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Volumn 272, Issue 6, 2005, Pages 1465-1477

Functional analysis of the methylmalonyl-CoA epimerase from Caenorhabditis elegans

Author keywords

Caenorhabditis elegans; Epimerase; Methylmalonyl CoA

Indexed keywords

AMINO ACID; COENZYME A; FATTY ACID; GREEN FLUORESCENT PROTEIN; LIGAND; METAL; METHYLMALONYL COENZYME A EPIMERASE; PROPIONYL COENZYME A; SUCCINYL COENZYME A; UNCLASSIFIED DRUG;

EID: 20144387333     PISSN: 1742464X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2005.04579.x     Document Type: Article
Times cited : (22)

References (48)
  • 1
    • 0034649338 scopus 로고    scopus 로고
    • Mechanistic diversity in a metalloenzyme superfamily
    • Armstrong RN (2000) Mechanistic diversity in a metalloenzyme superfamily. Biochemistry 39, 13625-13632.
    • (2000) Biochemistry , vol.39 , pp. 13625-13632
    • Armstrong, R.N.1
  • 2
    • 0030667789 scopus 로고    scopus 로고
    • Understanding enzyme superfamilies
    • Babbitt PC & Gerlt JA (1997) Understanding enzyme superfamilies. J Biol Chem 272, 30591-30594.
    • (1997) J Biol Chem , vol.272 , pp. 30591-30594
    • Babbitt, P.C.1    Gerlt, J.A.2
  • 3
    • 0034923923 scopus 로고    scopus 로고
    • Divergent evolution of enzymatic function: Mechanistically diverse superfamilies and functionally distinct superfamilies
    • Gerlt JA & Babbitt PC (2001) Divergent Evolution of enzymatic function: Mechanistically diverse superfamilies and functionally distinct superfamilies. Annu Rev Biochem 70, 209-246.
    • (2001) Annu Rev Biochem , vol.70 , pp. 209-246
    • Gerlt, J.A.1    Babbitt, P.C.2
  • 4
    • 0001362219 scopus 로고
    • Disorders of propionate and methylmalonate metabolism
    • (Scriver CR, Beaudet AL, Sly WS & Valle D, eds). McGraw-Hill, New York
    • Fenton WA & Rosenberg LE (1995) Disorders of propionate and methylmalonate metabolism. In The Metabolic and Molecular Bases of Inherited Disease, Vol. 2. (Scriver CR, Beaudet AL, Sly WS & Valle D, eds), pp. 1423-1449. McGraw-Hill, New York.
    • (1995) The Metabolic and Molecular Bases of Inherited Disease , vol.2 , pp. 1423-1449
    • Fenton, W.A.1    Rosenberg, L.E.2
  • 7
    • 0035813109 scopus 로고    scopus 로고
    • Identification of the human methylmalonyl-CoA racemase gene based on the analysis of prokaryotic gene arrangements: Implications for decoding the human genome
    • Bobik TA & Rasche ME (2001) Identification of the human methylmalonyl-CoA racemase gene based on the analysis of prokaryotic gene arrangements: implications for decoding the human genome. J Biol Chem 276, 37194-37198.
    • (2001) J Biol Chem , vol.276 , pp. 37194-37198
    • Bobik, T.A.1    Rasche, M.E.2
  • 8
    • 0037161282 scopus 로고    scopus 로고
    • Metabolic engineering of a methylmalonyl-CoA mutase-epimerase pathway for complex polyketide biosynthesis in Escherichia coli
    • Dayem LC, Carney JR, Santi DV, Pfeifer BA, Khosla C & Kealey JT (2002) Metabolic engineering of a methylmalonyl-CoA mutase-epimerase pathway for complex polyketide biosynthesis in Escherichia coli. Biochemistry 41, 5193-5201.
    • (2002) Biochemistry , vol.41 , pp. 5193-5201
    • Dayem, L.C.1    Carney, J.R.2    Santi, D.V.3    Pfeifer, B.A.4    Khosla, C.5    Kealey, J.T.6
  • 9
    • 0036838170 scopus 로고    scopus 로고
    • L-Malyl-coenzyme A lyase/beta-methylmalyl-coenzyme A lyase from Chloroflexus aurantiacus, a bifunctional enzyme involved in autotrophic CO(2) fixation
    • Herter S, Busch A & Fuchs G (2002) L-Malyl-coenzyme A lyase/beta-methylmalyl-coenzyme A lyase from Chloroflexus aurantiacus, a bifunctional enzyme involved in autotrophic CO(2) fixation. J Bacteriol 184, 5999-6006.
    • (2002) J Bacteriol , vol.184 , pp. 5999-6006
    • Herter, S.1    Busch, A.2    Fuchs, G.3
  • 10
    • 0036191839 scopus 로고    scopus 로고
    • Glyoxylate regeneration pathway in the methylotroph Methylobacterium extorquens AM1
    • Korotkova N, Chistoserdova L, Kuksa K & Lidstrom ME (2002) Glyoxylate regeneration pathway in the methylotroph Methylobacterium extorquens AM1. J Bacteriol 184, 1750-1758.
    • (2002) J Bacteriol , vol.184 , pp. 1750-1758
    • Korotkova, N.1    Chistoserdova, L.2    Kuksa, K.3    Lidstrom, M.E.4
  • 11
    • 0035102454 scopus 로고    scopus 로고
    • Biosynthesis of polyketides in heterologous hosts
    • Pfeifer BA & Khosla C (2001) Biosynthesis of polyketides in heterologous hosts. Microbiol Mol Biol Rev 65, 106-118.
    • (2001) Microbiol Mol Biol Rev , vol.65 , pp. 106-118
    • Pfeifer, B.A.1    Khosla, C.2
  • 12
    • 0041691117 scopus 로고    scopus 로고
    • Engineered biosynthesis of an ansamycin polyketide precursor in Escherichia coli
    • Watanabe K, Rude MA, Walsh CT & Khosla C (2003) Engineered biosynthesis of an ansamycin polyketide precursor in Escherichia coli. Proc Natl Acad Sci USA 100, 9774-9778.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 9774-9778
    • Watanabe, K.1    Rude, M.A.2    Walsh, C.T.3    Khosla, C.4
  • 17
    • 15944376951 scopus 로고    scopus 로고
    • Institut für Humangenetik, Technische Universität, München and Institut für Humangenetik GSF, Forschungszentrum für Gesundheit und Umwelt, Neuherberg
    • Claros MG & Vincens P (1996) MITOPROT: Prediction of mitochondrial targeting sequences. Institut für Humangenetik, Technische Universität, München and Institut für Humangenetik GSF, Forschungszentrum für Gesundheit und Umwelt, Neuherberg, http://ihg.gsf.de/ihg/mitoprot.html.
    • (1996) MITOPROT: Prediction of Mitochondrial Targeting Sequences
    • Claros, M.G.1    Vincens, P.2
  • 18
    • 0029915525 scopus 로고    scopus 로고
    • Computational method to predict mitochondrially imported proteins and their targeting sequences
    • Claros MG & Vincens P (1996) Computational method to predict mitochondrially imported proteins and their targeting sequences. Eur J Biochem 241, 779-786.
    • (1996) Eur J Biochem , vol.241 , pp. 779-786
    • Claros, M.G.1    Vincens, P.2
  • 19
    • 0034928937 scopus 로고    scopus 로고
    • Crystal structure of methylmalonyl-coenzyme A epimerase from P. shermanii: A novel enzymatic function on an ancient metal binding scaffold
    • McCarthy AA, Baker HM, Shewry SC, Patchett ML & Baker EN (2001) Crystal structure of methylmalonyl-coenzyme A epimerase from P. shermanii: a novel enzymatic function on an ancient metal binding scaffold. Structure 9, 637-646.
    • (2001) Structure , vol.9 , pp. 637-646
    • McCarthy, A.A.1    Baker, H.M.2    Shewry, S.C.3    Patchett, M.L.4    Baker, E.N.5
  • 20
    • 0032463747 scopus 로고    scopus 로고
    • All in the family: Structural and evolutionary relationships among three modular proteins with diverse functions and variable assembly
    • Bergdoll M, Eltis LD, Cameron AD, Dumas P & Bolin JT (1998) All in the family: structural and evolutionary relationships among three modular proteins with diverse functions and variable assembly. Protein Sci 1, 1661-1670.
    • (1998) Protein Sci , vol.1 , pp. 1661-1670
    • Bergdoll, M.1    Eltis, L.D.2    Cameron, A.D.3    Dumas, P.4    Bolin, J.T.5
  • 21
    • 0020825803 scopus 로고
    • Proton transfer in methylmalonyl-CoA epimerase from Propionibacterium shermanii. The reaction of (2R)-methylmalonyl-CoA in tritiated water
    • Fuller JQ & Leadlay PF (1983) Proton transfer in methylmalonyl-CoA epimerase from Propionibacterium shermanii. The reaction of (2R)-methylmalonyl- CoA in tritiated water. Biochem J 213, 643-650.
    • (1983) Biochem J , vol.213 , pp. 643-650
    • Fuller, J.Q.1    Leadlay, P.F.2
  • 22
    • 0021276833 scopus 로고
    • Effects of cobalt or hydroxycobalamin supplementation on vitamin B-12 content and (S)-methylmalonyl-CoA mutase activity of tissue from cobalt-depleted sheep
    • Peters JP & Elliot JM (1984) Effects of cobalt or hydroxycobalamin supplementation on vitamin B-12 content and (S)-methylmalonyl-CoA mutase activity of tissue from cobalt-depleted sheep. J Nutr 114, 660-670.
    • (1984) J Nutr , vol.114 , pp. 660-670
    • Peters, J.P.1    Elliot, J.M.2
  • 23
    • 0037180440 scopus 로고    scopus 로고
    • Identification of the gene responsible for the cblA complementation group of vitamin B12-responsive methylmalonic acidemia based on analysis of prokaryotic gene arrangements
    • Dobson CM, Wai T, Leclerc D, Wilson A, Wu X, Dore C, Hudson T, Rosenblatt DS & Gravel RA (2002) Identification of the gene responsible for the cblA complementation group of vitamin B12-responsive methylmalonic acidemia based on analysis of prokaryotic gene arrangements. Proc Natl Acad Sci USA 99, 15554-15559.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 15554-15559
    • Dobson, C.M.1    Wai, T.2    Leclerc, D.3    Wilson, A.4    Wu, X.5    Dore, C.6    Hudson, T.7    Rosenblatt, D.S.8    Gravel, R.A.9
  • 24
    • 1842791547 scopus 로고    scopus 로고
    • MeaB is a component of the methylmalonyl-CoA mutase complex required for protection of the enzyme from inactivation
    • Korotkova N & Lidstrom ME (2004) MeaB is a component of the methylmalonyl-CoA mutase complex required for protection of the enzyme from inactivation. J Biol Chem 279, 13652-13658.
    • (2004) J Biol Chem , vol.279 , pp. 13652-13658
    • Korotkova, N.1    Lidstrom, M.E.2
  • 25
    • 0037646518 scopus 로고    scopus 로고
    • Identification of the human and bovine ATP: Cob (I) alamin adenosyltransferase cDNAs based on complementation of a bacterial mutant
    • Leal NA, Park SD, Kima PE & Bobik TA (2003) Identification of the human and bovine ATP: Cob (I) alamin adenosyltransferase cDNAs based on complementation of a bacterial mutant. J Biol Chem 278, 9227-9234.
    • (2003) J Biol Chem , vol.278 , pp. 9227-9234
    • Leal, N.A.1    Park, S.D.2    Kima, P.E.3    Bobik, T.A.4
  • 27
    • 0021112564 scopus 로고
    • Recognition, isolation, and characterization of rat liver D-methylmalonyl coenzyme A hydrolase
    • Kovachy RJ, Copley SD & Allen RH (1983) Recognition, isolation, and characterization of rat liver D-methylmalonyl coenzyme A hydrolase. J Biol Chem 258, 11415-11421.
    • (1983) J Biol Chem , vol.258 , pp. 11415-11421
    • Kovachy, R.J.1    Copley, S.D.2    Allen, R.H.3
  • 29
    • 0021036189 scopus 로고
    • Metabolism of methylmalonic acid in rats. Is methylmalonyl-coenzyme a racemase deficiency symptomatic in man?
    • Montgomery JA, Mamer OA & Scriver CR (1983) Metabolism of methylmalonic acid in rats. Is methylmalonyl-coenzyme a racemase deficiency symptomatic in man? J Clin Invest 72, 1937-1947.
    • (1983) J Clin Invest , vol.72 , pp. 1937-1947
    • Montgomery, J.A.1    Mamer, O.A.2    Scriver, C.R.3
  • 30
    • 0000242498 scopus 로고
    • Metabolism of propionic acid in animal tissues. IX. Methylmalonyl coenzyme A racemase
    • Mazumder R, Sasakawa T, Kaziro Y & Ochoa S (1962) Metabolism of propionic acid in animal tissues. IX. Methylmalonyl coenzyme A racemase. J Biol Chem 237, 3065-3068.
    • (1962) J Biol Chem , vol.237 , pp. 3065-3068
    • Mazumder, R.1    Sasakawa, T.2    Kaziro, Y.3    Ochoa, S.4
  • 31
    • 4344630828 scopus 로고    scopus 로고
    • The role of oxidative damage in the neuropathology of organic acidurias: Insights from animal studies
    • Wajner M, Latini A, Wyse AT & Dutra-Filho CS (2004) The role of oxidative damage in the neuropathology of organic acidurias: insights from animal studies. J Inherit Metab Dis 21, 427-434.
    • (2004) J Inherit Metab Dis , vol.21 , pp. 427-434
    • Wajner, M.1    Latini, A.2    Wyse, A.T.3    Dutra-Filho, C.S.4
  • 33
    • 0037228016 scopus 로고    scopus 로고
    • A systematic RNAi screen identifies a critical role for mitochondria in C. elegans longevity
    • Lee SS, Lee RY, Fraser AG, Kamath RS, Ahringer J & Ruvkun G (2003) A systematic RNAi screen identifies a critical role for mitochondria in C. elegans longevity. Nat Genet 33, 40-48.
    • (2003) Nat Genet , vol.33 , pp. 40-48
    • Lee, S.S.1    Lee, R.Y.2    Fraser, A.G.3    Kamath, R.S.4    Ahringer, J.5    Ruvkun, G.6
  • 36
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • Edgar RC (2004) MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32, 1792-1797.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 38
    • 15944405408 scopus 로고    scopus 로고
    • Gouy M (2004) Unrooted. http://pbil.University-lyon1.fr/software/ unrooted.html
    • (2004) Unrooted
    • Gouy, M.1
  • 39
    • 3242889054 scopus 로고    scopus 로고
    • Wurst: A protein threading server with a structural scoring function, sequence profiles and optimized substitution matrices
    • Torda AE, Procter JB & Huber T (2004) Wurst: a protein threading server with a structural scoring function, sequence profiles and optimized substitution matrices. Nucleic Acids Res 32, W532-W535.
    • (2004) Nucleic Acids Res , vol.32
    • Torda, A.E.1    Procter, J.B.2    Huber, T.3
  • 40
    • 0347383758 scopus 로고    scopus 로고
    • Modeller: Generation and refinement of homology-based protein structure models
    • Fiser A & Sali A (2003) Modeller: generation and refinement of homology-based protein structure models. Methods Enzymol 374, 461-491.
    • (2003) Methods Enzymol , vol.374 , pp. 461-491
    • Fiser, A.1    Sali, A.2
  • 41
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend G (1990) WHAT IF: a molecular modeling and drug design program. J Mol Graph 8, 52-56.
    • (1990) J Mol Graph , vol.8 , pp. 52-56
    • Vriend, G.1
  • 43
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Luthy R, Bowie JU & Eisenberg D (1992) Assessment of protein models with three-dimensional profiles. Nature 356, 83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 44
    • 0027995077 scopus 로고
    • pJC20 and pJC40 - Two high-copy-number vectors for T7 RNA polymerase-dependent expression of recombinant genes in Escherichia coli
    • Clos J & Brandau S (1994) pJC20 and pJC40 - two high-copy-number vectors for T7 RNA polymerase-dependent expression of recombinant genes in Escherichia coli. Protein Expr Purif 5, 133-137.
    • (1994) Protein Expr Purif , vol.5 , pp. 133-137
    • Clos, J.1    Brandau, S.2
  • 46
    • 0028238895 scopus 로고
    • Pha-1, a selectable marker for gene transfer in C. elegans
    • Granato M, Schnabel H & Schnabel R (1994) Pha-1, a selectable marker for gene transfer in C. elegans. Nucleic Acids Res 22, 1762-1763.
    • (1994) Nucleic Acids Res , vol.22 , pp. 1762-1763
    • Granato, M.1    Schnabel, H.2    Schnabel, R.3
  • 47
    • 0035941485 scopus 로고    scopus 로고
    • Ingestion of bacterially expressed dsRNAs can produce specific and potent genetic interference in Caenorhabditis elegans
    • Timmons L & Fire A (2001) Ingestion of bacterially expressed dsRNAs can produce specific and potent genetic interference in Caenorhabditis elegans. Gene 263, 103-112.
    • (2001) Gene , vol.263 , pp. 103-112
    • Timmons, L.1    Fire, A.2
  • 48
    • 0030796721 scopus 로고    scopus 로고
    • Reverse genetics by chemical mutagenesis in Caenorhabditis elegans
    • Jansen G, Hazendonk E, Thijssen KL & Plasterk RH (1997) Reverse genetics by chemical mutagenesis in Caenorhabditis elegans. Nat Genet 17, 119-121.
    • (1997) Nat Genet , vol.17 , pp. 119-121
    • Jansen, G.1    Hazendonk, E.2    Thijssen, K.L.3    Plasterk, R.H.4


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