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Volumn 279, Issue 1, 2008, Pages 64-70

Cloning of a cDNA encoding a NAD-dependent formate dehydrogenase involved in oxalic acid metabolism from the white-rot fungus Ceriporiopsis subvermispora and its gene expression analysis

Author keywords

Ceriporiopsis subvermispora; Formate dehydrogenase; Oxalate dacarboxylase; Oxalate oxidase; Oxalic acid; Wood rotting fungi

Indexed keywords

FORMATE DEHYDROGENASE; FUNGAL DNA; FUNGAL ENZYME; NICOTINAMIDE ADENINE DINUCLEOTIDE; RECOMBINANT PROTEIN;

EID: 37349024023     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1111/j.1574-6968.2007.01022.x     Document Type: Article
Times cited : (15)

References (21)
  • 1
    • 0033563869 scopus 로고    scopus 로고
    • Oxalate oxidase from Ceriporiopsis subvermispora. Biochemical and cytochemical studies
    • Aguilar C, Urzúa U, Koenig C Vicuña R (1999) Oxalate oxidase from Ceriporiopsis subvermispora. Biochemical and cytochemical studies. Arch Biochem Biophys 366 : 275 282.
    • (1999) Arch Biochem Biophys , vol.366 , pp. 275-282
    • Aguilar, C.1    Urzúa, U.2    Koenig, C.3    Vicuña, R.4
  • 2
    • 0025039578 scopus 로고
    • A novel enzymatic decarboxylation of oxalic acid by lignin peroxidase system of white-rot fungus Phanerochaete chrysosporium
    • Akamatsu Y, Ma DB, Higuchi T Shimada M (1990) A novel enzymatic decarboxylation of oxalic acid by lignin peroxidase system of white-rot fungus Phanerochaete chrysosporium. FEBS Lett 269 : 261 263.
    • (1990) FEBS Lett , vol.269 , pp. 261-263
    • Akamatsu, Y.1    Ma, D.B.2    Higuchi, T.3    Shimada, M.4
  • 3
    • 0022348589 scopus 로고
    • Biosynthesis, isolation and properties of NAD-dependent formate dehydrogenase from the yeast Candida methylica
    • Avilova TV, Egorova OA, Ioanesyan lS Egorov AM (1985) Biosynthesis, isolation and properties of NAD-dependent formate dehydrogenase from the yeast Candida methylica. Eur J Biochem 152 : 657 662.
    • (1985) Eur J Biochem , vol.152 , pp. 657-662
    • Avilova, T.V.1    Egorova, O.A.2    Ls, I.3    Egorov, A.M.4
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 : 248 254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0027154574 scopus 로고
    • Developmental regulation of the gene for formate dehydrogenase in Neurospora crassa
    • Chow CM RajBhandary UL (1993) Developmental regulation of the gene for formate dehydrogenase in Neurospora crassa. J Bacteriol 175 : 3703 3709.
    • (1993) J Bacteriol , vol.175 , pp. 3703-3709
    • Chow, C.M.1    Rajbhandary, U.L.2
  • 6
    • 0029660710 scopus 로고    scopus 로고
    • Oxalate production by fungi: Its role in pathogenicity and ecology in the soil environment
    • Dutton MV Evans CS (1996) Oxalate production by fungi: its role in pathogenicity and ecology in the soil environment. Can J Microbiol 42 : 881 895.
    • (1996) Can J Microbiol , vol.42 , pp. 881-895
    • Dutton, M.V.1    Evans, C.S.2
  • 7
    • 22144459829 scopus 로고    scopus 로고
    • Cloning and sequencing of two Ceriporiopsis subvermispora bicupin oxalate oxidase allelic isoforms: Implications for the reaction specificity of oxalate oxidases and decarboxylases
    • Escutia MR, Bowater L, Edwards A, Bottrill AR, Burrull MR, Polanco R, Vicuña R Bornemann S (2005) Cloning and sequencing of two Ceriporiopsis subvermispora bicupin oxalate oxidase allelic isoforms: implications for the reaction specificity of oxalate oxidases and decarboxylases. Appl Environ Microbiol 71 : 3608 3616.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 3608-3616
    • Escutia, M.R.1    Bowater, L.2    Edwards, A.3    Bottrill, A.R.4    Burrull, M.R.5    Polanco, R.6    Vicuña, R.7    Bornemann, S.8
  • 8
    • 18144367735 scopus 로고    scopus 로고
    • An enzymatic study of an oxalate producing system in relation to the glyoxylate cycle in white-rot fungus Phanerochaete chrysosporium
    • Hayashi N, Tokimatsu T, Hattori T Shimada M (2000) An enzymatic study of an oxalate producing system in relation to the glyoxylate cycle in white-rot fungus Phanerochaete chrysosporium. Wood Res 87 : 15 16.
    • (2000) Wood Res , vol.87 , pp. 15-16
    • Hayashi, N.1    Tokimatsu, T.2    Hattori, T.3    Shimada, M.4
  • 9
    • 0017879346 scopus 로고
    • Influence of culture parameters on lignin metabolism by Phanerochaete chrysosporium
    • Kirk TK, Schultz E, Connors WJ, Lorenz LR Zeikus JG (1978) Influence of culture parameters on lignin metabolism by Phanerochaete chrysosporium. Arch Microbiol 117 : 277 285.
    • (1978) Arch Microbiol , vol.117 , pp. 277-285
    • Kirk, T.K.1    Schultz, E.2    Connors, W.J.3    Lorenz, L.R.4    Zeikus, J.G.5
  • 10
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature 227 : 680 685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 11
    • 0029188962 scopus 로고
    • Oxalate decarboxylase in the brown-rot decay fungus Postia placenta
    • Micales J (1995) Oxalate decarboxylase in the brown-rot decay fungus Postia placenta. Mater Organismen (Berlin) 29 : 177 186.
    • (1995) Mater Organismen (Berlin) , vol.29 , pp. 177-186
    • Micales, J.1
  • 12
    • 37349034726 scopus 로고    scopus 로고
    • Occurrence of enzyme systems for production and decomposition of oxalate in a white-rot fungus Coriolus versicolor and characteristics of glyoxylate oxidase
    • Mii K, Hattori T Shimada M (1996) Occurrence of enzyme systems for production and decomposition of oxalate in a white-rot fungus Coriolus versicolor and characteristics of glyoxylate oxidase. Wood Res 87 : 15 16.
    • (1996) Wood Res , vol.87 , pp. 15-16
    • Mii, K.1    Hattori, T.2    Shimada, M.3
  • 13
    • 0027937347 scopus 로고
    • NAD-dependent formate dehydrogenase
    • Popov VO Lamzin VS (1994) NAD-dependent formate dehydrogenase. Biochem J 301 : 625 643.
    • (1994) Biochem J , vol.301 , pp. 625-643
    • Popov, V.O.1    Lamzin, V.S.2
  • 14
    • 0025202423 scopus 로고
    • 2+ in the presence of veratryl alcohol, malonic or oxalic acid and oxygen
    • 2+ in the presence of veratryl alcohol, malonic or oxalic acid and oxygen. Biochemistry 29 : 10475 10480.
    • (1990) Biochemistry , vol.29 , pp. 10475-10480
    • Popp, J.L.1    Kalyanaraman, B.2    Kirk, T.K.3
  • 15
    • 33745272235 scopus 로고    scopus 로고
    • Subcellular localization of glyoxylate cycle key enzymes involved in oxalate biosynthesis of wood-destroying basidiomycete Fomitopsis palustris grown on glucose
    • Sakai S, Nishide T, Munir E, Baba K, Inui H, Nakano Y, Hattori T Shimada M (2006) Subcellular localization of glyoxylate cycle key enzymes involved in oxalate biosynthesis of wood-destroying basidiomycete Fomitopsis palustris grown on glucose. Microbiology 152 : 1857 1866.
    • (2006) Microbiology , vol.152 , pp. 1857-1866
    • Sakai, S.1    Nishide, T.2    Munir, E.3    Baba, K.4    Inui, H.5    Nakano, Y.6    Hattori, T.7    Shimada, M.8
  • 16
    • 0030762532 scopus 로고    scopus 로고
    • Regulation of the formate dehydrogenase gene, FDH1, in the methylotrophic yeast Candida boidinii and growth characteristics of an FDH1-disrupted strain on methanol, methylamine, and choline
    • Sakai Y, Murdanoto AP, Konishi T, Tamatsu A Kato N (1997) Regulation of the formate dehydrogenase gene, FDH1, in the methylotrophic yeast Candida boidinii and growth characteristics of an FDH1-disrupted strain on methanol, methylamine, and choline. J Bacteriol 179 : 4480 4485.
    • (1997) J Bacteriol , vol.179 , pp. 4480-4485
    • Sakai, Y.1    Murdanoto, A.P.2    Konishi, T.3    Tamatsu, A.4    Kato, N.5
  • 17
    • 0342941155 scopus 로고    scopus 로고
    • Possible biochemical roles of oxalic acid as a low molecular weight compound involved in brown-rot and white-rot wood decays
    • Shimada M, Akamtsu Y, Tokimatsu T, Mii K Hattori T (1997) Possible biochemical roles of oxalic acid as a low molecular weight compound involved in brown-rot and white-rot wood decays. J Biotechnol 53 : 103 113.
    • (1997) J Biotechnol , vol.53 , pp. 103-113
    • Shimada, M.1    Akamtsu, Y.2    Tokimatsu, T.3    Mii, K.4    Hattori, T.5
  • 18
    • 0000007203 scopus 로고
    • Oxalic acid decarboxylase, a new enzyme from the mycelium of wood destroying fungi
    • Shimazono H (1955) Oxalic acid decarboxylase, a new enzyme from the mycelium of wood destroying fungi. J Biochem 42 : 321 340.
    • (1955) J Biochem , vol.42 , pp. 321-340
    • Shimazono, H.1
  • 19
    • 0027968068 scopus 로고
    • Clustal w: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, poison-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG Gibson TJ (1994) Clustal w: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, poison-specific gap penalties and weight matrix choice. Nucleic Acids Res 22 : 4673 4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 20
    • 18144420433 scopus 로고    scopus 로고
    • Purification and characterization of NAD-dependent formate dehydrogenase from the white-rot fungus Ceriporiopsis subvermispora and a possible role of the enzyme in oxalate metabolism
    • Watanabe T, Tengku S, Hattori S Shimada M (2005) Purification and characterization of NAD-dependent formate dehydrogenase from the white-rot fungus Ceriporiopsis subvermispora and a possible role of the enzyme in oxalate metabolism. Enzyme Microb Tech 37 : 68 75.
    • (2005) Enzyme Microb Tech , vol.37 , pp. 68-75
    • Watanabe, T.1    Tengku, S.2    Hattori, S.3    Shimada, M.4
  • 21
    • 0031985659 scopus 로고    scopus 로고
    • Manganese peroxidase dependent oxidation of glyoxylic and oxalic acids synthesized by Ceriporiopsis subvermispora produces extracellular hydrogen peroxide
    • Urzúa U, Kersten PJ Vicuña R (1998) Manganese peroxidase dependent oxidation of glyoxylic and oxalic acids synthesized by Ceriporiopsis subvermispora produces extracellular hydrogen peroxide. Appl Environ Microbiol 64 : 68 73.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 68-73
    • Urzúa, U.1    Kersten, P.J.2    Vicuña, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.