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Volumn 393, Issue 1-2, 2007, Pages 53-61

Characterization of a lipoate-protein ligase A gene of rice (Oryza sativa L.)

Author keywords

Lipoate dependent enzymes; Lipoate protein ligase A (LPLA); Lipoic acids; Oryza sativa L.

Indexed keywords

GLYCINE DEHYDROGENASE (DECARBOXYLATING); LIGASE; OXOGLUTARATE DEHYDROGENASE; PROTEIN LIGASE A; PYRUVATE DEHYDROGENASE; THIOCTIC ACID; UNCLASSIFIED DRUG;

EID: 34047258486     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2007.01.011     Document Type: Article
Times cited : (19)

References (26)
  • 1
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • Altschul S.F., et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acid Res. 25 (1997) 3389-3402
    • (1997) Nucleic Acid Res. , vol.25 , pp. 3389-3402
    • Altschul, S.F.1
  • 2
    • 0030739786 scopus 로고    scopus 로고
    • Cloning and characterization of the lipoyl-protein ligase gene LIPB from the yeast Kluyveromyces lactis: synergistic respiratory deficiency due to mutations in LIPB and mitochondrial F1-ATPase subunits
    • Chen X.J. Cloning and characterization of the lipoyl-protein ligase gene LIPB from the yeast Kluyveromyces lactis: synergistic respiratory deficiency due to mutations in LIPB and mitochondrial F1-ATPase subunits. Mol. Gen. Genet. 255 (1997) 341-349
    • (1997) Mol. Gen. Genet. , vol.255 , pp. 341-349
    • Chen, X.J.1
  • 3
    • 2542641045 scopus 로고    scopus 로고
    • Lipoyl synthase requires two equivalents of S-adenosyl-l-methionine to synthesize one equivalent of lipoic acid
    • Cicchillo R.M., et al. Lipoyl synthase requires two equivalents of S-adenosyl-l-methionine to synthesize one equivalent of lipoic acid. Biochemistry 43 (2004) 6378-6386
    • (2004) Biochemistry , vol.43 , pp. 6378-6386
    • Cicchillo, R.M.1
  • 4
    • 0026757052 scopus 로고
    • Expression of mature bovine H-protein of the glycine cleavage system in Escherichia coli and in vitro lipoylation of the apoform
    • Fujiwara K., Okamura-Ikeda K., and Motokawa Y. Expression of mature bovine H-protein of the glycine cleavage system in Escherichia coli and in vitro lipoylation of the apoform. J. Biol. Chem. 267 (1992) 20011-20016
    • (1992) J. Biol. Chem. , vol.267 , pp. 20011-20016
    • Fujiwara, K.1    Okamura-Ikeda, K.2    Motokawa, Y.3
  • 5
    • 0028244665 scopus 로고
    • Purification and characterization of lipoyl-AMP:Nε-lysine lipoyltransferase from bovine liver mitochondria
    • Fujiwara K., Okamura-Ikeda K., and Motokawa Y. Purification and characterization of lipoyl-AMP:Nε-lysine lipoyltransferase from bovine liver mitochondria. J. Biol. Chem. 269 (1994) 16605-16609
    • (1994) J. Biol. Chem. , vol.269 , pp. 16605-16609
    • Fujiwara, K.1    Okamura-Ikeda, K.2    Motokawa, Y.3
  • 6
    • 17544383938 scopus 로고    scopus 로고
    • Lipoylation of acyltransferase components of α-ketoacid dehydrogenase complexes
    • Fujiwara K., Okamura-Ikeda K., and Motokawa Y. Lipoylation of acyltransferase components of α-ketoacid dehydrogenase complexes. J. Biol. Chem. 271 (1996) 12932-13936
    • (1996) J. Biol. Chem. , vol.271 , pp. 12932-13936
    • Fujiwara, K.1    Okamura-Ikeda, K.2    Motokawa, Y.3
  • 7
    • 0031450153 scopus 로고    scopus 로고
    • Cloning and expression of a cDNA encoding bovine lipoyltransferase
    • Fujiwara K., Okamura-Ikeda K., and Motokawa Y. Cloning and expression of a cDNA encoding bovine lipoyltransferase. J. Biol. Chem. 272 (1997) 31974-31978
    • (1997) J. Biol. Chem. , vol.272 , pp. 31974-31978
    • Fujiwara, K.1    Okamura-Ikeda, K.2    Motokawa, Y.3
  • 8
    • 0024559375 scopus 로고
    • Acylation of viral and eukaryotic proteins
    • Grand R.J.A. Acylation of viral and eukaryotic proteins. Biochem. J. 258 (1989) 625-638
    • (1989) Biochem. J. , vol.258 , pp. 625-638
    • Grand, R.J.A.1
  • 9
    • 0030747906 scopus 로고    scopus 로고
    • A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria
    • Jordan S.W., and Cronan Jr. J.E. A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria. J. Biol. Chem. 272 29 (1997) 17903-17906
    • (1997) J. Biol. Chem. , vol.272 , Issue.29 , pp. 17903-17906
    • Jordan, S.W.1    Cronan Jr., J.E.2
  • 10
    • 0037371576 scopus 로고    scopus 로고
    • The Escherichia coli lipB gene encodes lipoyl (octanoyl)-acyl carrier protein:protein transferase
    • Jordan S.W., and Cronan Jr. J.E. The Escherichia coli lipB gene encodes lipoyl (octanoyl)-acyl carrier protein:protein transferase. J. Bacteriol. 185 5 (2003) 1582-1589
    • (2003) J. Bacteriol. , vol.185 , Issue.5 , pp. 1582-1589
    • Jordan, S.W.1    Cronan Jr., J.E.2
  • 11
    • 4344607491 scopus 로고    scopus 로고
    • Characterization of a new member of the glutathione peroxidase gene family in Oryza sativa
    • Kang S.G., Jeong H.K., and Suh H.S. Characterization of a new member of the glutathione peroxidase gene family in Oryza sativa. Mol. Cells 17 (2004) 23-28
    • (2004) Mol. Cells , vol.17 , pp. 23-28
    • Kang, S.G.1    Jeong, H.K.2    Suh, H.S.3
  • 12
    • 0028247161 scopus 로고
    • Identification of the gene encoding lipoate-protein ligase A of Escherichia coli. Molecular cloning and characterization of the lplA gene and gene product
    • Morris T.W., Reed K.E., and Cronan Jr. J.E. Identification of the gene encoding lipoate-protein ligase A of Escherichia coli. Molecular cloning and characterization of the lplA gene and gene product. J. Biol. Chem. 269 23 (1994) 16091-16100
    • (1994) J. Biol. Chem. , vol.269 , Issue.23 , pp. 16091-16100
    • Morris, T.W.1    Reed, K.E.2    Cronan Jr., J.E.3
  • 13
    • 0028821293 scopus 로고
    • Lipoic acid metabolism in Escherichia coli: the lplA and lipB genes define redundant pathways for ligation of lipoyl groups to apoprotein
    • Morris T.W., Reed K.E., and Cronan Jr. J.E. Lipoic acid metabolism in Escherichia coli: the lplA and lipB genes define redundant pathways for ligation of lipoyl groups to apoprotein. J. Bacteriol. 177 1 (1995) 1-10
    • (1995) J. Bacteriol. , vol.177 , Issue.1 , pp. 1-10
    • Morris, T.W.1    Reed, K.E.2    Cronan Jr., J.E.3
  • 14
    • 0019321718 scopus 로고
    • Rapid isolation of high molecular weight plant DNA
    • Murray M.G., and Thompson W.F. Rapid isolation of high molecular weight plant DNA. Nucleic Acids Res. 8 19 (1980) 4321-4325
    • (1980) Nucleic Acids Res. , vol.8 , Issue.19 , pp. 4321-4325
    • Murray, M.G.1    Thompson, W.F.2
  • 15
    • 0026079562 scopus 로고
    • Domains, motifs, and linkers in 2-oxo acid dehydrogenase multienzyme complexes: a paradigm in the design of a multifunctional protein
    • Perham R.N. Domains, motifs, and linkers in 2-oxo acid dehydrogenase multienzyme complexes: a paradigm in the design of a multifunctional protein. Biochemistry 30 35 (1991) 8501-8512
    • (1991) Biochemistry , vol.30 , Issue.35 , pp. 8501-8512
    • Perham, R.N.1
  • 16
    • 0033790516 scopus 로고    scopus 로고
    • Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions
    • Perham R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Ann. Rev. Biochem. 69 (2000) 961-1004
    • (2000) Ann. Rev. Biochem. , vol.69 , pp. 961-1004
    • Perham, R.N.1
  • 17
    • 0033769643 scopus 로고    scopus 로고
    • Lipoylating and biotinylating enzymes contain a homologous catalytic module
    • Reche P.A. Lipoylating and biotinylating enzymes contain a homologous catalytic module. Protein Sci. 10 (2000) 1922-1929
    • (2000) Protein Sci. , vol.10 , pp. 1922-1929
    • Reche, P.A.1
  • 18
    • 0027401765 scopus 로고
    • Lipoic acid metabolism in Escherichia coli: sequencing and functional characterization of the lipA and lipB genes
    • Reed K.E., and Cronan Jr. J.E. Lipoic acid metabolism in Escherichia coli: sequencing and functional characterization of the lipA and lipB genes. J. Bacteriol. 175 (1993) 14325-1336
    • (1993) J. Bacteriol. , vol.175 , pp. 14325-1336
    • Reed, K.E.1    Cronan Jr., J.E.2
  • 19
    • 0025370816 scopus 로고
    • Structure-function relationships in dihydrolipoamide acyltransferases
    • Reed L.J., and Hackert M.L. Structure-function relationships in dihydrolipoamide acyltransferases. J. Biol. Chem. 265 16 (1990) 8971-8974
    • (1990) J. Biol. Chem. , vol.265 , Issue.16 , pp. 8971-8974
    • Reed, L.J.1    Hackert, M.L.2
  • 20
    • 0028331916 scopus 로고
    • Mutants of Escherichia coli K-12 that are resistant to a selenium analog of lipoic acid identify unknown genes in lipoate metabolism
    • Reed K.E., Morris T.W., and Cronan Jr. J.E. Mutants of Escherichia coli K-12 that are resistant to a selenium analog of lipoic acid identify unknown genes in lipoate metabolism. Proc. Natl. Acad. Sci. U. S. A. 91 (1994) 3720-3724
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 3720-3724
    • Reed, K.E.1    Morris, T.W.2    Cronan Jr., J.E.3
  • 21
    • 0028247161 scopus 로고
    • Identification of the gene encoding lipoate-protein ligase A of Escherichia coli: molecular cloning and characterization of the lplA gene and gene product
    • Timothy W.M., Kelynne E.R., and Cronan Jr. J.E. Identification of the gene encoding lipoate-protein ligase A of Escherichia coli: molecular cloning and characterization of the lplA gene and gene product. J. Biol. Chem. 269 23 (1994) 16091-16100
    • (1994) J. Biol. Chem. , vol.269 , Issue.23 , pp. 16091-16100
    • Timothy, W.M.1    Kelynne, E.R.2    Cronan Jr., J.E.3
  • 22
    • 0014057782 scopus 로고
    • Mammalian lipoic acid activating enzyme
    • Tsunoda J.N., and Yasunobu K.T. Mammalian lipoic acid activating enzyme. Arch. Biochem. Biophys. 118 2 (1967) 395-401
    • (1967) Arch. Biochem. Biophys. , vol.118 , Issue.2 , pp. 395-401
    • Tsunoda, J.N.1    Yasunobu, K.T.2
  • 23
    • 0026018074 scopus 로고
    • Lipoic acid metabolism in Escherichia coli: isolation of null mutants defective in lipoic acid biosynthesis, molecular cloning and characterization of the E. coli lip locus, and identification of the lipoylated protein of the glycine cleavage system
    • Vanden Boom T.J., Reed K.E., and Cronan Jr. J.E. Lipoic acid metabolism in Escherichia coli: isolation of null mutants defective in lipoic acid biosynthesis, molecular cloning and characterization of the E. coli lip locus, and identification of the lipoylated protein of the glycine cleavage system. J. Bacteriol. 173 (1991) 6412-6420
    • (1991) J. Bacteriol. , vol.173 , pp. 6412-6420
    • Vanden Boom, T.J.1    Reed, K.E.2    Cronan Jr., J.E.3
  • 24
    • 0034953587 scopus 로고    scopus 로고
    • Lipoic acid metabolism in Arabidopsis thaliana: cloning and characterization of a cDNA encoding lipoyltransferase
    • Wada M., Yasuno R., Jordan S.W., Cronan Jr. J.E., and Wada H. Lipoic acid metabolism in Arabidopsis thaliana: cloning and characterization of a cDNA encoding lipoyltransferase. Plant Cell Physiol. 42 6 (2001) 650-656
    • (2001) Plant Cell Physiol. , vol.42 , Issue.6 , pp. 650-656
    • Wada, M.1    Yasuno, R.2    Jordan, S.W.3    Cronan Jr., J.E.4    Wada, H.5
  • 25
    • 0035850835 scopus 로고    scopus 로고
    • Identification of an Arabidopsis cDNA encoding a lipoyltransferase located in plastids
    • Wada M., Yasuno R., and Wada H. Identification of an Arabidopsis cDNA encoding a lipoyltransferase located in plastids. FEBS Lett. 506 3 (2001) 286-290
    • (2001) FEBS Lett. , vol.506 , Issue.3 , pp. 286-290
    • Wada, M.1    Yasuno, R.2    Wada, H.3
  • 26
    • 0348229020 scopus 로고    scopus 로고
    • Assembly of the covalent linkage between lipoic acid and its cognate enzymes
    • Zhao X., Miller J.R., Jiang Y., Marletta M.A., and Cronan J.E. Assembly of the covalent linkage between lipoic acid and its cognate enzymes. Chem. Biol. 10 (2003) 1293-1302
    • (2003) Chem. Biol. , vol.10 , pp. 1293-1302
    • Zhao, X.1    Miller, J.R.2    Jiang, Y.3    Marletta, M.A.4    Cronan, J.E.5


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