev. Biochem. 1995, 64:721-762.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 721-762
    • Carreras, C.W.1    Santi, D.V.2
  • 5
    • 4043057882 scopus 로고    scopus 로고
    • Mechanistic studies of a flavin-dependent thymidylate synthase
    • Agrawal N., Lesley S.A., Kuhn P., Kohen A. Mechanistic studies of a flavin-dependent thymidylate synthase. Biochemistry 2004, 43:10295-12301.
    • (2004) Biochemistry , vol.43 , pp. 10295-12301
    • Agrawal, N.1    Lesley, S.A.2    Kuhn, P.3    Kohen, A.4
  • 10
    • 0142103146 scopus 로고    scopus 로고
    • Functional analysis of substrate and cofactor complex structures of a thymidylate synthase-complementing protein
    • Mathews A.M., Deacon J.M.Canaves, McMullan D., Lesley S.A., Agarwalla S., Kuhn P. Functional analysis of substrate and cofactor complex structures of a thymidylate synthase-complementing protein. Structure 2003, 11:677-690.
    • (2003) Structure , vol.11 , pp. 677-690
    • Mathews, A.M.1    Deacon, J.2    McMullan, D.3    Lesley, S.A.4    Agarwalla, S.5    Kuhn, P.6
  • 12
    • 0037025202 scopus 로고    scopus 로고
    • DNA building block reinvented
    • Murzin A.G. DNA building block reinvented. Science 2002, 297:61-62.
    • (2002) Science , vol.297 , pp. 61-62
    • Murzin, A.G.1
  • 13
    • 4444319825 scopus 로고    scopus 로고
    • Bacterial thymidylate synthase with intein, group II intron, and distinctive ThyX motifs
    • Liu X.Q., Yang J. Bacterial thymidylate synthase with intein, group II intron, and distinctive ThyX motifs. J. Bacteriol. 2004, 186:6316-6319.
    • (2004) J. Bacteriol. , vol.186 , pp. 6316-6319
    • Liu, X.Q.1    Yang, J.2
  • 14
    • 24944591878 scopus 로고    scopus 로고
    • Structure of the Mycobacterium tuberculosis flavin dependent thymidylate synthase (MtbThyX) at 2.0Å resolution
    • Sampathkumar P., Turley S., Ulmer J.E., Rhie H.G., Sibley C.H., Hol W.G. Structure of the Mycobacterium tuberculosis flavin dependent thymidylate synthase (MtbThyX) at 2.0Å resolution. J. Mol. Biol. 2005, 352:1091-1104.
    • (2005) J. Mol. Biol. , vol.352 , pp. 1091-1104
    • Sampathkumar, P.1    Turley, S.2    Ulmer, J.E.3    Rhie, H.G.4    Sibley, C.H.5    Hol, W.G.6
  • 18
    • 48249126476 scopus 로고    scopus 로고
    • Kinetics and ligand-binding preferences of Mycobacterium tuberculosis thymidylate synthases, ThyA and ThyX
    • Hunter J.H., Gujjar R., Pang C.K., Rathod P.K. Kinetics and ligand-binding preferences of Mycobacterium tuberculosis thymidylate synthases, ThyA and ThyX. PLoS ONE 2008, 3:e2237.
    • (2008) PLoS ONE , vol.3
    • Hunter, J.H.1    Gujjar, R.2    Pang, C.K.3    Rathod, P.K.4
  • 20
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho S.N., Hunt H.D., Horton R.M., Pullen J.K., Pease L.R. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 1989, 77:51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 21
    • 33746274673 scopus 로고    scopus 로고
    • Structure-stability-activity relationship in covalently cross-linked N-carbamoyl-d-amino acid amidohydrolase and N-acylamino acid racemase
    • Chiu W.C., You J.Y., Liu J.S., Hsu S.K., Hsu W.H., Shih C.H., Hwang J.K., Wang W.C. Structure-stability-activity relationship in covalently cross-linked N-carbamoyl-d-amino acid amidohydrolase and N-acylamino acid racemase. J. Mol. Biol. 2006, 359:741-753.
    • (2006) J. Mol. Biol. , vol.359 , pp. 741-753
    • Chiu, W.C.1    You, J.Y.2    Liu, J.S.3    Hsu, S.K.4    Hsu, W.H.5    Shih, C.H.6    Hwang, J.K.7    Wang, W.C.8
  • 22
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 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. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 23
    • 14044273636 scopus 로고    scopus 로고
    • Catalytic mechanism of Chlamydia trachomatis flavin-dependent thymidylate synthase
    • Griffin J., Roshick C., Iliffe-Lee E., McClarty G. Catalytic mechanism of Chlamydia trachomatis flavin-dependent thymidylate synthase. J. Biol. Chem. 2005, 280:5456-5467.
    • (2005) J. Biol. Chem. , vol.280 , pp. 5456-5467
    • Griffin, J.1    Roshick, C.2    Iliffe-Lee, E.3    McClarty, G.4
  • 24
    • 0002242695 scopus 로고
    • Direct spectrophotometric evidence for the oxidation of tetrahydrofolate during the enzymatic synthesis of thymidylate
    • Wahba A.J., Friedkin M. Direct spectrophotometric evidence for the oxidation of tetrahydrofolate during the enzymatic synthesis of thymidylate. J. Biol. Chem. 1961, 236:PC11-PC12.
    • (1961) J. Biol. Chem. , vol.236
    • Wahba, A.J.1    Friedkin, M.2
  • 26
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Meth. Enzymol. 1997, 276:307-326.
    • (1997) Meth. Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 27
    • 84920325457 scopus 로고
    • AMoRe: an automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A Found. Crystallogr. 1994, 50:157-163.
    • (1994) Acta Crystallogr. A Found. Crystallogr. , vol.50 , pp. 157-163
    • Navaza, J.1
  • 30
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A Found. Crystallogr. 1991, 47:110-119.
    • (1991) Acta Crystallogr. A Found. Crystallogr. , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 32
    • 31344462130 scopus 로고    scopus 로고
    • Function and evolution of plasmid-borne genes for pyrimidine biosynthesis in Borrelia spp
    • Zhong J., Skouloubris S., Dai Q., Myllykallio H., Barbour A.G. Function and evolution of plasmid-borne genes for pyrimidine biosynthesis in Borrelia spp. J. Bacteriol. 2006, 188:909-918.
    • (2006) J. Bacteriol. , vol.188 , pp. 909-918
    • Zhong, J.1    Skouloubris, S.2    Dai, Q.3    Myllykallio, H.4    Barbour, A.G.5
  • 34
    • 0025149019 scopus 로고
    • Crystal structure of Escherichia coli thymidylate synthase containing bound 5-fluoro-2'-deoxyuridylate and 10-propargyl-5, 8-dideazafolate
    • Matthews D.A., Appelt K., Oatley S.J., Xuong N.H. Crystal structure of Escherichia coli thymidylate synthase containing bound 5-fluoro-2'-deoxyuridylate and 10-propargyl-5, 8-dideazafolate. J. Mol. Biol. 1990, 214:923-936.
    • (1990) J. Mol. Biol. , vol.214 , pp. 923-936
    • Matthews, D.A.1    Appelt, K.2    Oatley, S.J.3    Xuong, N.H.4
  • 35
    • 0023971856 scopus 로고
    • Functional role of cysteine-146 in Escherichia coli thymidylate synthase
    • Dev I.K., Yates B.B., Leong J., Dallas W.S. Functional role of cysteine-146 in Escherichia coli thymidylate synthase. Proc. Natl Acad. Sci. U. S. A. 1988, 85:1472-1476.
    • (1988) Proc. Natl Acad. Sci. U. S. A. , vol.85 , pp. 1472-1476
    • Dev, I.K.1    Yates, B.B.2    Leong, J.3    Dallas, W.S.4
  • 36
    • 33745270753 scopus 로고    scopus 로고
    • + expels both the co-factor and a substrate analog from the Mycobacterium tuberculosis ThyX active site: opportunities for anti-bacterial drug design
    • + expels both the co-factor and a substrate analog from the Mycobacterium tuberculosis ThyX active site: opportunities for anti-bacterial drug design. J. Mol. Biol. 2006, 360:1-6.
    • (2006) J. Mol. Biol. , vol.360 , pp. 1-6
    • Sampathkumar, P.1    Turley, S.2    Sibley, C.H.3    Hol, W.G.4
  • 37
    • 0030623823 scopus 로고    scopus 로고
    • Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential
    • Bahar I., Atilgan A.R., Erman B. Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential. Fold. Des. 1997, 2:173-181.
    • (1997) Fold. Des. , vol.2 , pp. 173-181
    • Bahar, I.1    Atilgan, A.R.2    Erman, B.3
  • 38
    • 40449136466 scopus 로고    scopus 로고
    • Functional analysis of the Mycobacterium tuberculosis FAD-dependent thymidylate synthase, ThyX, reveals new amino acid residues contributing to an extended ThyX motif
    • Ulmer J.E., Boum Y., Thouvenel C.D., Myllykallio H., Sibley C.H. Functional analysis of the Mycobacterium tuberculosis FAD-dependent thymidylate synthase, ThyX, reveals new amino acid residues contributing to an extended ThyX motif. J. Bacteriol. 2008, 190:2056-2064.
    • (2008) J. Bacteriol. , vol.190 , pp. 2056-2064
    • Ulmer, J.E.1    Boum, Y.2    Thouvenel, C.D.3    Myllykallio, H.4    Sibley, C.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.