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Volumn 46, Issue 3, 2006, Pages 426-435

Evidence for folate-salvage reactions in plants

Author keywords

Arabidopsis; Folate salvage; p aminobenzoylglutamate; Pea; Pterins; Tomato

Indexed keywords

MICROORGANISMS; OXIDATION; SYNTHESIS (CHEMICAL); TISSUE;

EID: 33645655501     PISSN: 09607412     EISSN: 1365313X     Source Type: Journal    
DOI: 10.1111/j.1365-313X.2006.02685.x     Document Type: Article
Times cited : (45)

References (49)
  • 2
    • 0027996240 scopus 로고
    • PTR1: A reductase mediating salvage of oxidized pteridines and methotrexate resistance in the protozoan parasite Leishmania major
    • Bello A.R. Nare B. Freedman D. Hardy L. Beverley S.M. 1994 PTR1: a reductase mediating salvage of oxidized pteridines and methotrexate resistance in the protozoan parasite Leishmania major Proc. Natl Acad. Sci. USA 91 11442 11446
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 11442-11446
    • Bello, A.R.1    Nare, B.2    Freedman, D.3    Hardy, L.4    Beverley, S.M.5
  • 3
    • 0010255637 scopus 로고
    • Chemical and physical properties of pterins and folate derivatives
    • In. Wiley New York pp
    • Blakley R.L. ed. 1969 Chemical and physical properties of pterins and folate derivatives In The Biochemistry of Folic Acid and Related Pteridines New York Wiley pp 58 105
    • (1969) The Biochemistry of Folic Acid and Related Pteridines , pp. 58-105
    • Blakley, R.L.1    Ed2
  • 4
    • 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. 1976 A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0000486275 scopus 로고
    • The biosynthesis of folic acid. I. Substrate and cofactor requirements for enzymatic synthesis by cell-free extracts of Escherichia coli
    • Brown G.M. Weisman R.A. Molnar D.A. 1961 The biosynthesis of folic acid. I. Substrate and cofactor requirements for enzymatic synthesis by cell-free extracts of Escherichia coli J. Biol. Chem. 236 2534 2543
    • (1961) J. Biol. Chem. , vol.236 , pp. 2534-2543
    • Brown, G.M.1    Weisman, R.A.2    Molnar, D.A.3
  • 6
    • 0348042100 scopus 로고    scopus 로고
    • The intracellular distribution of folate derivatives in pea leaves
    • Chan S.Y. Cossins E.A. 2003 The intracellular distribution of folate derivatives in pea leaves Pteridines 14 67 76
    • (2003) Pteridines , vol.14 , pp. 67-76
    • Chan, S.Y.1    Cossins, E.A.2
  • 7
    • 0033841497 scopus 로고    scopus 로고
    • The fascinating world of folate and one-carbon metabolism
    • Cossins E.A. 2000 The fascinating world of folate and one-carbon metabolism Can. J. Bot. 78 691 708
    • (2000) Can. J. Bot. , vol.78 , pp. 691-708
    • Cossins, E.A.1
  • 9
    • 0015860653 scopus 로고
    • The enzymic synthesis of dihydropteroate and dihydrofolate by Plasmodium berghei
    • Ferone R. 1973 The enzymic synthesis of dihydropteroate and dihydrofolate by Plasmodium berghei J. Protozool. 20 459 464
    • (1973) J. Protozool. , vol.20 , pp. 459-464
    • Ferone, R.1
  • 11
    • 0029749371 scopus 로고    scopus 로고
    • Effects of epidermal cell shape and pigmentation on optical properties of antirrhinum petals at visible and ultraviolet wavelengths
    • Gorton H.L. Vogelmann T.C. 1996 Effects of epidermal cell shape and pigmentation on optical properties of antirrhinum petals at visible and ultraviolet wavelengths Plant Physiol. 112 879 888
    • (1996) Plant Physiol. , vol.112 , pp. 879-888
    • Gorton, H.L.1    Vogelmann, T.C.2
  • 13
  • 14
    • 0024815959 scopus 로고
    • Chemical and nutritional aspects of folate research: Analytical procedures, methods of folate synthesis, stability, and bioavailability of dietary folates
    • Gregory J.F. III. 1989 Chemical and nutritional aspects of folate research: analytical procedures, methods of folate synthesis, stability, and bioavailability of dietary folates Adv. Food Nutr. Res. 33 1 101
    • (1989) Adv. Food Nutr. Res. , vol.33 , pp. 1-101
    • Gregory Iii., J.F.1
  • 16
    • 0014151463 scopus 로고
    • Effect of substrate decomposition on the spectrophotometric assay of dihydrofolate reductase
    • Hillcoat B.L. Nixon P.F. Blakley R.L. 1967 Effect of substrate decomposition on the spectrophotometric assay of dihydrofolate reductase Anal. Biochem. 21 178 189
    • (1967) Anal. Biochem. , vol.21 , pp. 178-189
    • Hillcoat, B.L.1    Nixon, P.F.2    Blakley, R.L.3
  • 17
    • 0031725643 scopus 로고    scopus 로고
    • Characterization of mutations that allow p-aminobenzoyl-glutamate utilization by Escherichia coli
    • Hussein M.J. Green J.M. Nichols B.P. 1998 Characterization of mutations that allow p-aminobenzoyl-glutamate utilization by Escherichia coli J. Bacteriol. 180 6260 6268
    • (1998) J. Bacteriol. , vol.180 , pp. 6260-6268
    • Hussein, M.J.1    Green, J.M.2    Nichols, B.P.3
  • 18
    • 0000787618 scopus 로고
    • Folylpolyglutamyl derivatives of Pisum sativum L. Determination of polyglutamate chain lengths by high performance liquid chromatography following conversion to p-aminobenzoylpolyglutamates
    • Imeson H.C. Zheng L.L. Cossins E.A. 1990 Folylpolyglutamyl derivatives of Pisum sativum L. Determination of polyglutamate chain lengths by high performance liquid chromatography following conversion to p- aminobenzoylpolyglutamates Plant Cell Physiol. 31 223 231
    • (1990) Plant Cell Physiol. , vol.31 , pp. 223-231
    • Imeson, H.C.1    Zheng, L.L.2    Cossins, E.A.3
  • 19
    • 0000801638 scopus 로고
    • Photolytic and enzymatic transformations of pteroylglutamic acid
    • Lowry O.H. Bessey O.A. Crawford E.J. 1949 Photolytic and enzymatic transformations of pteroylglutamic acid J. Biol. Chem. 180 389 398
    • (1949) J. Biol. Chem. , vol.180 , pp. 389-398
    • Lowry, O.H.1    Bessey, O.A.2    Crawford, E.J.3
  • 21
    • 0026496458 scopus 로고
    • The quantitative analysis of endogenous folate catabolites in human urine
    • McPartlin J. Courtney G. McNulty H. Weir D. Scott J. 1992 The quantitative analysis of endogenous folate catabolites in human urine Anal. Biochem. 206 256 261
    • (1992) Anal. Biochem. , vol.206 , pp. 256-261
    • McPartlin, J.1    Courtney, G.2    McNulty, H.3    Weir, D.4    Scott, J.5
  • 22
    • 0015217295 scopus 로고
    • Enzymatic conversion of 2-amino-4-hydroxy-6-formyl-7,8-dihydropteridine to 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine by cell-free extracts of Escherichia coli B
    • Mitsuda H. Suzuki Y. 1971 Enzymatic conversion of 2-amino-4-hydroxy-6- formyl-7,8-dihydropteridine to 2-amino-4-hydroxy-6-hydroxymethyl-7,8- dihydropteridine by cell-free extracts of Escherichia coli B J. Vitaminol. 17 5 9
    • (1971) J. Vitaminol. , vol.17 , pp. 5-9
    • Mitsuda, H.1    Suzuki, Y.2
  • 23
    • 0037090805 scopus 로고    scopus 로고
    • Folate synthesis in higher-plant mitochondria: Coupling between the dihydropterin pyrophosphokinase and the dihydropteroate synthase activities
    • Mouillon J.M. Ravanel S. Douce R. Rébeillé F. 2002 Folate synthesis in higher-plant mitochondria: coupling between the dihydropterin pyrophosphokinase and the dihydropteroate synthase activities Biochem. J. 363 313 319
    • (2002) Biochem. J. , vol.363 , pp. 313-319
    • Mouillon, J.M.1    Ravanel, S.2    Douce, R.3    Rébeillé, F.4
  • 24
    • 0030946111 scopus 로고    scopus 로고
    • The roles of pteridine reductase 1 and dihydrofolate reductase- thymidylate synthase in pteridine metabolism in the protozoan parasite Leishmania major
    • Nare B. Hardy L.W. Beverley S.M. 1997 The roles of pteridine reductase 1 and dihydrofolate reductase-thymidylate synthase in pteridine metabolism in the protozoan parasite Leishmania major J. Biol. Chem. 272 13883 13891
    • (1997) J. Biol. Chem. , vol.272 , pp. 13883-13891
    • Nare, B.1    Hardy, L.W.2    Beverley, S.M.3
  • 27
    • 0014955610 scopus 로고
    • Dihydrofolate and dihydropteroate synthesis by partially purified enzymes from wild-type and sulfonamide-resistant Pneumonococcus
    • Ortiz P.J. 1970 Dihydrofolate and dihydropteroate synthesis by partially purified enzymes from wild-type and sulfonamide-resistant Pneumonococcus Biochemistry 9 355 361
    • (1970) Biochemistry , vol.9 , pp. 355-361
    • Ortiz, P.J.1
  • 28
    • 0002556548 scopus 로고
    • Chemistry of naturally occurring pteridines
    • In. Vol. 2*Blakley R.L.*Benkovic S. eds. Wiley New York pp
    • Pfleiderer W. 1985 Chemistry of naturally occurring pteridines In Folates and Pterins Vol. 2 Blakley R.L. Benkovic S. eds New York Wiley pp 43 114
    • (1985) Folates and Pterins , pp. 43-114
    • Pfleiderer, W.1
  • 29
    • 0029659032 scopus 로고    scopus 로고
    • 13C Nuclear magnetic resonance detection of interactions of serine hydroxymethyltransferase with C1-tetrahydrofolate synthase and glycine decarboxylase complex activities in Arabidopsis
    • 13C Nuclear magnetic resonance detection of interactions of serine hydroxymethyltransferase with C1-tetrahydrofolate synthase and glycine decarboxylase complex activities in Arabidopsis Plant Physiol. 112 207 216
    • (1996) Plant Physiol. , vol.112 , pp. 207-216
    • Prabhu, V.1    Chatson, K.B.2    Abrams, G.D.3    King, J.4
  • 30
    • 3643128069 scopus 로고    scopus 로고
    • 13C fluxes through the glycine decarboxylase/serine hydroxymethyltransferase enzyme system in Arabidopsis
    • 13C fluxes through the glycine decarboxylase/serine hydroxymethyltransferase enzyme system in Arabidopsis Plant Physiol. 116 137 144
    • (1998) Plant Physiol. , vol.116 , pp. 137-144
    • Prabhu, V.1    Chatson, K.B.2    Lui, H.3    Abrams, G.D.4    King, J.5
  • 31
    • 0037743470 scopus 로고    scopus 로고
    • The folate precursor p-aminobenzoate is reversibly converted to its glucose ester in the plant cytosol
    • Quinlivan E.P. Roje S. Basset G. Shachar-Hill Y. Gregory J.F. III. Hanson A.D. 2003 The folate precursor p-aminobenzoate is reversibly converted to its glucose ester in the plant cytosol J. Biol. Chem. 278 20731 20737
    • (2003) J. Biol. Chem. , vol.278 , pp. 20731-20737
    • Quinlivan, E.P.1    Roje, S.2    Basset, G.3    Shachar-Hill, Y.4    Gregory Iii., J.F.5    Hanson, A.D.6
  • 32
    • 0037733208 scopus 로고    scopus 로고
    • Folate biosynthesis in higher plants: Purification and molecular cloning of a bifunctional 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase/7,8- dihydropteroate synthase localized in mitochondria
    • Rébeillé F. Macherel D. Mouillon J.M. Garin J. Douce R. 1997 Folate biosynthesis in higher plants: purification and molecular cloning of a bifunctional 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase/7,8- dihydropteroate synthase localized in mitochondria EMBO J. 16 947 957
    • (1997) EMBO J. , vol.16 , pp. 947-957
    • Rébeillé, F.1    MacHerel, D.2    Mouillon, J.M.3    Garin, J.4    Douce, R.5
  • 33
    • 0001234239 scopus 로고
    • Oxidation of tetrahydrofolic acid by air
    • Reed L.S. Archer M.C. 1980 Oxidation of tetrahydrofolic acid by air J. Agric. Food Chem. 28 801 805
    • (1980) J. Agric. Food Chem. , vol.28 , pp. 801-805
    • Reed, L.S.1    Archer, M.C.2
  • 34
    • 0039904323 scopus 로고
    • Catabolism of pterins
    • In. Vol. 2*Blakley R.L.*Benkovic S.J. eds. Wiley New York pp
    • Rembold H. 1985 Catabolism of pterins In Folates and Pterins Vol. 2 Blakley R.L. Benkovic S.J. eds New York Wiley pp 155 178
    • (1985) Folates and Pterins , pp. 155-178
    • Rembold, H.1
  • 35
    • 0007468148 scopus 로고
    • Catabolism of folates
    • In. Vol. 1*Blakley R.L.*Benkovic S.J. eds. Wiley New York pp
    • Scott J.M. 1984 Catabolism of folates In Folates and Pterins Vol. 1 Blakley R.L. Benkovic S.J. eds New York Wiley pp 307 327
    • (1984) Folates and Pterins , pp. 307-327
    • Scott, J.M.1
  • 36
    • 0342700245 scopus 로고    scopus 로고
    • Folic acid and folates: The feasibility of nutritional enhancement in plant foods
    • Scott J. Rébeillé F. Fletcher J. 2000 Folic acid and folates: the feasibility of nutritional enhancement in plant foods J. Sci. Food Agric. 80 795 824
    • (2000) J. Sci. Food Agric. , vol.80 , pp. 795-824
    • Scott, J.1    Rébeillé, F.2    Fletcher, J.3
  • 37
    • 0018845614 scopus 로고
    • Methods for reduction, stabilization, and analyses of folates
    • Scrimgeour K.G. 1980 Methods for reduction, stabilization, and analyses of folates Methods Enzymol. 66 517 523
    • (1980) Methods Enzymol. , vol.66 , pp. 517-523
    • Scrimgeour, K.G.1
  • 38
    • 0021871027 scopus 로고
    • Purification and properties of carboxypeptidase G2 from Pseudomonas sp. strain RS-16. Use of a novel triazine dye affinity method
    • Sherwood R.F. Melton R.G. Alwan S.M. Hughes P. 1985 Purification and properties of carboxypeptidase G2 from Pseudomonas sp. strain RS-16. Use of a novel triazine dye affinity method Eur. J. Biochem. 148 447 453
    • (1985) Eur. J. Biochem. , vol.148 , pp. 447-453
    • Sherwood, R.F.1    Melton, R.G.2    Alwan, S.M.3    Hughes, P.4
  • 39
    • 12644307227 scopus 로고
    • Enzymic synthesis of folic acid-like compounds by cell-free extracts of Lactobacillus arabinosus
    • Shiota T. 1959 Enzymic synthesis of folic acid-like compounds by cell-free extracts of Lactobacillus arabinosus Arch. Biochem. Biophys. 80 155 161
    • (1959) Arch. Biochem. Biophys. , vol.80 , pp. 155-161
    • Shiota, T.1
  • 40
    • 0014640227 scopus 로고
    • The enzymatic synthesis of hydroxylmethyldihydropteridine pyrophosphate and dihydrofolate
    • Shiota T. Baugh C.M. Jackson R. Dillard R. 1969 The enzymatic synthesis of hydroxylmethyldihydropteridine pyrophosphate and dihydrofolate Biochemistry 8 5022 5028
    • (1969) Biochemistry , vol.8 , pp. 5022-5028
    • Shiota, T.1    Baugh, C.M.2    Jackson, R.3    Dillard, R.4
  • 41
    • 11144226809 scopus 로고    scopus 로고
    • The tomato carotenoid cleavage dioxygenase 1 genes contribute to the formation of the flavor volatiles beta-ionone, pseudoionone, and geranylacetone
    • Simkin A.J. Schwartz S.H. Auldridge M. Taylor M.G. Klee H.J. 2004 The tomato carotenoid cleavage dioxygenase 1 genes contribute to the formation of the flavor volatiles beta-ionone, pseudoionone, and geranylacetone Plant J. 40 882 892
    • (2004) Plant J. , vol.40 , pp. 882-892
    • Simkin, A.J.1    Schwartz, S.H.2    Auldridge, M.3    Taylor, M.G.4    Klee, H.J.5
  • 42
    • 85044699503 scopus 로고    scopus 로고
    • Effect of ultraviolet C irradiation on folate and free amino acid contents in leaves of Pisum sativum
    • Stakhov L.F. Ladygin V.G. Stakhova L.N. 2002 Effect of ultraviolet C irradiation on folate and free amino acid contents in leaves of Pisum sativum Biofizika 47 878 885
    • (2002) Biofizika , vol.47 , pp. 878-885
    • Stakhov, L.F.1    Ladygin, V.G.2    Stakhova, L.N.3
  • 43
    • 0018886130 scopus 로고
    • Quantitative determination of pterins in biological fluids by high-performance liquid chromatography
    • Stea B. Halpern R.M. Halpern B.C. Smith R.A. 1980 Quantitative determination of pterins in biological fluids by high-performance liquid chromatography J. Chromatogr. 188 363 375
    • (1980) J. Chromatogr. , vol.188 , pp. 363-375
    • Stea, B.1    Halpern, R.M.2    Halpern, B.C.3    Smith, R.A.4
  • 44
    • 0037227938 scopus 로고    scopus 로고
    • Folate content in strawberries (Fragaria × ananassa): Effects of cultivar, ripeness, year of harvest, storage, and commercial processing
    • Strålsjö L.M. Witthöft C.M. Sjöholm I.M. Jägerstad M.I. 2003 Folate content in strawberries (Fragaria × ananassa): effects of cultivar, ripeness, year of harvest, storage, and commercial processing J. Agric. Food Chem. 51 128 133
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 128-133
    • Strålsjö, L.M.1    Witthöft, C.M.2    Sjöholm, I.M.3    Jägerstad, M.I.4
  • 46
    • 0018341925 scopus 로고
    • Characterization of mutationally altered dihydropteroate synthase and its ability to form a sulfonamide-containing dihydrofolate analog
    • Swedberg G. Castensson S. Sköld O. 1979 Characterization of mutationally altered dihydropteroate synthase and its ability to form a sulfonamide-containing dihydrofolate analog J. Bacteriol. 137 129 136
    • (1979) J. Bacteriol. , vol.137 , pp. 129-136
    • Swedberg, G.1    Castensson, S.2    Sköld, O.3
  • 47
    • 0014409778 scopus 로고
    • Synthesis of 2-amino-4-hydroxy-6-formyl-7,8-dihydropteridine and its identification as a degradation product of dihydrofolate
    • Whiteley J.M. Drais J. Kirchner J. Huennekens F.M. 1968 Synthesis of 2-amino-4-hydroxy-6-formyl-7,8-dihydropteridine and its identification as a degradation product of dihydrofolate Arch. Biochem. Biophys. 126 955 957
    • (1968) Arch. Biochem. Biophys. , vol.126 , pp. 955-957
    • Whiteley, J.M.1    Drais, J.2    Kirchner, J.3    Huennekens, F.M.4
  • 48
    • 0027976083 scopus 로고
    • Subcellular volumes and metabolite concentrations in spinach leaves
    • Winter H. Robinson D.G. Heldt H.W. 1994 Subcellular volumes and metabolite concentrations in spinach leaves Planta 193 530 535
    • (1994) Planta , vol.193 , pp. 530-535
    • Winter, H.1    Robinson, D.G.2    Heldt, H.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.