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Volumn 185, Issue 1, 2003, Pages 41-50

Characterization of the 4-carboxy-4-hydroxy-2-oxoadipate aldolase gene and operon structure of the protocatechuate 4,5-cleavage pathway genes in Sphingomonas paucimobilis SYK-6

Author keywords

[No Author keywords available]

Indexed keywords

4 CARBOXY 4 HYDROXY 2 OXOADIPATE ALDOLASE; BACTERIAL ENZYME; UNCLASSIFIED DRUG;

EID: 0037215527     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.1.41-50.2003     Document Type: Article
Times cited : (50)

References (51)
  • 2
    • 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
  • 3
    • 0033754309 scopus 로고    scopus 로고
    • Key aromaticring-cleaving enzyme, protocatechuate 3,4-dioxygenase, in the ecologically important marine Roseobacter lineage
    • Buchan, A., L. S. Collier, E. L. Neidle, and M. A. Moran. 2000. Key aromaticring-cleaving enzyme, protocatechuate 3,4-dioxygenase, in the ecologically important marine Roseobacter lineage. Appl. Environ. Microbiol. 66:4662-4672.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 4662-4672
    • Buchan, A.1    Collier, L.S.2    Neidle, E.L.3    Moran, M.A.4
  • 4
    • 0033763853 scopus 로고    scopus 로고
    • Characterization of the genes for two protocatechuate 3,4-dioxygenases from the 4-sulfocatechol-degrading bacterium Agrobacterium radiobacter strain S2
    • Contzen, M., and A. Stolz. 2000. Characterization of the genes for two protocatechuate 3,4-dioxygenases from the 4-sulfocatechol-degrading bacterium Agrobacterium radiobacter strain S2. J. Bacteriol. 182:6123-6129.
    • (2000) J. Bacteriol. , vol.182 , pp. 6123-6129
    • Contzen, M.1    Stolz, A.2
  • 5
    • 0026576795 scopus 로고
    • Cloning and sequencing of Pseudomonas genes determining sodium dodecyl sulfate biodegradation
    • Davison, J., F. Brunel, A. Phanopoulos, D. Prozzi, and P. Terpstra. 1992. Cloning and sequencing of Pseudomonas genes determining sodium dodecyl sulfate biodegradation. Gene 114:19-24.
    • (1992) Gene , vol.114 , pp. 19-24
    • Davison, J.1    Brunel, F.2    Phanopoulos, A.3    Prozzi, D.4    Terpstra, P.5
  • 6
    • 0034991776 scopus 로고    scopus 로고
    • Plasmid-encoded phthalate catabolic pathway in Arthrobacter keyseri 12B
    • Eaton, R. W. 2001. Plasmid-encoded phthalate catabolic pathway in Arthrobacter keyseri 12B. J. Bacteriol. 183:3689-3703.
    • (2001) J. Bacteriol. , vol.183 , pp. 3689-3703
    • Eaton, R.W.1
  • 7
    • 0031909725 scopus 로고    scopus 로고
    • Characterization of a protocatechuate catabolic gene cluster from Rhodococcus opacus 1CP: Evidence for a merged enzyme with 4-carboxymuconolactonedecarboxylating and 3-oxoadipate enol-lactone-hydrolyzing activity
    • Eulberg, D., S. Lakner, L. A. Golovleva, and M. Schlömann. 1998. Characterization of a protocatechuate catabolic gene cluster from Rhodococcus opacus 1CP: Evidence for a merged enzyme with 4-carboxymuconolactonedecarboxylating and 3-oxoadipate enol-lactone-hydrolyzing activity. J. Bacteriol. 180:1072-1081.
    • (1998) J. Bacteriol. , vol.180 , pp. 1072-1081
    • Eulberg, D.1    Lakner, S.2    Golovleva, L.A.3    Schlömann, M.4
  • 9
    • 0027508335 scopus 로고
    • Cloning, sequencing, and expression of the Pseudomonas putida protocatechuate 3,4-dioxygenase genes
    • Frazee, R. W., D. M. Livingston, D. C. LaPorte, and J. D. Lipscomb. 1993. Cloning, sequencing, and expression of the Pseudomonas putida protocatechuate 3,4-dioxygenase genes. J. Bacteriol. 175:6194-6202.
    • (1993) J. Bacteriol. , vol.175 , pp. 6194-6202
    • Frazee, R.W.1    Livingston, D.M.2    LaPorte, D.C.3    Lipscomb, J.D.4
  • 10
    • 0031938056 scopus 로고    scopus 로고
    • PcaU, a transcriptional activator of genes for protocatechuate utilization in Acinetobacter
    • Gerischer, U., A. Segura, and L. N. Ornston. 1998. PcaU, a transcriptional activator of genes for protocatechuate utilization in Acinetobacter. J. Bacteriol. 180:1512-1524.
    • (1998) J. Bacteriol. , vol.180 , pp. 1512-1524
    • Gerischer, U.1    Segura, A.2    Ornston, L.N.3
  • 11
    • 0034459639 scopus 로고    scopus 로고
    • The 4-oxalomesaconate hydratase gene, involved in the protocatechuate 4,5-cleavage pathway, is essential to vanillate and syringate degradation in Sphingomonas paucimobilis SYK-6
    • Hara, H., E. Masai, Y. Katayama, and M. Fukuda. 2000. The 4-oxalomesaconate hydratase gene, involved in the protocatechuate 4,5-cleavage pathway, is essential to vanillate and syringate degradation in Sphingomonas paucimobilis SYK-6. J. Bacteriol. 182:6950-6957.
    • (2000) J. Bacteriol. , vol.182 , pp. 6950-6957
    • Hara, H.1    Masai, E.2    Katayama, Y.3    Fukuda, M.4
  • 12
    • 0025056536 scopus 로고
    • DNA sequences of genes encoding Acinetobacter calcoaceticus protocatechuate 3,4-dioxygenase: Evidence indicating shuffling of genes and of DNA sequences within genes during their evolutionally divergence
    • Hartnett, C., E. L. Neidle, K. L. Ngai, and L. N. Ornston. 1990. DNA sequences of genes encoding Acinetobacter calcoaceticus protocatechuate 3,4-dioxygenase: Evidence indicating shuffling of genes and of DNA sequences within genes during their evolutionally divergence. J. Bacteriol. 172:956-966.
    • (1990) J. Bacteriol. , vol.172 , pp. 956-966
    • Hartnett, C.1    Neidle, E.L.2    Ngai, K.L.3    Ornston, L.N.4
  • 13
    • 0029795374 scopus 로고    scopus 로고
    • The β-ketoadipate pathway and the biology of self-identity
    • Harwood, C. S., and R. E. Parales. 1996. The β-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
  • 14
    • 0034087467 scopus 로고    scopus 로고
    • Characterization of the protocatechuic acid catabolic gene cluster from Streptomyces sp. strain 2065
    • Iwagami, S. G., K. Yang, and J. Davies. 2000. Characterization of the protocatechuic acid catabolic gene cluster from Streptomyces sp. strain 2065. Appl. Environ. Microbiol. 66:1499-1508.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 1499-1508
    • Iwagami, S.G.1    Yang, K.2    Davies, J.3
  • 15
    • 0001830934 scopus 로고
    • Cloning and expression of Pseudomonas paucimobilis SYK-6 genes involved in the degradation of vanillate and protocatechuate in P. putida
    • Katayama, Y., S. Nishikawa, M. Nakamura, K. Yano, M. Yamasaki, N. Morohoshi, and T. Haraguchi. 1987. Cloning and expression of Pseudomonas paucimobilis SYK-6 genes involved in the degradation of vanillate and protocatechuate in P. putida. Mokuzai Gakkaisi 33:77-79.
    • (1987) Mokuzai Gakkaisi , vol.33 , pp. 77-79
    • Katayama, Y.1    Nishikawa, S.2    Nakamura, M.3    Yano, K.4    Yamasaki, M.5    Morohoshi, N.6    Haraguchi, T.7
  • 16
    • 0020465543 scopus 로고
    • 2-Pyrone-4,6-dicarboxylic acid, a catabolite of gallic acids in Pseudomonas species
    • Kersten, P. J., S. Dagley, J. W. Whittaker, D. M. Arciero, and J. D. Lipscomb. 1982. 2-Pyrone-4,6-dicarboxylic acid, a catabolite of gallic acids in Pseudomonas species. J. Bacteriol. 152:1154-1162.
    • (1982) J. Bacteriol. , vol.152 , pp. 1154-1162
    • Kersten, P.J.1    Dagley, S.2    Whittaker, J.W.3    Arciero, D.M.4    Lipscomb, J.D.5
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0018621990 scopus 로고
    • Isolation and identification of the reaction product of α-hydroxy-γ-carboxymuconic-ε-semialdehyde dehydrogenase
    • Maruyama, K. 1979. Isolation and identification of the reaction product of α-hydroxy-γ-carboxymuconic-ε-semialdehyde dehydrogenase. J. Biochem. 86:1671-1677.
    • (1979) J. Biochem. , vol.86 , pp. 1671-1677
    • Maruyama, K.1
  • 19
    • 0020710193 scopus 로고
    • Purification and properties of 2-pyrone-4,6-dicarboxylate hydrolase
    • Maruyama, K. 1983. Purification and properties of 2-pyrone-4,6-dicarboxylate hydrolase. J. Biochem. 93:557-565.
    • (1983) J. Biochem. , vol.93 , pp. 557-565
    • Maruyama, K.1
  • 20
    • 0022410180 scopus 로고
    • Purification and properties of α-oxalomesaconate hydratase from Pseudomonas ochraceae grown with phthalate
    • Maruyama, K. 1985. Purification and properties of α-oxalomesaconate hydratase from Pseudomonas ochraceae grown with phthalate. Biochem. Biophys. Res. Commun. 128:271-277.
    • (1985) Biochem. Biophys. Res. Commun. , vol.128 , pp. 271-277
    • Maruyama, K.1
  • 21
    • 0025348317 scopus 로고
    • Purification and properties of 4-hydroxy-4-methyl-2-oxoglutarate aldolase from Pseudomonas ochraceae grown on phthalate
    • Maruyama, K. 1990. Purification and properties of 4-hydroxy-4-methyl-2-oxoglutarate aldolase from Pseudomonas ochraceae grown on phthalate. J. Biochem. 108:327-333.
    • (1990) J. Biochem. , vol.108 , pp. 327-333
    • Maruyama, K.1
  • 22
    • 0017854725 scopus 로고
    • Purification and properties of α-hydroxy-γ-carboxymuconic-ε-semialdehyde dehydrogenase
    • Maruyama, K., N. Ariga, M. Tsuda, and K. Deguchi. 1978. Purification and properties of α-hydroxy-γ-carboxymuconic-ε-semialdehyde dehydrogenase. J. Biochem. 83:1125-1134.
    • (1978) J. Biochem. , vol.83 , pp. 1125-1134
    • Maruyama, K.1    Ariga, N.2    Tsuda, M.3    Deguchi, K.4
  • 23
    • 0035751609 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of the gene encoding 4-hydroxy-4-methyl-2-oxoglutarate aldolase from Pseudomonas ochraceae NGJ1
    • Maruyama, K., M. Miwa, N. Tsujii, T. Nagai, N. Tomita, T. Harada, H. Sobajima, and H. Sugisaki. 2001. Cloning, sequencing, and expression of the gene encoding 4-hydroxy-4-methyl-2-oxoglutarate aldolase from Pseudomonas ochraceae NGJ1. Biosci. Biotechnol. Biochem. 65:2701-2709.
    • (2001) Biosci. Biotechnol. Biochem. , vol.65 , pp. 2701-2709
    • Maruyama, K.1    Miwa, M.2    Tsujii, N.3    Nagai, T.4    Tomita, N.5    Harada, T.6    Sobajima, H.7    Sugisaki, H.8
  • 24
    • 0026340042 scopus 로고
    • Cloning and sequencing of the gene for a Pseudomonas paucimobilis enzyme that cleaves β-aryl ether
    • Masai, E., Y. Katayama, S. Kawai, S. Nishikawa, M. Yamasaki, and N. Morohoshi. 1991. Cloning and sequencing of the gene for a Pseudomonas paucimobilis enzyme that cleaves β-aryl ether. J. Bacteriol. 173:7950-7955.
    • (1991) J. Bacteriol. , vol.173 , pp. 7950-7955
    • Masai, E.1    Katayama, Y.2    Kawai, S.3    Nishikawa, S.4    Yamasaki, M.5    Morohoshi, N.6
  • 25
    • 0027223168 scopus 로고
    • A bacterial enzyme degrading the model lignin compound β-etherase is a member of the glutathione-S-transferase superfamily
    • Masai, E., Y. Katayama, S. Kubota, S. Kawai, M. Yamasaki, and N. Morohoshi. 1993. A bacterial enzyme degrading the model lignin compound β-etherase is a member of the glutathione-S-transferase superfamily. FEBS Lett. 323:135-140.
    • (1993) FEBS Lett. , vol.323 , pp. 135-140
    • Masai, E.1    Katayama, Y.2    Kubota, S.3    Kawai, S.4    Yamasaki, M.5    Morohoshi, N.6
  • 26
    • 0033383704 scopus 로고    scopus 로고
    • Characterization of Sphingomonas paucimobilis SYK-6 genes involved in degradation of lignin-related compounds
    • Masai, E., Y. Katayama, S. Nishikawa, and M. Fukuda. 1999. Characterization of Sphingomonas paucimobilis SYK-6 genes involved in degradation of lignin-related compounds. J. Ind. Microbiol. Biotechnol. 23:364-373.
    • (1999) J. Ind. Microbiol. Biotechnol. , vol.23 , pp. 364-373
    • Masai, E.1    Katayama, Y.2    Nishikawa, S.3    Fukuda, M.4
  • 27
    • 0034462107 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase and its role in the protocatechuate 4,5-cleavage pathway in Sphingomonas paucimobilis SYK-6
    • Masai, E., K. Momose, H. Hara, S. Nishikawa, Y. Katayama, and M. Fukuda. 2000. Genetic and biochemical characterization of 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase and its role in the protocatechuate 4,5-cleavage pathway in Sphingomonas paucimobilis SYK-6. J. Bacteriol. 182:6651-6658.
    • (2000) J. Bacteriol. , vol.182 , pp. 6651-6658
    • Masai, E.1    Momose, K.2    Hara, H.3    Nishikawa, S.4    Katayama, Y.5    Fukuda, M.6
  • 28
    • 0032934359 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of a 2-pyrone-4,6-dicarboxylic acid hydrolase involved in the protocatechuate 4,5-cleavage pathway of Sphingomonas paucimobilis SYK-6
    • Masai, E., S. Shinohara, H. Hara, S. Nishikawa, Y. Katayama, and M. Fukuda. 1999. Genetic and biochemical characterization of a 2-pyrone-4,6-dicarboxylic acid hydrolase involved in the protocatechuate 4,5-cleavage pathway of Sphingomonas paucimobilis SYK-6. J. Bacteriol. 181:55-62.
    • (1999) J. Bacteriol. , vol.181 , pp. 55-62
    • Masai, E.1    Shinohara, S.2    Hara, H.3    Nishikawa, S.4    Katayama, Y.5    Fukuda, M.6
  • 29
    • 0015523608 scopus 로고
    • Purification, substrate specificity and binding, β-decarboxylase activity, and other properties of Escherichia coli 2-keto-4-hydroxyglutarate aldolase
    • Nishihara, H., and E. E. Dekker. 1972. Purification, substrate specificity and binding, β-decarboxylase activity, and other properties of Escherichia coli 2-keto-4-hydroxyglutarate aldolase. J. Biol. Chem. 247:5079-5087.
    • (1972) J. Biol. Chem. , vol.247 , pp. 5079-5087
    • Nishihara, H.1    Dekker, E.E.2
  • 30
    • 0031885226 scopus 로고    scopus 로고
    • Cloning and sequencing of the Sphingomonas (Pseudomonas)paucimobilis gene essential for the O demethylation of vanillate and syringate
    • Nishikawa, S., T. Sonoki, T. Kasahara, T. Obi, S. Kubota, S. Kawai, N. Morohoshi, and Y. Katayama. 1998. Cloning and sequencing of the Sphingomonas (Pseudomonas)paucimobilis gene essential for the O demethylation of vanillate and syringate. Appl. Environ. Microbiol. 64:836-842.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 836-842
    • Nishikawa, S.1    Sonoki, T.2    Kasahara, T.3    Obi, T.4    Kubota, S.5    Kawai, S.6    Morohoshi, N.7    Katayama, Y.8
  • 32
    • 0031017926 scopus 로고    scopus 로고
    • Acquisition, reorganization, and merger of genes: Novel management of the β-ketoadipate pathway in Agrobacterium tumefaciens
    • Parke, D. 1997. Acquisition, reorganization, and merger of genes: Novel management of the β-ketoadipate pathway in Agrobacterium tumefaciens. FEMS Microbiol. Lett. 146:3-12.
    • (1997) FEMS Microbiol. Lett. , vol.146 , pp. 3-12
    • Parke, D.1
  • 33
    • 0031869637 scopus 로고    scopus 로고
    • Cloning of a Sphingomonas paucimobilis SYK-6 gene encoding a novel oxygenase that cleaves lignin-related biphenyl and characterization of the enzyme
    • Peng, X., T. Egashira, K. Hanashiro, E. Masai, S. Nishikawa, Y. Katayama, K. Kimbara, and M. Fukuda. 1998. Cloning of a Sphingomonas paucimobilis SYK-6 gene encoding a novel oxygenase that cleaves lignin-related biphenyl and characterization of the enzyme. Appl. Environ. Microbiol. 64:2520-2527.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 2520-2527
    • Peng, X.1    Egashira, T.2    Hanashiro, K.3    Masai, E.4    Nishikawa, S.5    Katayama, Y.6    Kimbara, K.7    Fukuda, M.8
  • 34
    • 0032978661 scopus 로고    scopus 로고
    • Characterization of the meta-cleavage compound hydrolase gene involved in degradation of the lignin-related biphenyl structure by Sphingomonas paucimobilis SYK-6
    • Peng, X., E. Masai, Y. Katayama, and M. Fukuda. 1999. Characterization of the meta-cleavage compound hydrolase gene involved in degradation of the lignin-related biphenyl structure by Sphingomonas paucimobilis SYK-6. Appl. Environ. Microbiol. 65:2789-2793.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 2789-2793
    • Peng, X.1    Masai, E.2    Katayama, Y.3    Fukuda, M.4
  • 35
    • 0036203062 scopus 로고    scopus 로고
    • Differential DNA biding of transcriptional regulator PcaU from Acinetobacter sp. strain ADP1
    • Popp, R., T. Kohl, P. Patz, G. Trautwein, and U. Gerischer. 2002. Differential DNA biding of transcriptional regulator PcaU from Acinetobacter sp. strain ADP1. J. Bacteriol. 184:1988-1997.
    • (2002) J. Bacteriol. , vol.184 , pp. 1988-1997
    • Popp, R.1    Kohl, T.2    Patz, P.3    Trautwein, G.4    Gerischer, U.5
  • 36
    • 0034858327 scopus 로고    scopus 로고
    • Comamonas testosteroni BR6020 possesses a single genetic locus for extradiol cleavage of protocatechuate
    • Providenti, M. A., J. Mampel, S, MacSween, A. M. Cook, and R. C. Wyndham. 2001. Comamonas testosteroni BR6020 possesses a single genetic locus for extradiol cleavage of protocatechuate. Microbiology 147:2157-2167.
    • (2001) Microbiology , vol.147 , pp. 2157-2167
    • Providenti, M.A.1    Mampel, J.2    MacSween, S.3    Cook, A.M.4    Wyndham, R.C.5
  • 37
    • 0001097975 scopus 로고
    • Preparation and properties of yeast aldolase
    • Richards, O. C., and W. J. Rutter, 1961. Preparation and properties of yeast aldolase. J. Biol. Chem. 236:3177-3184.
    • (1961) J. Biol. Chem. , vol.236 , pp. 3177-3184
    • Richards, O.C.1    Rutter, W.J.2
  • 40
    • 0028289983 scopus 로고
    • Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: Selection of defined deletions in the chromosome of Corynebacterium glutamicum
    • Schäfer, A., A. Tauch, W. Jäger, J. Kalinowski, G. Thierbach, and A. Pühler. 1994. Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: Selection of defined deletions in the chromosome of Corynebacterium glutamicum. Gene 145:69-73.
    • (1994) Gene , vol.145 , pp. 69-73
    • Schäfer, A.1    Tauch, A.2    Jäger, W.3    Kalinowski, J.4    Thierbach, G.5    Pühler, A.6
  • 41
    • 0027446708 scopus 로고
    • Molecular biology of the LysR family of transcriptional regulators
    • Schell, M. A. 1993. Molecular biology of the LysR family of transcriptional regulators. Annu. Rev. Microbiol. 47:597-626.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 597-626
    • Schell, M.A.1
  • 42
    • 0024284551 scopus 로고
    • λZAP: A bacteriophage λ expression vector with in vivo excision properties
    • Short, J. M., J. M. Fernandez, J. A. Sorge, and W. Huse. 1988. λZAP: A bacteriophage λ expression vector with in vivo excision properties. Nucleic Acids Res. 16:7583-7600.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 7583-7600
    • Short, J.M.1    Fernandez, J.M.2    Sorge, J.A.3    Huse, W.4
  • 43
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier, F. W., and B. A. Moffatt. 1986. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189:113-130.
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 44
    • 0033566802 scopus 로고    scopus 로고
    • Crystal structure of an aromatic ring opening dioxygenase LigAB which is a protocatechuate 4,5-dioxygenase
    • Sugimoto, K., T. Senda, H. Aoshima, E. Masai, M. Fukuda, and Y. Mitsui. 1999. Crystal structure of an aromatic ring opening dioxygenase LigAB which is a protocatechuate 4,5-dioxygenase. Struct. Fold. Des. 15:953-965.
    • (1999) Struct. Fold. Des. , vol.15 , pp. 953-965
    • Sugimoto, K.1    Senda, T.2    Aoshima, H.3    Masai, E.4    Fukuda, M.5    Mitsui, Y.6
  • 45
    • 0015523862 scopus 로고
    • Purification and properties of 4-hydroxy-4-methyl-2-oxoglutarate aldolase
    • Tack, B. F., P. J. Chapman, and S. Dagley. 1972. Purification and properties of 4-hydroxy-4-methyl-2-oxoglutarate aldolase. J. Biol. Chem. 247:6444-6449.
    • (1972) J. Biol. Chem. , vol.247 , pp. 6444-6449
    • Tack, B.F.1    Chapman, P.J.2    Dagley, S.3
  • 46
    • 0035153271 scopus 로고    scopus 로고
    • Effects exerted by transcriptional regulator PcaU from Acinetobacter sp. strain ADP1
    • Trautwein, G., and U. Gerischer. 2001. Effects exerted by transcriptional regulator PcaU from Acinetobacter sp. strain ADP1. J. Bacteriol. 183:873-881.
    • (2001) J. Bacteriol. , vol.183 , pp. 873-881
    • Trautwein, G.1    Gerischer, U.2
  • 47
    • 0020442864 scopus 로고
    • The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers
    • Vieira, J., and J. Messing. 1982. The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers. Gene 19:259-268.
    • (1982) Gene , vol.19 , pp. 259-268
    • Vieira, J.1    Messing, J.2
  • 49
    • 0027293730 scopus 로고
    • Purification and characterization of protocatechuate 2,3-dioxygenase from Bacillus macerans: A new extradiol catecholic dioxygenase
    • Wolgel, S. A., J. E. Dege, P. E. Perkins-Olson, C. H. Jaurez-Garcia, R. L. Crawford, E. Münck. and J. D. Lipscomb. 1993. Purification and characterization of protocatechuate 2,3-dioxygenase from Bacillus macerans: A new extradiol catecholic dioxygenase. J. Bacteriol. 175:4414-4426.
    • (1993) J. Bacteriol. , vol.175 , pp. 4414-4426
    • Wolgel, S.A.1    Dege, J.E.2    Perkins-Olson, P.E.3    Jaurez-Garcia, C.H.4    Crawford, R.L.5    Münck, E.6    Lipscomb, J.D.7
  • 50
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 51
    • 0024465719 scopus 로고
    • Genetic organization and sequence of the Pseudomonas cepacia genes for the alpha and beta subunits of protocatechuate 3,4-dioxygenase
    • Zylstra, G. J., R. H. Olsen, and D. P. Ballou. 1989. Genetic organization and sequence of the Pseudomonas cepacia genes for the alpha and beta subunits of protocatechuate 3,4-dioxygenase. J. Bacteriol. 171:5915-5921.
    • (1989) J. Bacteriol. , vol.171 , pp. 5915-5921
    • Zylstra, G.J.1    Olsen, R.H.2    Ballou, D.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.