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Volumn 89, Issue 1-2, 2006, Pages 64-73

Propionyl-CoA and adenosylcobalamin metabolism in Caenorhabditis elegans: Evidence for a role of methylmalonyl-CoA epimerase in intermediary metabolism

Author keywords

Bioinformatics; C. elegans; Cobalamin; Mass spectrometry; Methylmalonic acidemia; Methylmalonyl CoA epimerase; Methylmalonyl CoA mutase; Methylmalonyl CoA racemase; Propionate metabolism; RNA interference

Indexed keywords

COBAMAMIDE; LENTIVIRUS VECTOR; METHYLMALONYL COENZYME A MUTASE; PROPIONIC ACID; PROPIONYL COENZYME A; RNA;

EID: 33746982979     PISSN: 10967192     EISSN: 10967206     Source Type: Journal    
DOI: 10.1016/j.ymgme.2006.06.001     Document Type: Article
Times cited : (24)

References (35)
  • 1
    • 0002911516 scopus 로고    scopus 로고
    • Disorders of propionate and methylmalonate metabolism
    • Scriver C.R., Beaudet A.L., Sly W.S., and Valle D. (Eds), McGraw-Hill, New York
    • Fenton W.A., Gravel R.A., and Rosenblatt D.S. Disorders of propionate and methylmalonate metabolism. In: Scriver C.R., Beaudet A.L., Sly W.S., and Valle D. (Eds). The Metabolic and Molecular Bases for Inhertited Disease (2001), McGraw-Hill, New York 2165-2192
    • (2001) The Metabolic and Molecular Bases for Inhertited Disease , pp. 2165-2192
    • Fenton, W.A.1    Gravel, R.A.2    Rosenblatt, D.S.3
  • 2
    • 0029035831 scopus 로고
    • Long-term follow-up of 77 patients with isolated methylmalonic acidaemia
    • Baumgarter E.R., and Viardot C. Long-term follow-up of 77 patients with isolated methylmalonic acidaemia. J. Inherit. Metab. Dis. 18 (1995) 138-142
    • (1995) J. Inherit. Metab. Dis. , vol.18 , pp. 138-142
    • Baumgarter, E.R.1    Viardot, C.2
  • 4
    • 0020539836 scopus 로고
    • The natural history of the inherited methylmalonic acidemias
    • Matsui S.M., Mahoney M.J., and Rosenberg L.E. The natural history of the inherited methylmalonic acidemias. N. Engl. J. Med. 308 (1983) 857-861
    • (1983) N. Engl. J. Med. , vol.308 , pp. 857-861
    • Matsui, S.M.1    Mahoney, M.J.2    Rosenberg, L.E.3
  • 6
    • 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 C.M., Wai T., Leclerc D., Wilson A., Wu X., Dore C., Hudson T., Rosenblatt D.S., and Gravel R.A. 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 (2002) 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
  • 9
    • 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., and Lidstrom M.E. MeaB is a component of the methylmalonyl-CoA mutase complex required for protection of the enzyme from inactivation. J. Biol. Chem. 279 (2004) 13652-13658
    • (2004) J. Biol. Chem. , vol.279 , pp. 13652-13658
    • Korotkova, N.1    Lidstrom, M.E.2
  • 10
    • 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 N.A., Park S.D., Kima P.E., and Bobik T.A. Identification of the human and bovine ATP:Cob(I)alamin adenosyltransferase cDNAs based on complementation of a bacterial mutant. J. Biol. Chem. 278 (2003) 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
  • 11
    • 0017184537 scopus 로고
    • Rapid prenatal and postnatal detection of inborn errors of propionate, methylmalonate, and cobalamin metabolism: a sensitive assay using cultured cells
    • Willard H.F., Ambani L.M., Hart A.C., Mahoney M.J., and Rosenberg L.E. Rapid prenatal and postnatal detection of inborn errors of propionate, methylmalonate, and cobalamin metabolism: a sensitive assay using cultured cells. Hum. Genet. 34 (1976) 277-283
    • (1976) Hum. Genet. , vol.34 , pp. 277-283
    • Willard, H.F.1    Ambani, L.M.2    Hart, A.C.3    Mahoney, M.J.4    Rosenberg, L.E.5
  • 12
    • 0017171836 scopus 로고
    • A simple, rapid method for prenatal detection of defects in propionate metabolism
    • Morrow G.D., Revsin B., Mathews C., and Giles H. A simple, rapid method for prenatal detection of defects in propionate metabolism. Clin. Genet. 10 (1976) 218-221
    • (1976) Clin. Genet. , vol.10 , pp. 218-221
    • Morrow, G.D.1    Revsin, B.2    Mathews, C.3    Giles, H.4
  • 13
    • 0021036189 scopus 로고
    • Metabolism of methylmalonic acid in rats. Is methylmalonyl-coenzyme a racemase deficiency symptomatic in man?
    • Montgomery J.A., Mamer O.A., and Scriver C.R. Metabolism of methylmalonic acid in rats. Is methylmalonyl-coenzyme a racemase deficiency symptomatic in man?. J. Clin. Invest. 72 (1983) 1937-1947
    • (1983) J. Clin. Invest. , vol.72 , pp. 1937-1947
    • Montgomery, J.A.1    Mamer, O.A.2    Scriver, C.R.3
  • 14
    • 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 T.A., and Rasche M.E. 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 (2001) 37194-37198
    • (2001) J. Biol. Chem. , vol.276 , pp. 37194-37198
    • Bobik, T.A.1    Rasche, M.E.2
  • 16
    • 0025320472 scopus 로고
    • Coenzyme A metabolism in vitamin B-12-deficient rats
    • Brass E.P., Tahiliani A.G., Allen R.H., and Stabler S.P. Coenzyme A metabolism in vitamin B-12-deficient rats. J. Nutr. 120 (1990) 290-297
    • (1990) J. Nutr. , vol.120 , pp. 290-297
    • Brass, E.P.1    Tahiliani, A.G.2    Allen, R.H.3    Stabler, S.P.4
  • 17
    • 0025852644 scopus 로고
    • Inhibition of cobalamin-dependent enzymes by cobalamin analogues in rats
    • Stabler S.P., Brass E.P., Marcell P.D., and Allen R.H. Inhibition of cobalamin-dependent enzymes by cobalamin analogues in rats. J. Clin. Invest. 87 (1991) 1422-1430
    • (1991) J. Clin. Invest. , vol.87 , pp. 1422-1430
    • Stabler, S.P.1    Brass, E.P.2    Marcell, P.D.3    Allen, R.H.4
  • 19
    • 26444531132 scopus 로고    scopus 로고
    • Genetic and genomic systems to study methylmalonic acidemia
    • Chandler R.J., and Venditti C.P. Genetic and genomic systems to study methylmalonic acidemia. Mol. Genet. Metab. 86 (2005) 34-43
    • (2005) Mol. Genet. Metab. , vol.86 , pp. 34-43
    • Chandler, R.J.1    Venditti, C.P.2
  • 20
    • 0028347485 scopus 로고
    • Propionate metabolism in Saccharomyces cerevisiae: implications for the metabolon hypothesis
    • Pronk J.T., van der Linden-Beuman A., Verduyn C., Scheffers W.A., and van Dijken J.P. Propionate metabolism in Saccharomyces cerevisiae: implications for the metabolon hypothesis. Microbiology 140 Pt 4 (1994) 717-722
    • (1994) Microbiology , vol.140 , Issue.PART 4 , pp. 717-722
    • Pronk, J.T.1    van der Linden-Beuman, A.2    Verduyn, C.3    Scheffers, W.A.4    van Dijken, J.P.5
  • 21
    • 0016063911 scopus 로고
    • The genetics of Caenorhabditis elegans
    • Brenner S. The genetics of Caenorhabditis elegans. Genetics 77 (1974) 71-94
    • (1974) Genetics , vol.77 , pp. 71-94
    • Brenner, S.1
  • 22
    • 0035941485 scopus 로고    scopus 로고
    • Ingestion of bacterially expressed dsRNAs can produce specific and potent genetic interference in Caenorhabditis elegans
    • Timmons L., Court D.L., and Fire A. Ingestion of bacterially expressed dsRNAs can produce specific and potent genetic interference in Caenorhabditis elegans. Gene 263 (2001) 103-112
    • (2001) Gene , vol.263 , pp. 103-112
    • Timmons, L.1    Court, D.L.2    Fire, A.3
  • 23
    • 0027420975 scopus 로고
    • Expression of recombinant human methylmalonyl-CoA mutase: in primary mut fibroblasts and Saccharomyces cerevisiae
    • Andrews E., Jansen R., Crane A.M., Cholin S., McDonnell D., and Ledley F.D. Expression of recombinant human methylmalonyl-CoA mutase: in primary mut fibroblasts and Saccharomyces cerevisiae. Biochem. Med. Metab. B. 50 (1993) 135-144
    • (1993) Biochem. Med. Metab. B. , vol.50 , pp. 135-144
    • Andrews, E.1    Jansen, R.2    Crane, A.M.3    Cholin, S.4    McDonnell, D.5    Ledley, F.D.6
  • 24
    • 0027182884 scopus 로고
    • Elevation of 2-methylcitric acid I and II levels in serum, urine, and cerebrospinal fluid of patients with cobalamin deficiency
    • Allen R.H., Stabler S.P., Savage D.G., and Lindenbaum J. Elevation of 2-methylcitric acid I and II levels in serum, urine, and cerebrospinal fluid of patients with cobalamin deficiency. Metabolism 42 (1993) 978-988
    • (1993) Metabolism , vol.42 , pp. 978-988
    • Allen, R.H.1    Stabler, S.P.2    Savage, D.G.3    Lindenbaum, J.4
  • 26
    • 0035827706 scopus 로고    scopus 로고
    • Mitochondrial expression and function of GAS-1 in Caenorhabditis elegans
    • Kayser E.B., Morgan P.G., Hoppel C.L., and Sedensky M.M. Mitochondrial expression and function of GAS-1 in Caenorhabditis elegans. J. Biol. Chem. 276 (2001) 20551-20558
    • (2001) J. Biol. Chem. , vol.276 , pp. 20551-20558
    • Kayser, E.B.1    Morgan, P.G.2    Hoppel, C.L.3    Sedensky, M.M.4
  • 28
  • 31
    • 0030760612 scopus 로고    scopus 로고
    • Expression and kinetic characterization of methylmalonyl-CoA mutase from patients with the mut- phenotype: evidence for naturally occurring interallelic complementation
    • Janata J., Kogekar N., and Fenton W.A. Expression and kinetic characterization of methylmalonyl-CoA mutase from patients with the mut- phenotype: evidence for naturally occurring interallelic complementation. Hum. Mol. Genet. 6 (1997) 1457-1464
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 1457-1464
    • Janata, J.1    Kogekar, N.2    Fenton, W.A.3
  • 32
    • 0021161544 scopus 로고
    • Purification and characterization of methylmalonyl-CoA mutase from Ascaris lumbricoides
    • Han Y.S., Bratt J.M., and Hogenkamp H.P. Purification and characterization of methylmalonyl-CoA mutase from Ascaris lumbricoides. Comp. Biochem. Phys. B. 78 (1984) 41-45
    • (1984) Comp. Biochem. Phys. B. , vol.78 , pp. 41-45
    • Han, Y.S.1    Bratt, J.M.2    Hogenkamp, H.P.3
  • 33
    • 0015464609 scopus 로고
    • Methylmalonyl coenzyme A racemase defect: another cause of methylmalonic aciduria
    • Kang E.S., Snodgrass P.J., and Gerald P.S. Methylmalonyl coenzyme A racemase defect: another cause of methylmalonic aciduria. Pediatr. Res. 6 (1972) 875-879
    • (1972) Pediatr. Res. , vol.6 , pp. 875-879
    • Kang, E.S.1    Snodgrass, P.J.2    Gerald, P.S.3
  • 34
    • 0034916889 scopus 로고    scopus 로고
    • Differences in the human and mouse amino-terminal leader peptides of ornithine transcarbamylase affect mitochondrial import and efficacy of adenoviral vectors
    • Ye X., Zimmer K.P., Brown R., Pabin C., Batshaw M.L., Wilson J.M., and Robinson M.B. Differences in the human and mouse amino-terminal leader peptides of ornithine transcarbamylase affect mitochondrial import and efficacy of adenoviral vectors. Hum. Gene Ther. 12 (2001) 1035-1046
    • (2001) Hum. Gene Ther. , vol.12 , pp. 1035-1046
    • Ye, X.1    Zimmer, K.P.2    Brown, R.3    Pabin, C.4    Batshaw, M.L.5    Wilson, J.M.6    Robinson, M.B.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.