메뉴 건너뛰기




Volumn 327, Issue 2, 2012, Pages 134-141

Biochemical and molecular characterization of NAD +-dependent isocitrate dehydrogenase from the ethanologenic bacterium Zymomonas mobilis

Author keywords

Catalytic efficiency; Coenzyme specificity; Isocitrate dehydrogenase; Zymomonas mobilis

Indexed keywords

DIVALENT CATION; HOMODIMER; ISOCITRATE DEHYDROGENASE (NAD); MAGNESIUM ION; MANGANESE; RECOMBINANT ENZYME;

EID: 84855813501     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1111/j.1574-6968.2011.02467.x     Document Type: Article
Times cited : (20)

References (26)
  • 1
    • 1242320293 scopus 로고    scopus 로고
    • A novel biotin protein required for reductive carboxylation of 2-oxoglutarate by isocitrate dehydrogenase in Hydrogenobacter thermophilus TK-6
    • Aoshima M, Ishii M & Igarashi Y (2004) A novel biotin protein required for reductive carboxylation of 2-oxoglutarate by isocitrate dehydrogenase in Hydrogenobacter thermophilus TK-6. Mol Microbiol 51: 791-798.
    • (2004) Mol Microbiol , vol.51 , pp. 791-798
    • Aoshima, M.1    Ishii, M.2    Igarashi, Y.3
  • 3
    • 0034491418 scopus 로고    scopus 로고
    • Functional prediction: identification of protein orthologs and paralogs
    • Chen R & Jeong SS (2000) Functional prediction: identification of protein orthologs and paralogs. Protein Sci 9: 2344-2353.
    • (2000) Protein Sci , vol.9 , pp. 2344-2353
    • Chen, R.1    Jeong, S.S.2
  • 4
    • 0034669370 scopus 로고    scopus 로고
    • A highly specific monomeric isocitrate dehydrogenase from Corynebacterium glutamicum
    • Chen R & Yang H (2000) A highly specific monomeric isocitrate dehydrogenase from Corynebacterium glutamicum. Arch Biochem Biophys 383: 238-245.
    • (2000) Arch Biochem Biophys , vol.383 , pp. 238-245
    • Chen, R.1    Yang, H.2
  • 5
    • 0031019456 scopus 로고    scopus 로고
    • Role of the citrate pathway in glutamate biosynthesis by Streptococcus mutans
    • Cvitkovitch DG, Gutierrez JA & Bleiweis AS (1997) Role of the citrate pathway in glutamate biosynthesis by Streptococcus mutans. J Bacteriol 179: 650-655.
    • (1997) J Bacteriol , vol.179 , pp. 650-655
    • Cvitkovitch, D.G.1    Gutierrez, J.A.2    Bleiweis, A.S.3
  • 6
    • 0032529898 scopus 로고    scopus 로고
    • Control of metabolic interconversion of isocitrate between the catalytically active and inactive Escherichia coli
    • El-Mansi EMT (1998) Control of metabolic interconversion of isocitrate between the catalytically active and inactive Escherichia coli. FEMS Microbiol Lett 166: 333-339.
    • (1998) FEMS Microbiol Lett , vol.166 , pp. 333-339
    • El-Mansi, E.M.T.1
  • 7
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: analysis of multiple sequence alignments in PostScript
    • Gouet P, Courcelle E, Stuart DI & Métoz F (1999) ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15: 305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Métoz, F.4
  • 9
    • 0037183391 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of the NAD-dependent isocitrate dehydrogenase from the chemolithotroph Acidithiobacillus thiooxidans
    • Inoue H, Tamura T, Ehara N, Nishito A, Nakayama Y, Maekawa M, Imada K, Tanaka H & Inagaki K (2002) Biochemical and molecular characterization of the NAD-dependent isocitrate dehydrogenase from the chemolithotroph Acidithiobacillus thiooxidans. FEMS Microbiol Lett 214: 127-132.
    • (2002) FEMS Microbiol Lett , vol.214 , pp. 127-132
    • Inoue, H.1    Tamura, T.2    Ehara, N.3    Nishito, A.4    Nakayama, Y.5    Maekawa, M.6    Imada, K.7    Tanaka, H.8    Inagaki, K.9
  • 10
    • 0035844289 scopus 로고    scopus 로고
    • +-dependent isocitrate dehydrogenase
    • +-dependent isocitrate dehydrogenase. J Biol Chem 276: 16168-16176.
    • (2001) J Biol Chem , vol.276 , pp. 16168-16176
    • Jo, S.H.1    Son, M.K.2    Koh, H.J.3
  • 13
    • 77953147390 scopus 로고    scopus 로고
    • Structural characterization of tartrate dehydrogenase: a versatile enzyme catalyzing multiple reactions
    • Malik R & Viola RE (2010) Structural characterization of tartrate dehydrogenase: a versatile enzyme catalyzing multiple reactions. Acta Cryst 66: 673-684.
    • (2010) Acta Cryst , vol.66 , pp. 673-684
    • Malik, R.1    Viola, R.E.2
  • 14
    • 25144438461 scopus 로고    scopus 로고
    • Crystal structure of tetrameric homoisocitrate dehydrogenase from an extreme thermophile, Thermus thermophilus: involvement of hydrophobic dimer-dimer interaction in extremely high thermotolerance
    • Miyazaki J, Asada K, Fushinobu S, Kuzuyama T & Nishiyama M (2005) Crystal structure of tetrameric homoisocitrate dehydrogenase from an extreme thermophile, Thermus thermophilus: involvement of hydrophobic dimer-dimer interaction in extremely high thermotolerance. J Bacteriol 187: 6779-6788.
    • (2005) J Bacteriol , vol.187 , pp. 6779-6788
    • Miyazaki, J.1    Asada, K.2    Fushinobu, S.3    Kuzuyama, T.4    Nishiyama, M.5
  • 15
    • 80052550947 scopus 로고    scopus 로고
    • Genome sequence of the ethanol-producing Zymomonas mobilis subsp. mobilis lectotype strain ATCC 10988
    • Pappas KM, Kouvelis VN, Saunders E et al. (2011) Genome sequence of the ethanol-producing Zymomonas mobilis subsp. mobilis lectotype strain ATCC 10988. J Bacteriol 193: 5051-5052.
    • (2011) J Bacteriol , vol.193 , pp. 5051-5052
    • Pappas, K.M.1    Kouvelis, V.N.2    Saunders, E.3
  • 16
    • 50049087891 scopus 로고    scopus 로고
    • Structural studies of Saccharomyces cerevesiae mitochondrial NADP-dependent Isocitrate dehydrogenase in different enzymatic states reveal substantial conformational changes during the catalytic reaction
    • Peng Y, Zhong C, Huang W & Ding J (2008) Structural studies of Saccharomyces cerevesiae mitochondrial NADP-dependent Isocitrate dehydrogenase in different enzymatic states reveal substantial conformational changes during the catalytic reaction. Protein Sci 17: 1542-1554.
    • (2008) Protein Sci , vol.17 , pp. 1542-1554
    • Peng, Y.1    Zhong, C.2    Huang, W.3    Ding, J.4
  • 18
    • 21144437397 scopus 로고    scopus 로고
    • The genome sequence of the ethanologenic bacterium Zymomonas mobilis ZM4
    • Seo JS, Chong H, Park HS et al. (2005) The genome sequence of the ethanologenic bacterium Zymomonas mobilis ZM4. Nat Biotechnol 23: 63-68.
    • (2005) Nat Biotechnol , vol.23 , pp. 63-68
    • Seo, J.S.1    Chong, H.2    Park, H.S.3
  • 19
    • 0030589557 scopus 로고    scopus 로고
    • Carbohydrate metabolism in Zymomonas mobilis: a catabolic highway with some scenic routes
    • Sprenger GA (1996) Carbohydrate metabolism in Zymomonas mobilis: a catabolic highway with some scenic routes. FEMS Microbiol Lett 145: 301-307.
    • (1996) FEMS Microbiol Lett , vol.145 , pp. 301-307
    • Sprenger, G.A.1
  • 20
    • 0035941275 scopus 로고    scopus 로고
    • Comparison of isocitrate dehydrogenase from three hyperthermophiles reveals differences in thermostability, cofactor specificity, oligomeric state, and phylogenetic affiliation
    • Steen IH, Madern D, Karlström M, Lien T, Ladenstein R & Birkeland NK (2001) Comparison of isocitrate dehydrogenase from three hyperthermophiles reveals differences in thermostability, cofactor specificity, oligomeric state, and phylogenetic affiliation. J Biol Chem 276: 43924-43931.
    • (2001) J Biol Chem , vol.276 , pp. 43924-43931
    • Steen, I.H.1    Madern, D.2    Karlström, M.3    Lien, T.4    Ladenstein, R.5    Birkeland, N.K.6
  • 21
    • 34247097911 scopus 로고    scopus 로고
    • Biochemical characterization of isocitrate dehydrogenase from Methylococcus capsulatus reveals a unique NAD-dependent homotetrameric enzyme
    • Stokke R, Madern D, Fedøy AE, Karlsen S, Birkeland NK & Steen IH (2007) Biochemical characterization of isocitrate dehydrogenase from Methylococcus capsulatus reveals a unique NAD-dependent homotetrameric enzyme. Arch Microbiol 187: 361-370.
    • (2007) Arch Microbiol , vol.187 , pp. 361-370
    • Stokke, R.1    Madern, D.2    Fedøy, A.E.3    Karlsen, S.4    Birkeland, N.K.5    Steen, I.H.6
  • 23
    • 33947658343 scopus 로고    scopus 로고
    • Quantifying the metabolic capabilities of engineered Zymomonas mobilis using linear programming analysis
    • Tsantili IC, Karim MN & Klapa MI (2007) Quantifying the metabolic capabilities of engineered Zymomonas mobilis using linear programming analysis. Microb Cell Fact 6: 8.
    • (2007) Microb Cell Fact , vol.6 , pp. 8
    • Tsantili, I.C.1    Karim, M.N.2    Klapa, M.I.3
  • 24
    • 4043105583 scopus 로고    scopus 로고
    • Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity
    • Xu X, Zhao J, Xu Z, Peng B, Huang Q, Arnold E & Ding J (2004) Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity. J Biol Chem 279: 33946-33957.
    • (2004) J Biol Chem , vol.279 , pp. 33946-33957
    • Xu, X.1    Zhao, J.2    Xu, Z.3    Peng, B.4    Huang, Q.5    Arnold, E.6    Ding, J.7
  • 25
    • 72649105234 scopus 로고    scopus 로고
    • Enzymatic characterization of a monomeric isocitrate dehydrogenase from Streptomyces lividans TK54
    • Zhang B, Wang B, Wang P, Cao Z, Huang E, Hao J, Dean AM & Zhu G (2009) Enzymatic characterization of a monomeric isocitrate dehydrogenase from Streptomyces lividans TK54. Biochimie 91: 1405-1410.
    • (2009) Biochimie , vol.91 , pp. 1405-1410
    • Zhang, B.1    Wang, B.2    Wang, P.3    Cao, Z.4    Huang, E.5    Hao, J.6    Dean, A.M.7    Zhu, G.8
  • 26
    • 14544286855 scopus 로고    scopus 로고
    • The selective cause of an ancient adaptation
    • Zhu GP, Golding GB & Dean AM (2005) The selective cause of an ancient adaptation. Science 307: 1279-1282.
    • (2005) Science , vol.307 , pp. 1279-1282
    • Zhu, G.P.1    Golding, G.B.2    Dean, A.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.