메뉴 건너뛰기




Volumn 6, Issue 4, 1999, Pages 359-365

The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia

Author keywords

[No Author keywords available]

Indexed keywords

FOLIC ACID; METHYLENETETRAHYDROFOLATE DEHYDROGENASE; MUTANT PROTEIN;

EID: 0032895522     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/7594     Document Type: Article
Times cited : (374)

References (38)
  • 1
    • 0029049553 scopus 로고
    • A candidate genetic risk factor for vascular disease: A common mutation in methylenetetrahydrofolate reductase
    • Frosst, P. et al. A candidate genetic risk factor for vascular disease: a common mutation in methylenetetrahydrofolate reductase. Nature Genet. 10, 111-113 (1995).
    • (1995) Nature Genet. , vol.10 , pp. 111-113
    • Frosst, P.1
  • 2
    • 0029655724 scopus 로고    scopus 로고
    • Molecular genetic analysis in mild hyperhomocysteinemia: A common mutation in the methylenetetrahydrofolate reductase gene is a genetic risk factor for cardiovascular disease
    • Kluijtmans, LA. et al. Molecular genetic analysis in mild hyperhomocysteinemia: a common mutation in the methylenetetrahydrofolate reductase gene is a genetic risk factor for cardiovascular disease. Am. J. Hum. Genet. 58, 35-41 (1996).
    • (1996) Am. J. Hum. Genet. , vol.58 , pp. 35-41
    • Kluijtmans, L.A.1
  • 3
    • 0030897112 scopus 로고    scopus 로고
    • Genetic polymorphism of 5, 10-methylenetetrahydrofolate reductase (MTHFR) as a risk factor for coronary artery disease
    • Morita, H. et al. Genetic polymorphism of 5, 10-methylenetetrahydrofolate reductase (MTHFR) as a risk factor for coronary artery disease. Circulation 95, 2032-2036(1997).
    • (1997) Circulation , vol.95 , pp. 2032-2036
    • Morita, H.1
  • 4
    • 0030057401 scopus 로고    scopus 로고
    • Distribution in healthy and coronary populations of the methylenetetrahydrofolate reductase (MTHFR) C677T mutation
    • Wilcken, D.E., Wang, X.L, Sim, A.S. & McCredie, R.M. Distribution in healthy and coronary populations of the methylenetetrahydrofolate reductase (MTHFR) C677T mutation. Arteroider. Thromb. Vase. Biol. 16, 878-882 (1996).
    • (1996) Arteroider. Thromb. Vase. Biol. , vol.16 , pp. 878-882
    • Wilcken, D.E.1    Wang, X.L.2    Sim, A.S.3    McCredie, R.M.4
  • 5
    • 0029806746 scopus 로고    scopus 로고
    • Methylenetetrahydrofolate reductase polymorphism, plasma folate, homocysteine, and risk of myocardial infarction in US physicians
    • Ma, J. et al. Methylenetetrahydrofolate reductase polymorphism, plasma folate, homocysteine, and risk of myocardial infarction in US physicians. Circulation 94, 2410-2416(1996).
    • (1996) Circulation , vol.94 , pp. 2410-2416
    • Ma, J.1
  • 6
    • 0030027668 scopus 로고    scopus 로고
    • Relation between folate status, a common mutation in methylenetetrahydrofolate reductase, and plasma homocysteine concentrations
    • . 6. Jacques, P.F. et aL Relation between folate status, a common mutation in methylenetetrahydrofolate reductase, and plasma homocysteine concentrations. Circulation 93, 7-9 (1996).
    • (1996) Circulation , vol.93 , pp. 7-9
    • Jacques, P.F.1
  • 7
    • 0029738540 scopus 로고    scopus 로고
    • The common "thermolabile" variant of methylenetetrahydrofolate reductase is a major determinant of mild hyperhomocysteinaemia
    • Harmon, D.L. et al. The common "thermolabile" variant of methylenetetrahydrofolate reductase is a major determinant of mild hyperhomocysteinaemia. Q. J. Med. 89, 515-577(1996).
    • (1996) Q. J. Med. , vol.89 , pp. 515-577
    • Harmon, D.L.1
  • 10
    • 0031066138 scopus 로고    scopus 로고
    • Is the common 677C-VT mutation in the methylenetetrahydrofolate reductase gene a risk factor for neural tube defects? a meta-analysis
    • van der Put, N.M.J., Eskes, T.K.A.B. & Blom, H.J. Is the common 677C-VT mutation in the methylenetetrahydrofolate reductase gene a risk factor for neural tube defects? A meta-analysis. Q. J. Med. 90, 111-115 (1997).
    • (1997) Q. J. Med. , vol.90 , pp. 111-115
    • Van Der Put, N.M.J.1    Eskes, T.K.A.B.2    Blom, H.J.3
  • 11
    • 0029066299 scopus 로고
    • A quantitative assessment of plasma homocysteine as a risk factor for vascular disease
    • Boushey, C.J., Beresford. S.A.A. Omenn, G.S. & Motulsky, A.G. A quantitative assessment of plasma homocysteine as a risk factor for vascular disease. JAMA 274, 1049-1057(1995).
    • (1995) JAMA , vol.274 , pp. 1049-1057
    • Boushey, C.J.1    Beresford, S.A.A.2    Omenn, G.S.3    Motulsky, A.G.4
  • 13
    • 0028304102 scopus 로고
    • Human methylenetetrahydrofolate reductase: Isolation of cDNA, mapping and mutation identification
    • Goyette, P. et al. Human methylenetetrahydrofolate reductase: isolation of cDNA, mapping and mutation identification. Nature Genet. 7, 195-200 (1994).
    • (1994) Nature Genet. , vol.7 , pp. 195-200
    • Goyette, P.1
  • 14
    • 0026030641 scopus 로고
    • Database of homology-derived protein structures and the structural meaning of sequence alignment
    • Sander, C. & Schneider, R. Database of homology-derived protein structures and the structural meaning of sequence alignment. Proteins 9, 56-68 (1991).
    • (1991) Proteins , vol.9 , pp. 56-68
    • Sander, C.1    Schneider, R.2
  • 15
    • 0029847109 scopus 로고    scopus 로고
    • Severe and mild mutations in cis for the methylenetetrahydofolate reductase (MTHFR) gene, and description of five novel mutations in MTHFR
    • Goyette, P., Christensen, B., Rosenblatt, D.S. & Rozen, R. Severe and mild mutations in cis for the methylenetetrahydofolate reductase (MTHFR) gene, and description of five novel mutations in MTHFR. Am. J. Hum. Genet. 59, 1268-1275 (1996).
    • (1996) Am. J. Hum. Genet. , vol.59 , pp. 1268-1275
    • Goyette, P.1    Christensen, B.2    Rosenblatt, D.S.3    Rozen, R.4
  • 16
    • 0028905178 scopus 로고
    • Seven novel mutations in the methylenetetrahydrofolate reductase gene and genotype/phenotype correlations in severe methylenetetrahydrofolate reductase deficiency
    • Goyette, P., Fresst, P., Rosenblatt, D.S. & Rozen, R. Seven novel mutations in the methylenetetrahydrofolate reductase gene and genotype/phenotype correlations in severe methylenetetrahydrofolate reductase deficiency. Am. J. Hum. Genet. 56, 1052-1059 (1995).
    • (1995) Am. J. Hum. Genet. , vol.56 , pp. 1052-1059
    • Goyette, P.1    Fresst, P.2    Rosenblatt, D.S.3    Rozen, R.4
  • 17
    • 0024962365 scopus 로고
    • Refined structure of spinach glycolate oxidase at 2 a resolution
    • Lindqvist, Y. Refined structure of spinach glycolate oxidase at 2 A resolution. J. Mol. Biol. 209, 151-166 (1989).
    • (1989) J. Mol. Biol. , vol.209 , pp. 151-166
    • Lindqvist, Y.1
  • 18
    • 0025278264 scopus 로고
    • Molecular structure of flavocytochrome b2 at 2.4 a resolution
    • Xia, Z.X. & Mathews, F.S. Molecular structure of flavocytochrome b2 at 2.4 A resolution./ Mol. Biol. 212.837-863 (1990).
    • (1990) Mol. Biol. , vol.212 , pp. 837-863
    • Xia, Z.X.1    Mathews, F.S.2
  • 19
    • 0028774535 scopus 로고
    • Old yellow enzyme at 2 a resolution: Overall structure, ligand binding, and comparison with related flavoproteins
    • Fox, K.M. & Karplus, P.A. Old yellow enzyme at 2 A resolution: overall structure, ligand binding, and comparison with related flavoproteins. Structure 2, 1089-1105(1994).
    • (1994) Structure , vol.2 , pp. 1089-1105
    • Fox, K.M.1    Karplus, P.A.2
  • 20
    • 0022982155 scopus 로고
    • Three-dimensional structure of the iron-sulfur flavoprotein trimethylamine dehydrogenase at 2.4 a resolution
    • Lim, L.W. Three-dimensional structure of the iron-sulfur flavoprotein trimethylamine dehydrogenase at 2.4 A resolution. J. Biol. Chem. 261, 15140-15146(1986).
    • (1986) J. Biol. Chem. , vol.261 , pp. 15140-15146
    • Lim, L.W.1
  • 21
    • 0031568812 scopus 로고    scopus 로고
    • The crystal structure of the flavin containing enzyme dihydroorotate dehydrogenase a from
    • Rowland, P., Nielsen, F.S., Jensen, K.F. & Larsen, S. The crystal structure of the flavin containing enzyme dihydroorotate dehydrogenase A from Lactococcus /art. Structure 5. 239-252 (1997).
    • (1997) Lactococcus /Art. Structure , vol.5 , pp. 239-252
    • Rowland, P.1    Nielsen, F.S.2    Jensen, K.F.3    Larsen, S.4
  • 22
    • 0000282187 scopus 로고
    • Stereochemistry and mechanism of hydrogen transfer between NADPH and methylenetetrahydrofolate in the reaction catalyzed by methylenetetrahydrofolate reductase from pig liver
    • Sumner, J.S. & Matthews, R.G. Stereochemistry and mechanism of hydrogen transfer between NADPH and methylenetetrahydrofolate in the reaction catalyzed by methylenetetrahydrofolate reductase from pig liver. J. Am. Chem. Soc. 114, 6949-6956 (1992).
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6949-6956
    • Sumner, J.S.1    Matthews, R.G.2
  • 23
    • 0025265852 scopus 로고
    • Rubredoxin reductase of Pseudomonas oleovorans. Structural relationship to other flavoprotein oxidoreductases based on one NAD and two FAD fingerprints
    • Eggink, G., Engel, H., Vriend, G., Terpstra, P. & Witholt, B. Rubredoxin reductase of Pseudomonas oleovorans. Structural relationship to other flavoprotein oxidoreductases based on one NAD and two FAD fingerprints. J. Mol. Biol. 212, 135-142(1990).
    • (1990) J. Mol. Biol , vol.212 , pp. 135-142
    • Eggink, G.1    Engel, H.2    Vriend, G.3    Terpstra, P.4    Witholt, B.5
  • 24
    • 0032945180 scopus 로고    scopus 로고
    • Purification and properties of NADH-dependent 5, 10-methylenetetrahydrofolate reductase from
    • Sheppard, CA., Trimmer, E.E. & Matthews, R.G. Purification and properties of NADH-dependent 5, 10-methylenetetrahydrofolate reductase from Escherichia coli.J. Bacteriol. 181.718-725 (1999).
    • (1999) Escherichia Coli.J. Bacteriol. , vol.181 , pp. 718-725
    • Sheppard, C.A.1    Trimmer, E.E.2    Matthews, R.G.3
  • 25
    • 0026034240 scopus 로고
    • Thermolabile methylenetetrahydrofolate reductase: An inherited risk factor for coronary artery disease
    • Kang, S.-S. etal. Thermolabile methylenetetrahydrofolate reductase: an inherited risk factor for coronary artery disease. Am. J. Hum. Genet. 48, 536-545 (1991).
    • (1991) Am. J. Hum. Genet , vol.48 , pp. 536-545
    • Kang, S.-S.1
  • 26
    • 0032575295 scopus 로고    scopus 로고
    • Thermodynamic stability of arachaeal histones
    • U, W.-T. etal. Thermodynamic stability of arachaeal histones. Biochemistry 37, 10563-10572(1998).
    • (1998) Biochemistry , vol.37 , pp. 10563-10572
    • W-T, U.1
  • 27
    • 0019323528 scopus 로고
    • Interactions of pig liver methylenetetrahydrofolate reductase with methylenetetrahydropteroylpolyglutamate substrates and with dihydropteroylpolyglutamate inhibitors
    • Matthews, R.G. & Baugh, C.M. Interactions of pig liver methylenetetrahydrofolate reductase with methylenetetrahydropteroylpolyglutamate substrates and with dihydropteroylpolyglutamate inhibitors. Biochemistry 19, 2040-2045 (1980).
    • (1980) Biochemistry , vol.19 , pp. 2040-2045
    • Matthews, R.G.1    Baugh, C.M.2
  • 28
    • 0029109468 scopus 로고
    • Protein-protein interactions: A review of protein dimer structures
    • Jones, S. & Thornton, J.M. Protein-protein interactions: a review of protein dimer structures. Prog. Biophys. Mol. Biol. 63, 31-65 (1995).
    • (1995) Prog. Biophys. Mol. Biol. , vol.63 , pp. 31-65
    • Jones, S.1    Thornton, J.M.2
  • 29
    • 0030997363 scopus 로고    scopus 로고
    • Hydrophobie patches on protein subunit interfaces: Characteristics and prediction
    • Lijnzaad, P. & Argos, P. Hydrophobie patches on protein subunit interfaces: characteristics and prediction. Proteins 28, 333-343 (1997).
    • (1997) Proteins , vol.28 , pp. 333-343
    • Lijnzaad, P.1    Argos, P.2
  • 30
    • 0030979178 scopus 로고    scopus 로고
    • Folate deficiency causes uracil misincorporation into human DNA and chromosome breakage: Implications for cancer and neuronal damage
    • Blount, B.C. et al. Folate deficiency causes uracil misincorporation into human DNA and chromosome breakage: implications for cancer and neuronal damage. Fron. Natl. Acad. Sci. USA 94, 3290-3295 (1997).
    • (1997) Fron. Natl. Acad. Sci. USA , vol.94 , pp. 3290-3295
    • Blount, B.C.1
  • 31
    • 0030476385 scopus 로고    scopus 로고
    • Common mutation in methylenetetrahydrofolate reductase. Correlation with homocysteine metabolism and late-onset vascular disease
    • Deloughery, T.G. et al. Common mutation in methylenetetrahydrofolate reductase. Correlation with homocysteine metabolism and late-onset vascular disease. Circulation 94.3074-3078 (1996).
    • (1996) Circulation , vol.94 , pp. 3074-3078
    • Deloughery, T.G.1
  • 32
    • 0031058883 scopus 로고    scopus 로고
    • Phase determination from multiwavelength anomalous diffraction experiments
    • Hendrickson, W.A. & Ogata, C.M. Phase determination from multiwavelength anomalous diffraction experiments. Methods fnzymo/276, 494-522 (1997).
    • (1997) Methods Fnzymo , vol.276 , pp. 494-522
    • Hendrickson, W.A.1    Ogata, C.M.2
  • 33
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763(1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 36
    • 0028172551 scopus 로고
    • Protein hydration observed by X-ray diffraction. Solvation properties of penicillopepsin and neuraminidase crystal structures
    • Jiang, J.S. & Brunger, A.T. Protein hydration observed by X-ray diffraction. Solvation properties of penicillopepsin and neuraminidase crystal structures. J. Mol. Biol. 264, 100-115 (1994).
    • (1994) J. Mol. Biol. , vol.264 , pp. 100-115
    • Jiang, J.S.1    Brunger, A.T.2
  • 38
    • 0017667672 scopus 로고
    • Methylenetetrahydrofolate reductase in cultured human cells. I. Growth and metabolic studies
    • Rosenblatt, D.S. & Erbe, R.W. Methylenetetrahydrofolate reductase in cultured human cells. I. Growth and metabolic studies. Pediatr. Res. 11, 1137-1141 (1977).
    • (1977) Pediatr. Res. , vol.11 , pp. 1137-1141
    • Rosenblatt, D.S.1    Erbe, R.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.