메뉴 건너뛰기




Volumn 9, Issue 1, 2016, Pages 116-126

Ustilago maydis produces itaconic acid via the unusual intermediate trans-aconitate

Author keywords

[No Author keywords available]

Indexed keywords

3 CARBOXY MUCONATE LACTONIZING ENZYME; ACONITATE DECARBOXYLASE; ACONITIC ACID; CARBOXYLYASE; FUNGAL ENZYME; ITACONIC ACID; UNCLASSIFIED DRUG; FUNGAL PROTEIN; SUCCINIC ACID DERIVATIVE;

EID: 84953231041     PISSN: 17517907     EISSN: 17517915     Source Type: Journal    
DOI: 10.1111/1751-7915.12329     Document Type: Article
Times cited : (106)

References (61)
  • 1
    • 75549094030 scopus 로고
    • Microbiological dissimilation of tricarballylate and trans-aconitate
    • Altekar, W.W., and Raghavendra Rao, M.R. (1963) Microbiological dissimilation of tricarballylate and trans-aconitate. J Bacteriol 85: 604-613.
    • (1963) J Bacteriol , vol.85 , pp. 604-613
    • Altekar, W.W.1    Raghavendra Rao, M.R.2
  • 2
    • 0000412104 scopus 로고
    • Biosynthesis of itaconic acid in Aspergillus terreus I Tracer studies with C-14-labeled substrates
    • Bentley, R., and Thiessen, C.P. (1957a) Biosynthesis of itaconic acid in Aspergillus terreus I Tracer studies with C-14-labeled substrates. J Biol Chem 226: 673-687.
    • (1957) J Biol Chem , vol.226 , pp. 673-687
    • Bentley, R.1    Thiessen, C.P.2
  • 3
    • 0000412103 scopus 로고
    • Biosynthesis of itaconic acid in Aspergillus terreus. III The properties and reaction mechanism of cis-aconitic acid decarboxylase
    • Bentley, R., and Thiessen, C.P. (1957b) Biosynthesis of itaconic acid in Aspergillus terreus. III The properties and reaction mechanism of cis-aconitic acid decarboxylase. J Biol Chem 226: 703-720.
    • (1957) J Biol Chem , vol.226 , pp. 703-720
    • Bentley, R.1    Thiessen, C.P.2
  • 5
    • 84879292930 scopus 로고    scopus 로고
    • Targeting enzymes to the right compartment: metabolic engineering for itaconic acid production by Aspergillus niger
    • Blumhoff, M.L., Steiger, M.G., Mattanovich, D., and Sauer, M. (2013) Targeting enzymes to the right compartment: metabolic engineering for itaconic acid production by Aspergillus niger. Metab Eng 19: 26-32.
    • (2013) Metab Eng , vol.19 , pp. 26-32
    • Blumhoff, M.L.1    Steiger, M.G.2    Mattanovich, D.3    Sauer, M.4
  • 6
    • 5644228880 scopus 로고    scopus 로고
    • A reverse genetic approach for generating gene replacement mutants in Ustilago maydis
    • Brachmann, A., Konig, J., Julius, C., and Feldbrugge, M. (2004) A reverse genetic approach for generating gene replacement mutants in Ustilago maydis. Mol Genet Genomics 272: 216-226.
    • (2004) Mol Genet Genomics , vol.272 , pp. 216-226
    • Brachmann, A.1    Konig, J.2    Julius, C.3    Feldbrugge, M.4
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation 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
  • 9
    • 84942566577 scopus 로고    scopus 로고
    • Photosynthetic production of itaconic acid in Synechocystis sp PCC6803
    • Chin, T., Sano, M., Takahashi, T., Ohara, H., and Aso, Y. (2015) Photosynthetic production of itaconic acid in Synechocystis sp PCC6803. J Biotechnol 195: 43-45.
    • (2015) J Biotechnol , vol.195 , pp. 43-45
    • Chin, T.1    Sano, M.2    Takahashi, T.3    Ohara, H.4    Aso, Y.5
  • 10
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate phenol chloroform extraction
    • Chomczynski, P., and Sacchi, N. (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate phenol chloroform extraction. Anal Biochem 162: 156-159.
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 11
    • 84937572123 scopus 로고    scopus 로고
    • Itaconic acid: the surprising role of an industrial compound as a mammalian antimicrobial metabolite
    • Cordes, T., Michelucci, A., and Hiller, K. (2015) Itaconic acid: the surprising role of an industrial compound as a mammalian antimicrobial metabolite. Annu Rev Nutr 35: 451-473.
    • (2015) Annu Rev Nutr , vol.35 , pp. 451-473
    • Cordes, T.1    Michelucci, A.2    Hiller, K.3
  • 13
    • 0343673773 scopus 로고    scopus 로고
    • Methods for intense aeration, growth, storage, and replication of bacterial strains in microtiter plates
    • Duetz, W.A., Ruedi, L., Hermann, R., O'Connor, K., Buchs, J., and Witholt, B. (2000) Methods for intense aeration, growth, storage, and replication of bacterial strains in microtiter plates. Appl Environ Microbiol 66: 2641-2646.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 2641-2646
    • Duetz, W.A.1    Ruedi, L.2    Hermann, R.3    O'Connor, K.4    Buchs, J.5    Witholt, B.6
  • 14
    • 0036054538 scopus 로고    scopus 로고
    • Purification and characterization of cis-aconitic acid decarboxylase from Aspergillus terreus TN484-M1
    • Dwiarti, L., Yamane, K., Yamatani, H., Kahar, P., and Okabe, M. (2002) Purification and characterization of cis-aconitic acid decarboxylase from Aspergillus terreus TN484-M1. J Biosci Bioeng 94: 29-33.
    • (2002) J Biosci Bioeng , vol.94 , pp. 29-33
    • Dwiarti, L.1    Yamane, K.2    Yamatani, H.3    Kahar, P.4    Okabe, M.5
  • 15
    • 77955035656 scopus 로고    scopus 로고
    • Selective and flexible transformation of biomass-derived platform chemicals by a multifunctional catalytic system
    • Geilen, F.M.A., Engendahl, B., Harwardt, A., Marquardt, W., Klankermayer, J., and Leitner, W. (2010) Selective and flexible transformation of biomass-derived platform chemicals by a multifunctional catalytic system. Angew Chem 49: 5510-5514.
    • (2010) Angew Chem , vol.49 , pp. 5510-5514
    • Geilen, F.M.A.1    Engendahl, B.2    Harwardt, A.3    Marquardt, W.4    Klankermayer, J.5    Leitner, W.6
  • 16
    • 84969309766 scopus 로고    scopus 로고
    • Prospecting the biodiversity of the fungal family Ustilaginaceae for the production of value-added chemicals
    • Geiser, E., Wiebach, V., Wierckx, N., and Blank, L.M. (2014) Prospecting the biodiversity of the fungal family Ustilaginaceae for the production of value-added chemicals. BMC Fungal Biol Biotechnol 1: 2.
    • (2014) BMC Fungal Biol Biotechnol , vol.1 , pp. 2
    • Geiser, E.1    Wiebach, V.2    Wierckx, N.3    Blank, L.M.4
  • 17
    • 0025084602 scopus 로고
    • The adenovirus major late transcription factor USF is a member of the helix-loop-helix group of regulatory proteins and binds to DNA as a dimer
    • Gregor, P.D., Sawadogo, M., and Roeder, R.G. (1990) The adenovirus major late transcription factor USF is a member of the helix-loop-helix group of regulatory proteins and binds to DNA as a dimer. Genes Dev 4: 1730-1740.
    • (1990) Genes Dev , vol.4 , pp. 1730-1740
    • Gregor, P.D.1    Sawadogo, M.2    Roeder, R.G.3
  • 18
    • 0347285392 scopus 로고    scopus 로고
    • The acnD genes of Shewenella oneidensis and Vibrio cholerae encode a new Fe/S-dependent 2-methylcitrate dehydratase enzyme that requires prpF function in vivo
    • Grimek, T.L., and Escalante-Semerena, J.C. (2004) The acnD genes of Shewenella oneidensis and Vibrio cholerae encode a new Fe/S-dependent 2-methylcitrate dehydratase enzyme that requires prpF function in vivo. J Bacteriol 186: 454-462.
    • (2004) J Bacteriol , vol.186 , pp. 454-462
    • Grimek, T.L.1    Escalante-Semerena, J.C.2
  • 19
    • 0000398267 scopus 로고
    • Accumulation of itaconic, 2-hydroxyparaconic, itatartaric, and malic-acids by strains of the genus Ustilago
    • Guevarra, E.D., and Tabuchi, T. (1990) Accumulation of itaconic, 2-hydroxyparaconic, itatartaric, and malic-acids by strains of the genus Ustilago. Agric Biol Chem 54: 2353-2358.
    • (1990) Agric Biol Chem , vol.54 , pp. 2353-2358
    • Guevarra, E.D.1    Tabuchi, T.2
  • 20
    • 0029795374 scopus 로고    scopus 로고
    • The beta-ketoadipate pathway and the biology of self-identity
    • Harwood, C.S., and Parales, R.E. (1996) The beta-ketoadipate pathway and the biology of self-identity. Annu Rev Microbiol 50: 553-590.
    • (1996) Annu Rev Microbiol , vol.50 , pp. 553-590
    • Harwood, C.S.1    Parales, R.E.2
  • 21
    • 0000214149 scopus 로고
    • Biochemistry of the Ustilaginales. 11. Metabolic products of Ustilago zeae in submerged culture
    • Haskins, R.H., Thorn, J.A., and Boothroyd, B. (1955) Biochemistry of the Ustilaginales. 11. Metabolic products of Ustilago zeae in submerged culture. Can J Microbiol 1: 749-756.
    • (1955) Can J Microbiol , vol.1 , pp. 749-756
    • Haskins, R.H.1    Thorn, J.A.2    Boothroyd, B.3
  • 22
    • 84942551397 scopus 로고    scopus 로고
    • Improving itaconic acid production through genetic engineering of an industrial Aspergillus terreus strain
    • Huang, X., Lu, X., Li, Y., Li, X., and Li, J.J. (2014) Improving itaconic acid production through genetic engineering of an industrial Aspergillus terreus strain. Microb Cell Fact 13: 119.
    • (2014) Microb Cell Fact , vol.13 , pp. 119
    • Huang, X.1    Lu, X.2    Li, Y.3    Li, X.4    Li, J.J.5
  • 24
    • 33750597877 scopus 로고    scopus 로고
    • Insights from the genome of the biotrophic fungal plant pathogen Ustilago maydis
    • Kaemper, J., Kahmann, R., Boelker, M., Ma, L.J., Brefort, T., Saville, B.J., etal. (2006) Insights from the genome of the biotrophic fungal plant pathogen Ustilago maydis. Nature 444: 97-101.
    • (2006) Nature , vol.444 , pp. 97-101
    • Kaemper, J.1    Kahmann, R.2    Boelker, M.3    Ma, L.J.4    Brefort, T.5    Saville, B.J.6
  • 25
    • 48349107488 scopus 로고    scopus 로고
    • Cloning and functional characterization of the cis-aconitic acid decarboxylase (CAD) gene from Aspergillus terreus
    • Kanamasa, S., Dwiarti, L., Okabe, M., and Park, E.Y. (2008) Cloning and functional characterization of the cis-aconitic acid decarboxylase (CAD) gene from Aspergillus terreus. Appl Microbiol Biotechnol 80: 223-229.
    • (2008) Appl Microbiol Biotechnol , vol.80 , pp. 223-229
    • Kanamasa, S.1    Dwiarti, L.2    Okabe, M.3    Park, E.Y.4
  • 26
    • 0028917910 scopus 로고
    • High level expression and characterization of the mitochondrial citrate transport protein from the yeast Saccharomyces cerevisiae
    • Kaplan, R.S., Mayor, J.A., Gremse, D.A., and Wood, D.O. (1995) High level expression and characterization of the mitochondrial citrate transport protein from the yeast Saccharomyces cerevisiae. J Biol Chem 270: 4108-4114.
    • (1995) J Biol Chem , vol.270 , pp. 4108-4114
    • Kaplan, R.S.1    Mayor, J.A.2    Gremse, D.A.3    Wood, D.O.4
  • 27
    • 0038364357 scopus 로고    scopus 로고
    • Aspergillus niger citric acid accumulation: do we understand this well working black box?
    • Karaffa, L., and Kubicek, C.P. (2003) Aspergillus niger citric acid accumulation: do we understand this well working black box? Appl Microbiol Biotechnol 61: 189-196.
    • (2003) Appl Microbiol Biotechnol , vol.61 , pp. 189-196
    • Karaffa, L.1    Kubicek, C.P.2
  • 28
    • 0004315250 scopus 로고
    • Über die Produktion von Itaconsäure und Mannit durch einen neuen Schimmelpilz Aspergillus itaconicus
    • Kinoshita, K. (1932) Über die Produktion von Itaconsäure und Mannit durch einen neuen Schimmelpilz Aspergillus itaconicus. Acta Phytochimica 5: 271-287.
    • (1932) Acta Phytochimica , vol.5 , pp. 271-287
    • Kinoshita, K.1
  • 29
    • 84876478562 scopus 로고    scopus 로고
    • Itaconic acid - a biotechnological process in change
    • Klement, T., and Büchs, J. (2013) Itaconic acid - a biotechnological process in change. Bioresour Technol 135: 422-431.
    • (2013) Bioresour Technol , vol.135 , pp. 422-431
    • Klement, T.1    Büchs, J.2
  • 31
    • 0015215170 scopus 로고
    • Purification and kinetic properties of aconitate isomerase from Pseudomonas putida
    • Klinman, J.P., and Rose, I.A. (1971) Purification and kinetic properties of aconitate isomerase from Pseudomonas putida. Biochemistry 10: 2253-2259.
    • (1971) Biochemistry , vol.10 , pp. 2253-2259
    • Klinman, J.P.1    Rose, I.A.2
  • 33
    • 79954632227 scopus 로고    scopus 로고
    • A clone-based transcriptomics approach for the identification of genes relevant for itaconic acid production in Aspergillus
    • Li, A., van Luijk, N., ter Beek, M., Caspers, M., Punt, P., and van der Werf, M. (2011) A clone-based transcriptomics approach for the identification of genes relevant for itaconic acid production in Aspergillus. Fungal Genet Biol 48: 602-611.
    • (2011) Fungal Genet Biol , vol.48 , pp. 602-611
    • Li, A.1    van Luijk, N.2    ter Beek, M.3    Caspers, M.4    Punt, P.5    van der Werf, M.6
  • 34
    • 84865322864 scopus 로고    scopus 로고
    • Enhanced itaconic acid production in Aspergillus niger using genetic modification and medium optimization
    • Li, A., Pfelzer, N., Zuijderwijk, R., and Punt, P. (2012) Enhanced itaconic acid production in Aspergillus niger using genetic modification and medium optimization. BMC Biotechnol 12: 57.
    • (2012) BMC Biotechnol , vol.12 , pp. 57
    • Li, A.1    Pfelzer, N.2    Zuijderwijk, R.3    Punt, P.4
  • 35
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(T)(-Delta Delta C) method
    • Livak, K.J., and Schmittgen, T.D. (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2(T)(-Delta Delta C) method. Methods 25: 402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 36
    • 0034999687 scopus 로고    scopus 로고
    • A homologue of the transcriptional repressor Ssn6p antagonizes cAMP signalling in Ustilago maydis
    • Loubradou, G., Brachmann, A., Feldbrugge, M., and Kahmann, R. (2001) A homologue of the transcriptional repressor Ssn6p antagonizes cAMP signalling in Ustilago maydis. Mol Microbiol 40: 719-730.
    • (2001) Mol Microbiol , vol.40 , pp. 719-730
    • Loubradou, G.1    Brachmann, A.2    Feldbrugge, M.3    Kahmann, R.4
  • 37
    • 84895929764 scopus 로고    scopus 로고
    • Influence of carbon and nitrogen concentration on itaconic acid production by the smut fungus Ustilago maydis
    • Maassen, N., Panakova, M., Wierckx, N., Geiser, E., Zimmermann, M., Bolker, M., etal. (2014) Influence of carbon and nitrogen concentration on itaconic acid production by the smut fungus Ustilago maydis. Eng Life Sci 14: 129-134.
    • (2014) Eng Life Sci , vol.14 , pp. 129-134
    • Maassen, N.1    Panakova, M.2    Wierckx, N.3    Geiser, E.4    Zimmermann, M.5    Bolker, M.6
  • 38
    • 0017404916 scopus 로고
    • Itaconate, an isocitrate lyase-directed inhibitor in Pseudomonas indigofera
    • McFadden, B.A., and Purohit, S. (1977) Itaconate, an isocitrate lyase-directed inhibitor in Pseudomonas indigofera. J Bacteriol 131: 136-144.
    • (1977) J Bacteriol , vol.131 , pp. 136-144
    • McFadden, B.A.1    Purohit, S.2
  • 39
    • 84877343356 scopus 로고    scopus 로고
    • Immune-responsive gene 1 protein links metabolism to immunity by catalyzing itaconic acid production
    • Michelucci, A., Cordes, T., Ghelfi, J., Pailot, A., Reiling, N., Goldmann, O., etal. (2013) Immune-responsive gene 1 protein links metabolism to immunity by catalyzing itaconic acid production. Proc Natl Acad Sci USA 110: 7820-7825.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 7820-7825
    • Michelucci, A.1    Cordes, T.2    Ghelfi, J.3    Pailot, A.4    Reiling, N.5    Goldmann, O.6
  • 40
    • 0040559975 scopus 로고    scopus 로고
    • 450 monooxygenase catalyzing phenylacetate 2-hydroxylation, results in penicillin overproduction
    • 450 monooxygenase catalyzing phenylacetate 2-hydroxylation, results in penicillin overproduction. J Biol Chem 274: 14545-14550.
    • (1999) J Biol Chem , vol.274 , pp. 14545-14550
    • Mingot, J.M.1    Penalva, M.A.2    Fernandez-Canon, J.M.3
  • 42
    • 69949136867 scopus 로고    scopus 로고
    • Biotechnological production of itaconic acid and its biosynthesis in Aspergillus terreus
    • Okabe, M., Lies, D., Kanamasa, S., and Park, E.Y. (2009) Biotechnological production of itaconic acid and its biosynthesis in Aspergillus terreus. Appl Microbiol Biotechnol 84: 597-606.
    • (2009) Appl Microbiol Biotechnol , vol.84 , pp. 597-606
    • Okabe, M.1    Lies, D.2    Kanamasa, S.3    Park, E.Y.4
  • 44
    • 0035890168 scopus 로고    scopus 로고
    • Modes of spindle pole body inheritance and segregation of the Bfa1p-Bub2p checkpoint protein complex
    • Pereira, G., Tanaka, T.U., Nasmyth, K., and Schiebel, E. (2001) Modes of spindle pole body inheritance and segregation of the Bfa1p-Bub2p checkpoint protein complex. EMBO J 20: 6359-6370.
    • (2001) EMBO J , vol.20 , pp. 6359-6370
    • Pereira, G.1    Tanaka, T.U.2    Nasmyth, K.3    Schiebel, E.4
  • 45
    • 0005916831 scopus 로고
    • Inhibition of aconitase by trans-aconitate
    • Saffran, M., and Prado, J.L. (1949) Inhibition of aconitase by trans-aconitate. J Biol Chem 180: 1301-1309.
    • (1949) J Biol Chem , vol.180 , pp. 1301-1309
    • Saffran, M.1    Prado, J.L.2
  • 47
    • 0025034813 scopus 로고
    • The b alleles of Ustilago maydis, whose combinations program pathogenic development, code for polypeptides containing a homeodomain-related motif
    • Schulz, B., Banuett, F., Dahl, M., Schlesinger, R., Schäfer, W., Martin, T., etal. (1990) The b alleles of Ustilago maydis, whose combinations program pathogenic development, code for polypeptides containing a homeodomain-related motif. Cell 60: 295-306.
    • (1990) Cell , vol.60 , pp. 295-306
    • Schulz, B.1    Banuett, F.2    Dahl, M.3    Schlesinger, R.4    Schäfer, W.5    Martin, T.6
  • 48
    • 33749424678 scopus 로고    scopus 로고
    • Proteomic analysis of Salmonella enterica serovar Typhimurium isolated from RAW 264.7 macrophages - identification of a novel protein that contributes to the replication of serovar Typhimurium inside macrophages
    • Shi, L., Adkins, J.N., Coleman, J.R., Schepmoes, A.A., Dohnkova, A., Mottaz, H.M., etal. (2006) Proteomic analysis of Salmonella enterica serovar Typhimurium isolated from RAW 264.7 macrophages - identification of a novel protein that contributes to the replication of serovar Typhimurium inside macrophages. J Biol Chem 281: 29131-29140.
    • (2006) J Biol Chem , vol.281 , pp. 29131-29140
    • Shi, L.1    Adkins, J.N.2    Coleman, J.R.3    Schepmoes, A.A.4    Dohnkova, A.5    Mottaz, H.M.6
  • 49
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R.S., and Hieter, P. (1989) A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122: 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 50
    • 0029962512 scopus 로고    scopus 로고
    • Green fluorescent protein (GFP) as a new vital marker in the phytopathogenic fungus Ustilago maydis
    • Spellig, T., Bottin, A., and Kahmann, R. (1996) Green fluorescent protein (GFP) as a new vital marker in the phytopathogenic fungus Ustilago maydis. Mol Genet Genomics 252: 503-509.
    • (1996) Mol Genet Genomics , vol.252 , pp. 503-509
    • Spellig, T.1    Bottin, A.2    Kahmann, R.3
  • 51
    • 84864053506 scopus 로고    scopus 로고
    • Non-targeted metabolite profiling in activated macrophage secretion
    • Sugimoto, M., Sakagami, H., Yokote, Y., Onuma, H., Kaneko, M., Mori, M., etal. (2012) Non-targeted metabolite profiling in activated macrophage secretion. Metabolomics 8: 624-633.
    • (2012) Metabolomics , vol.8 , pp. 624-633
    • Sugimoto, M.1    Sakagami, H.2    Yokote, Y.3    Onuma, H.4    Kaneko, M.5    Mori, M.6
  • 52
    • 0025017570 scopus 로고
    • Determination of aconitate isomerase in plants
    • Thompson, J.F., Schaefer, S.C., and Madison, J.T. (1990) Determination of aconitate isomerase in plants. Anal Biochem 184: 39-47.
    • (1990) Anal Biochem , vol.184 , pp. 39-47
    • Thompson, J.F.1    Schaefer, S.C.2    Madison, J.T.3
  • 53
    • 67651149462 scopus 로고    scopus 로고
    • Crystal structure and putative mechanism of 3-methylitaconate-delta-isomerase from Eubacterium barkeri
    • Velarde, M., Macieira, S., Hilberg, M., Broker, G., Tu, S.M., Golding, B.T., etal. (2009) Crystal structure and putative mechanism of 3-methylitaconate-delta-isomerase from Eubacterium barkeri. J Mol Biol 391: 609-620.
    • (2009) J Mol Biol , vol.391 , pp. 609-620
    • Velarde, M.1    Macieira, S.2    Hilberg, M.3    Broker, G.4    Tu, S.M.5    Golding, B.T.6
  • 55
    • 84953314190 scopus 로고    scopus 로고
    • Top value added chemicals from biomass. 2004 US-DoE report PNNL-16983.
    • Werpy, T. and Petersen, G. (2004). Top value added chemicals from biomass. 2004 US-DoE report PNNL-16983.
    • (2004)
    • Werpy, T.1    Petersen, G.2
  • 56
    • 77956672236 scopus 로고    scopus 로고
    • Growth promotion of plants inoculated with phosphate-solubilizing fungi
    • Sparks, D.L. (ed.). Waltham, MA, USA: Academic Press
    • Whitelaw, M.A. (1999) Growth promotion of plants inoculated with phosphate-solubilizing fungi. In Advances in Agronomy. Sparks, D.L. (ed.). Waltham, MA, USA: Academic Press, pp. 99-151.
    • (1999) Advances in Agronomy , pp. 99-151
    • Whitelaw, M.A.1
  • 57
    • 0026794264 scopus 로고
    • 3-carboxy-cis,cis-muconate lactonizing enzyme from Pseudomonas putida is homologous to the class-II fumarase family - a new reaction in the evolution of a mechanistic motif
    • Williams, S.E., Woolridge, E.M., Ransom, S.C., Landro, J.A., Babbitt, P.C., and Kozarich, J.W. (1992) 3-carboxy-cis, cis-muconate lactonizing enzyme from Pseudomonas putida is homologous to the class-II fumarase family - a new reaction in the evolution of a mechanistic motif. Biochemistry 31: 9768-9776.
    • (1992) Biochemistry , vol.31 , pp. 9768-9776
    • Williams, S.E.1    Woolridge, E.M.2    Ransom, S.C.3    Landro, J.A.4    Babbitt, P.C.5    Kozarich, J.W.6
  • 58
    • 0034886321 scopus 로고    scopus 로고
    • Biotechnological production of itaconic acid
    • Willke, T., and Vorlop, K.D. (2001) Biotechnological production of itaconic acid. Appl Microbiol Biotechnol 56: 289-295.
    • (2001) Appl Microbiol Biotechnol , vol.56 , pp. 289-295
    • Willke, T.1    Vorlop, K.D.2
  • 59
    • 4043057880 scopus 로고    scopus 로고
    • Crystal structure of 3-carboxy-cis,cis-muconate lactonizing enzyme from Pseudomonas putida, a fumarase class II type cycloisomerase: enzyme evolution in parallel pathways
    • Yang, J., Wang, Y., Woolridge, E.M., Arora, V., Petsko, G.A., Kozarich, J.W., and Ringe, D. (2004) Crystal structure of 3-carboxy-cis, cis-muconate lactonizing enzyme from Pseudomonas putida, a fumarase class II type cycloisomerase: enzyme evolution in parallel pathways. Biochemistry 43: 10424-10434.
    • (2004) Biochemistry , vol.43 , pp. 10424-10434
    • Yang, J.1    Wang, Y.2    Woolridge, E.M.3    Arora, V.4    Petsko, G.A.5    Kozarich, J.W.6    Ringe, D.7
  • 60
    • 33646445156 scopus 로고    scopus 로고
    • Structure of the multidrug transporter EmrD from Escherichia coli
    • Yin, Y., He, X., Szewczyk, P., Nguyen, T., and Chang, G. (2006) Structure of the multidrug transporter EmrD from Escherichia coli. Science 312: 741-744.
    • (2006) Science , vol.312 , pp. 741-744
    • Yin, Y.1    He, X.2    Szewczyk, P.3    Nguyen, T.4    Chang, G.5
  • 61
    • 44249103047 scopus 로고    scopus 로고
    • The Ustilago maydis Cys(2)His(2)-type zinc finger transcription factor Mzr1 regulates fungal gene expression during the biotrophic growth stage
    • Zheng, Y., Kief, J., Auffarth, K., Farfsing, J.W., Mahlert, M., Nieto, F., and Basse, C.W. (2008) The Ustilago maydis Cys(2)His(2)-type zinc finger transcription factor Mzr1 regulates fungal gene expression during the biotrophic growth stage. Mol Microbiol 68: 1450-1470.
    • (2008) Mol Microbiol , vol.68 , pp. 1450-1470
    • Zheng, Y.1    Kief, J.2    Auffarth, K.3    Farfsing, J.W.4    Mahlert, M.5    Nieto, F.6    Basse, C.W.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.