메뉴 건너뛰기




Volumn 47, Issue 3, 2008, Pages 949-956

Function of MoaB proteins in the biosynthesis of the molybdenum and tungsten cofactors

Author keywords

[No Author keywords available]

Indexed keywords

EUKARYOTIC PROTEINS; SULFUR CYCLES; TRIMERS;

EID: 38349181719     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7020487     Document Type: Article
Times cited : (34)

References (38)
  • 1
    • 0000273676 scopus 로고    scopus 로고
    • The mononuclear molybdenum enzymes
    • Hille, R. (1996) The mononuclear molybdenum enzymes, Chem. Rev. 96, 2757-2816.
    • (1996) Chem. Rev , vol.96 , pp. 2757-2816
    • Hille, R.1
  • 2
    • 0029900624 scopus 로고    scopus 로고
    • Tungsten in biological systems
    • Kletzin, A., and Adams, M. W. (1996) Tungsten in biological systems, FEMS Microbiol. Rev. 18, 5-63.
    • (1996) FEMS Microbiol. Rev , vol.18 , pp. 5-63
    • Kletzin, A.1    Adams, M.W.2
  • 3
    • 0026669725 scopus 로고
    • The pterin molybdenum cofactors
    • Rajagopalan, K. V., and Johnson, J. L. (1992) The pterin molybdenum cofactors, J. Biol. Chem. 267, 10199-10202.
    • (1992) J. Biol. Chem , vol.267 , pp. 10199-10202
    • Rajagopalan, K.V.1    Johnson, J.L.2
  • 4
    • 28844475146 scopus 로고    scopus 로고
    • Molybdenum cofactor biosynthesis and deficiency
    • Schwarz, G. (2005) Molybdenum cofactor biosynthesis and deficiency, Cell. Mol. Life Sci. 62, 2792-2810.
    • (2005) Cell. Mol. Life Sci , vol.62 , pp. 2792-2810
    • Schwarz, G.1
  • 5
    • 0036629252 scopus 로고    scopus 로고
    • Molybdenum and tungsten in biology
    • Hille, R. (2002) Molybdenum and tungsten in biology, Trends Biochem. Sci. 27, 360-367.
    • (2002) Trends Biochem. Sci , vol.27 , pp. 360-367
    • Hille, R.1
  • 6
    • 9944248111 scopus 로고    scopus 로고
    • Molybdenum-containing hydroxylases
    • Hille, R. (2005) Molybdenum-containing hydroxylases, Arch. Biochem. Biophys. 433, 107-116.
    • (2005) Arch. Biochem. Biophys , vol.433 , pp. 107-116
    • Hille, R.1
  • 8
    • 0026321415 scopus 로고
    • The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase. Evidence for its participation in a unique glycolytic pathway
    • Mukund, S., and Adams, M. W. (1991) The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase. Evidence for its participation in a unique glycolytic pathway, J. Biol. Chem. 266, 14208-14216.
    • (1991) J. Biol. Chem , vol.266 , pp. 14208-14216
    • Mukund, S.1    Adams, M.W.2
  • 9
    • 0033028106 scopus 로고    scopus 로고
    • Purification and molecular characterization of the tungsten-containing formaldehyde ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus: The third of a putative five-member tungstoenzyme family
    • Roy, R., Mukund, S., Schut, G. J., Dunn, D. M., Weiss, R., and Adams, M. W. W. (1999) Purification and molecular characterization of the tungsten-containing formaldehyde ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus: the third of a putative five-member tungstoenzyme family, J. Bacteriol. 181, 1171-1180.
    • (1999) J. Bacteriol , vol.181 , pp. 1171-1180
    • Roy, R.1    Mukund, S.2    Schut, G.J.3    Dunn, D.M.4    Weiss, R.5    Adams, M.W.W.6
  • 10
    • 0028927080 scopus 로고
    • Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus
    • Mukund, S., and Adams, M. W. (1995) Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus, J. Biol. Chem. 270, 8389-8392.
    • (1995) J. Biol. Chem , vol.270 , pp. 8389-8392
    • Mukund, S.1    Adams, M.W.2
  • 11
    • 0036372919 scopus 로고    scopus 로고
    • Tungsten-dependent aldehyde oxidoreductase: A new family of enzymes containing the pterin cofactor
    • Roy, R., and Adams, M. W. W. (2002) Tungsten-dependent aldehyde oxidoreductase: A new family of enzymes containing the pterin cofactor, Met. Ions Biol. Syst. 39, 673-697.
    • (2002) Met. Ions Biol. Syst , vol.39 , pp. 673-697
    • Roy, R.1    Adams, M.W.W.2
  • 12
    • 26444453929 scopus 로고    scopus 로고
    • WOR5, a novel tungsten-containing aldehyde oxidoreductase from Pyrococcus furiosus with a broad substrate specificity
    • Bevers, L. E., Bol, E., Hagedoorn, P.-L., and Hagen, W. R. (2005) WOR5, a novel tungsten-containing aldehyde oxidoreductase from Pyrococcus furiosus with a broad substrate specificity, J. Bacteriol. 187, 7056-7061.
    • (2005) J. Bacteriol , vol.187 , pp. 7056-7061
    • Bevers, L.E.1    Bol, E.2    Hagedoorn, P.-L.3    Hagen, W.R.4
  • 13
    • 0030882324 scopus 로고    scopus 로고
    • Molybdenum cofactor biosynthesis. The plant protein Cnx1 binds molybdopterin with high affinity
    • Schwarz, G., Boxer, D. H., and Mendel, R. R. (1997) Molybdenum cofactor biosynthesis. The plant protein Cnx1 binds molybdopterin with high affinity, J. Biol. Chem. 272, 26811-26814.
    • (1997) J. Biol. Chem , vol.272 , pp. 26811-26814
    • Schwarz, G.1    Boxer, D.H.2    Mendel, R.R.3
  • 14
    • 4043114792 scopus 로고    scopus 로고
    • Structure of molybdopterin-bound Cnx1G domain links molybdenum and copper metabolism
    • Kuper, J., Llamas, A., Hecht, H. J., Mendel, R. R., and Schwarz, G. (2004) Structure of molybdopterin-bound Cnx1G domain links molybdenum and copper metabolism, Nature 430, 806-806.
    • (2004) Nature , vol.430 , pp. 806-806
    • Kuper, J.1    Llamas, A.2    Hecht, H.J.3    Mendel, R.R.4    Schwarz, G.5
  • 15
    • 11244333112 scopus 로고    scopus 로고
    • Synthesis of adenylated molybdopterin: An essential step for molybdenum insertion
    • Llamas, A., Mendel, R. R., and Schwarz, G. (2004) Synthesis of adenylated molybdopterin: an essential step for molybdenum insertion, J. Biol. Chem. 279, 55241-55246.
    • (2004) J. Biol. Chem , vol.279 , pp. 55241-55246
    • Llamas, A.1    Mendel, R.R.2    Schwarz, G.3
  • 16
    • 33745863101 scopus 로고    scopus 로고
    • The mechanism of nucleotide-assisted molybdenum insertion into molybdopterin. A novel route toward metal cofactor assembly
    • Llamas, A., Otte, T., Multhaup, G., Mendel, R. R., and Schwarz, G. (2006) The mechanism of nucleotide-assisted molybdenum insertion into molybdopterin. A novel route toward metal cofactor assembly, J. Biol. Chem. 281, 18343-18350.
    • (2006) J. Biol. Chem , vol.281 , pp. 18343-18350
    • Llamas, A.1    Otte, T.2    Multhaup, G.3    Mendel, R.R.4    Schwarz, G.5
  • 17
    • 0034612373 scopus 로고    scopus 로고
    • Mutations in the molybdenum cofactor biosynthetic protein Cnx1G from Arabidopsis thaliana define functions for molybdopterin bind, Mo-insertion and molybdenum cofactor stabilization
    • Kuper, J., Palmer, T., Mendel, R. R., and Schwarz, G. (2000) Mutations in the molybdenum cofactor biosynthetic protein Cnx1G from Arabidopsis thaliana define functions for molybdopterin bind, Mo-insertion and molybdenum cofactor stabilization, Proc. Natl. Acad. Sci. U.S.A. 97, 6475-6480.
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 6475-6480
    • Kuper, J.1    Palmer, T.2    Mendel, R.R.3    Schwarz, G.4
  • 18
    • 14844331741 scopus 로고    scopus 로고
    • In vitro molybdenum ligation to molybdopterin using purified components
    • Nichols, J. D., and Rajagopalan, K. V. (2005) In vitro molybdenum ligation to molybdopterin using purified components, J. Biol. Chem. 280, 7817-7822.
    • (2005) J. Biol. Chem , vol.280 , pp. 7817-7822
    • Nichols, J.D.1    Rajagopalan, K.V.2
  • 19
    • 0034490077 scopus 로고    scopus 로고
    • The molybdenum cofactor biosynthetic protein Cnx1 complements molybdate-repairable mutants, transfers molybdenum to the metal binding pterin, and is associated with the cytoskeleton
    • Schwarz, G., Schulze, J., Bittner, F., Eilers, T., Kuper, J., Bollmann, G., Nerlich, A., Brinkmann, H., and Mendel, R. R. (2000) The molybdenum cofactor biosynthetic protein Cnx1 complements molybdate-repairable mutants, transfers molybdenum to the metal binding pterin, and is associated with the cytoskeleton, Plant Cell 12, 2455-2472.
    • (2000) Plant Cell , vol.12 , pp. 2455-2472
    • Schwarz, G.1    Schulze, J.2    Bittner, F.3    Eilers, T.4    Kuper, J.5    Bollmann, G.6    Nerlich, A.7    Brinkmann, H.8    Mendel, R.R.9
  • 20
    • 0034704126 scopus 로고    scopus 로고
    • Mechanism of assembly of the bis(molybdopterin guanine dinucleotide)molybdenum cofactor in Rhodobacter sphaeroides dimethyl sulfoxide reductase
    • Temple, C. A., and Rajagopalan, K. V. (2000) Mechanism of assembly of the bis(molybdopterin guanine dinucleotide)molybdenum cofactor in Rhodobacter sphaeroides dimethyl sulfoxide reductase, J. Biol. Chem. 275, 40202-40210.
    • (2000) J. Biol. Chem , vol.275 , pp. 40202-40210
    • Temple, C.A.1    Rajagopalan, K.V.2
  • 21
    • 33644872480 scopus 로고    scopus 로고
    • NarJ chaperone binds on two distinct sites of the aponitrate reductase of Escherichia coli to coordinate molybdenum cofactor insertion and assembly
    • Vergnes, A., Pommier, J., Toci, R., Blasco, F., Giordano, G., and Magalon, A. (2006) NarJ chaperone binds on two distinct sites of the aponitrate reductase of Escherichia coli to coordinate molybdenum cofactor insertion and assembly, J. Biol. Chem. 281, 2170-2176.
    • (2006) J. Biol. Chem , vol.281 , pp. 2170-2176
    • Vergnes, A.1    Pommier, J.2    Toci, R.3    Blasco, F.4    Giordano, G.5    Magalon, A.6
  • 22
    • 0032933144 scopus 로고    scopus 로고
    • Enzymatic and physiological properties of the tungsten-substituted molybdenum TMAO reductase from Escherichia coli
    • Buc, J., Santini, C. L., Giordani, R., Czjzek, M., Wu, L. F., and Giordano, G. (1999) Enzymatic and physiological properties of the tungsten-substituted molybdenum TMAO reductase from Escherichia coli, Mol. Microbiol. 32, 159-168.
    • (1999) Mol. Microbiol , vol.32 , pp. 159-168
    • Buc, J.1    Santini, C.L.2    Giordani, R.3    Czjzek, M.4    Wu, L.F.5    Giordano, G.6
  • 23
    • 33748777679 scopus 로고    scopus 로고
    • Tungsten transport protein A (WtpA) in Pyrococcus furiosus: The first member of a new class of tungstate and molybdate transporters
    • Bevers, L. E., Hagedoorn, P. L., Krijger, G. C., and Hagen, W. R. (2006) Tungsten transport protein A (WtpA) in Pyrococcus furiosus: the first member of a new class of tungstate and molybdate transporters, J. Bacteriol. 188, 6498-6505.
    • (2006) J. Bacteriol , vol.188 , pp. 6498-6505
    • Bevers, L.E.1    Hagedoorn, P.L.2    Krijger, G.C.3    Hagen, W.R.4
  • 24
    • 0022445886 scopus 로고
    • Pyrococcus furiosus sp. nov. represents a novel genus of marine heterotrophic archaebacteria growing optimally at 100 DegC
    • Fiala, G., and Stetter, K. O. (1986) Pyrococcus furiosus sp. nov. represents a novel genus of marine heterotrophic archaebacteria growing optimally at 100 DegC, Arch. Microbiol. 145, 56-61.
    • (1986) Arch. Microbiol , vol.145 , pp. 56-61
    • Fiala, G.1    Stetter, K.O.2
  • 25
    • 0020429524 scopus 로고
    • Nitrate reductase in Escherichia coli K-12: Involvement of chlC, chlE, and chlG loci
    • Stewart, V., and MacGregor, C. H. (1982) Nitrate reductase in Escherichia coli K-12: involvement of chlC, chlE, and chlG loci, J. Bacteriol. 151, 788-799.
    • (1982) J. Bacteriol , vol.151 , pp. 788-799
    • Stewart, V.1    MacGregor, C.H.2
  • 26
    • 0017616853 scopus 로고
    • Sites and specificity of the reaction of bipyridylium compounds with anaerobic respiratory enzymes of Escherichia coli. Effects of permeability barriers imposed by the cytoplasmic membrane
    • Jones, R. W., and Garland, P. B. (1977) Sites and specificity of the reaction of bipyridylium compounds with anaerobic respiratory enzymes of Escherichia coli. Effects of permeability barriers imposed by the cytoplasmic membrane, Biochem. J. 164, 199-211.
    • (1977) Biochem. J , vol.164 , pp. 199-211
    • Jones, R.W.1    Garland, P.B.2
  • 27
    • 1942501738 scopus 로고    scopus 로고
    • The tetrahydropyranopterin structure of the sulfur-free and metal-free molybdenum cofactor precursor
    • Santamaria-Araujo, J. A., Fischer, B., Otte, T., Nimtz, M., Mendel, R. R., Wray, V., and Schwarz, G. (2004) The tetrahydropyranopterin structure of the sulfur-free and metal-free molybdenum cofactor precursor, J. Biol. Chem. 279, 15994-15999.
    • (2004) J. Biol. Chem , vol.279 , pp. 15994-15999
    • Santamaria-Araujo, J.A.1    Fischer, B.2    Otte, T.3    Nimtz, M.4    Mendel, R.R.5    Wray, V.6    Schwarz, G.7
  • 28
    • 0035965266 scopus 로고    scopus 로고
    • Thiocarboxylation of molybdopterin synthase provides evidence for the mechanism of dithiolene formation in metal-binding pterins
    • Gutzke, G., Fischer, B., Mendel, R. R., and Schwarz, G. (2001) Thiocarboxylation of molybdopterin synthase provides evidence for the mechanism of dithiolene formation in metal-binding pterins, J. Biol. Chem. 276, 36268-36274.
    • (2001) J. Biol. Chem , vol.276 , pp. 36268-36274
    • Gutzke, G.1    Fischer, B.2    Mendel, R.R.3    Schwarz, G.4
  • 29
    • 0034695475 scopus 로고    scopus 로고
    • Crystal structure of the gephyrin-related molybdenum cofactor biosynthesis protein MogA from Escherichia coli
    • Liu, M. T., Wuebbens, M. M., Rajagopalan, K. V., and Schindelin, H. (2000) Crystal structure of the gephyrin-related molybdenum cofactor biosynthesis protein MogA from Escherichia coli, J. Biol. Chem. 275, 1814-1822.
    • (2000) J. Biol. Chem , vol.275 , pp. 1814-1822
    • Liu, M.T.1    Wuebbens, M.M.2    Rajagopalan, K.V.3    Schindelin, H.4
  • 30
    • 4744347062 scopus 로고    scopus 로고
    • The crystal structure of Escherichia coli MoaB suggests a probable role in molybdenum cofactor synthesis
    • Sanishvili, R., Beasley, S., Skarina, T., Glesne, D., Joachimiak, A., Edwards, A., and Savchenko, A. (2004) The crystal structure of Escherichia coli MoaB suggests a probable role in molybdenum cofactor synthesis, J. Biol. Chem. 279, 42139-42146.
    • (2004) J. Biol. Chem , vol.279 , pp. 42139-42146
    • Sanishvili, R.1    Beasley, S.2    Skarina, T.3    Glesne, D.4    Joachimiak, A.5    Edwards, A.6    Savchenko, A.7
  • 32
    • 0035078573 scopus 로고    scopus 로고
    • Structural basis for the ADP-specificity of a novel glucokinase from a hyperthermophilic archaeon
    • Ito, S., Fushinobu, S., Yoshioka, I., Koga, S., Matsuzawa, H., and Wakagi, T. (2001) Structural basis for the ADP-specificity of a novel glucokinase from a hyperthermophilic archaeon, Structure 9, 205-214.
    • (2001) Structure , vol.9 , pp. 205-214
    • Ito, S.1    Fushinobu, S.2    Yoshioka, I.3    Koga, S.4    Matsuzawa, H.5    Wakagi, T.6
  • 33
  • 34
    • 33947154878 scopus 로고    scopus 로고
    • Structure of an ABC transporter in complex with its binding protein
    • Hollenstein, K., Frei, D. C., and Locher, K. P. (2007) Structure of an ABC transporter in complex with its binding protein, Nature 446, 213-216.
    • (2007) Nature , vol.446 , pp. 213-216
    • Hollenstein, K.1    Frei, D.C.2    Locher, K.P.3
  • 35
    • 0029394803 scopus 로고
    • Molybdenum co-factor biosynthesis: The Arabidopsis thaliana cDNA cnx1 encodes a multifunctional two-domain protein homologous to a mammalian neuroprotein, the insect protein cinnamon and three Escherichia coli proteins
    • Stallmeyer, B., Nerlich, A., Schiemann, J., Brinkmann, H., and Mendel, R. R. (1995) Molybdenum co-factor biosynthesis: the Arabidopsis thaliana cDNA cnx1 encodes a multifunctional two-domain protein homologous to a mammalian neuroprotein, the insect protein cinnamon and three Escherichia coli proteins, Plant J. 8, 751-762.
    • (1995) Plant J , vol.8 , pp. 751-762
    • Stallmeyer, B.1    Nerlich, A.2    Schiemann, J.3    Brinkmann, H.4    Mendel, R.R.5
  • 36
    • 0034460301 scopus 로고    scopus 로고
    • ModE-dependent molybdate regulation of the molybdenum cofactor operon moa in Escherichia coli
    • Anderson, L. A., McNairn, E., Lubke, T., Pau, R. N., and Boxer, D. H. (2000) ModE-dependent molybdate regulation of the molybdenum cofactor operon moa in Escherichia coli, J. Bacteriol. 182, 7035-7043.
    • (2000) J. Bacteriol , vol.182 , pp. 7035-7043
    • Anderson, L.A.1    McNairn, E.2    Lubke, T.3    Pau, R.N.4    Boxer, D.H.5
  • 38
    • 0035860322 scopus 로고    scopus 로고
    • Crystal structures of human gephyrin and plant Cnx1 G domains: Comparative analysis and functional implications
    • Schwarz, G., Schrader, N., Mendel, R. R., Hecht, H. J., and Schindelin, H. (2001) Crystal structures of human gephyrin and plant Cnx1 G domains: comparative analysis and functional implications, J. Mol. Biol. 312, 405-418.
    • (2001) J. Mol. Biol , vol.312 , pp. 405-418
    • Schwarz, G.1    Schrader, N.2    Mendel, R.R.3    Hecht, H.J.4    Schindelin, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.