메뉴 건너뛰기




Volumn 191, Issue 21, 2009, Pages 6758-6768

Uncovering the protocatechuate 2,3-cleavage pathway genes

Author keywords

[No Author keywords available]

Indexed keywords

2 HYDROXYMUCONATE 6 SEMIALDEHYDE DEHYDROGENASE; 2 HYDROXYPENTA 2,4 DIENOATE; 2,3 DIOXYGENASE; 3 OXYGENASE; 4 HYDROXYBENZOIC ACID; 4 OXALOCROTONATE DECARBOXYLASE; 4 OXALOCROTONATE TAUTOMERASE; 5 CARBOXY 2 HYDROXYMUCONATE 6 SEMIALDEHYDE DECARBOXYLASE; BACTERIAL PROTEIN; CELL EXTRACT; OXYGENASE; PROTOCATECHUATE 2,3; RNA 16S; UNCLASSIFIED DRUG;

EID: 70350445534     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00840-09     Document Type: Article
Times cited : (88)

References (67)
  • 1
    • 14644431741 scopus 로고    scopus 로고
    • A tetrahydrofolate-dependent O-demethylase, LigM, is crucial for catabolism of vanillate and syringate in Sphingomonas paucimobilis SYK-6
    • Abe, T., E. Masai, K. Miyauchi, Y. Katayama, and M. Fukuda. 2005. A tetrahydrofolate-dependent O-demethylase, LigM, is crucial for catabolism of vanillate and syringate in Sphingomonas paucimobilis SYK-6. J. Bacteriol. 187:2030-2037.
    • (2005) J. Bacteriol. , vol.187 , pp. 2030-2037
    • Abe, T.1    Masai, E.2    Miyauchi, K.3    Katayama, Y.4    Fukuda, M.5
  • 2
    • 3242813728 scopus 로고    scopus 로고
    • The homogentisate pathway: A central catabolic pathway involved in the degradation of L-phenylalanine, L-tyrosine, and 3-hydroxyphenylacetate in Pseudomonas putida
    • Arias-Barrau, E., E. R. Olivera, J. M. Luengo, C. Fernández, B. Galán, J. L. García, E. Díaz, and B. Miñambres. 2004. The homogentisate pathway: a central catabolic pathway involved in the degradation of L-phenylalanine, L-tyrosine, and 3-hydroxyphenylacetate in Pseudomonas putida. J. Bacteriol. 186:5062-5077.
    • (2004) J. Bacteriol. , vol.186 , pp. 5062-5077
    • Arias-Barrau, E.1    Olivera, E.R.2    Luengo, J.M.3    Fernández, C.4    Galán, B.5    García, J.L.6    Díaz, E.7    Miñambres, B.8
  • 3
    • 0028276797 scopus 로고
    • Analysis of three 2,3-dihydroxybiphenyl 1,2-dioxygenases found in Rhodococcus globerulus P6. Identification of a new family of extradiol dioxygenases
    • Asturias, J. A., L. D. Eltis, M. Prucha, and K. N. Timmis. 1994. Analysis of three 2,3-dihydroxybiphenyl 1,2-dioxygenases found in Rhodococcus globerulus P6. Identification of a new family of extradiol dioxygenases. J. Biol. Chem. 269:7807-7815.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7807-7815
    • Asturias, J.A.1    Eltis, L.D.2    Prucha, M.3    Timmis, K.N.4
  • 4
    • 0024806267 scopus 로고
    • Nucleotide sequence and expression of the catechol 2,3-dioxygenase- encoding gene of phenol-catabolizing Pseudomonas CF600
    • Bartilson, M., and V. Shingler. 1989. Nucleotide sequence and expression of the catechol 2,3-dioxygenase-encoding gene of phenol-catabolizing Pseudomonas CF600. Gene 85:233-238.
    • (1989) Gene , vol.85 , pp. 233-238
    • Bartilson, M.1    Shingler, V.2
  • 5
    • 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
  • 7
    • 0016433894 scopus 로고
    • Novel pathway for degradation of protocatechuic acid in Bacillus species
    • Crawford, R. L. 1975. Novel pathway for degradation of protocatechuic acid in Bacillus species. J. Bacteriol. 121:531-536.
    • (1975) J. Bacteriol. , vol.121 , pp. 531-536
    • Crawford, R.L.1
  • 8
    • 0017077975 scopus 로고
    • Pathways of 4-hydroxybenzoate degradation among species of Bacillus
    • Crawford, R. L. 1976. Pathways of 4-hydroxybenzoate degradation among species of Bacillus. J. Bacteriol. 127:204-210.
    • (1976) J. Bacteriol. , vol.127 , pp. 204-210
    • Crawford, R.L.1
  • 10
    • 13544251411 scopus 로고    scopus 로고
    • Transcriptional organization of genes for protocatechuate and quinate degradation from Acinetobacter sp. strain ADP1
    • Dal, S., G. Trautwein, and U. Gerischer. 2005. Transcriptional organization of genes for protocatechuate and quinate degradation from Acinetobacter sp. strain ADP1. Appl. Environ. Microbiol. 71:1025-1034.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 1025-1034
    • Dal, S.1    Trautwein, G.2    Gerischer, U.3
  • 11
    • 0027321256 scopus 로고
    • Identification of the transcriptional activator pobR and characterization of its role in the expression of pobA, the structural gene for p-hydroxybenzoate hydroxylase in Acinetobacter calcoaceticus
    • DiMarco, A. A., B. Averhoff, and L. N. Ornston. 1993. Identification of the transcriptional activator pobR and characterization of its role in the expression of pobA, the structural gene for p-hydroxybenzoate hydroxylase in Acinetobacter calcoaceticus. J. Bacteriol. 175:4499-4506.
    • (1993) J. Bacteriol. , vol.175 , pp. 4499-4506
    • DiMarco, A.A.1    Averhoff, B.2    Ornston, L.N.3
  • 13
    • 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
  • 14
    • 0029846961 scopus 로고    scopus 로고
    • Evolutionary relationships among extradiol dioxygenases
    • Eltis, L. D., and J. T. Bolin. 1996. Evolutionary relationships among extradiol dioxygenases. J. Bacteriol. 178:5930-5937.
    • (1996) J. Bacteriol. , vol.178 , pp. 5930-5937
    • Eltis, L.D.1    Bolin, J.T.2
  • 16
    • 0032054604 scopus 로고    scopus 로고
    • Lys42 and Ser42 variants of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens reveal that Arg42 is essential for NADPH binding
    • Eppink, M. H., H. A. Schreuder, and W. J. van Berkel. 1998. Lys42 and Ser42 variants of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens reveal that Arg42 is essential for NADPH binding. Eur. J. Biochem. 253:194-201.
    • (1998) Eur. J. Biochem. , vol.253 , pp. 194-201
    • Eppink, M.H.1    Schreuder, H.A.2    Van Berkel, W.J.3
  • 17
    • 0025370615 scopus 로고
    • Construction of broad-host-range plasmid vectors for easy visible selection and analysis of promoters
    • Farinha, M. A., and A. M. Kropinski. 1990. Construction of broad-host-range plasmid vectors for easy visible selection and analysis of promoters. J. Bacteriol. 172:3496-3499. (Pubitemid 20179813)
    • (1990) Journal of Bacteriology , vol.172 , Issue.6 , pp. 3496-3499
    • Farinha, M.A.1    Kropinski, A.M.2
  • 18
    • 0005536404 scopus 로고
    • Molecular and functional analysis of the TOL plasmid pWWO from Pseudomonas putida and cloning of genes for the entire regulated aromatic ring meta cleavage pathway
    • Franklin, F. C., M. Bagdasarian, M. M. Bagdasarian, and K. N. Timmis. 1981. Molecular and functional analysis of the TOL plasmid pWWO from Pseudomonas putida and cloning of genes for the entire regulated aromatic ring meta cleavage pathway. Proc. Natl. Acad. Sci. USA 78:7458-7462.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 7458-7462
    • Franklin, F.C.1    Bagdasarian, M.2    Bagdasarian, M.M.3    Timmis, K.N.4
  • 19
    • 0037144592 scopus 로고    scopus 로고
    • Identification and expression of a cDNA encoding human α-amino-β-carboxymuconate-ε-semialdehyde decarboxylase (ACMSD). A key enzyme for the tryptophan-niacine pathway and "quinolinate hypothesis"
    • Fukuoka, S., K. Ishiguro, K. Yanagihara, A. Tanabe, Y. Egashira, H. Sanada, and K. Shibata. 2002. Identification and expression of a cDNA encoding human α-amino-β-carboxymuconate-ε-semialdehyde decarboxylase (ACMSD). A key enzyme for the tryptophan-niacine pathway and "quinolinate hypothesis". J. Biol. Chem. 277:35162-35167.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35162-35167
    • Fukuoka, S.1    Ishiguro, K.2    Yanagihara, K.3    Tanabe, A.4    Egashira, Y.5    Sanada, H.6    Shibata, K.7
  • 20
    • 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
  • 21
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. 1983. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166:557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 22
    • 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
    • DOI 10.1128/JB.182.24.6950-6957.2000
    • 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. (Pubitemid 32259598)
    • (2000) Journal of Bacteriology , vol.182 , Issue.24 , pp. 6950-6957
    • Hara, H.1    Masai, E.2    Katayama, Y.3    Fukuda, M.4
  • 23
    • 0021124798 scopus 로고
    • Transposon mutagenesis analysis of meta-cleavage pathway operon genes of the TOL plasmid of Pseudomonas putida mt-2
    • Harayama, S., P. R. Lehrbach, and K. N. Timmis. 1984. Transposon mutagenesis analysis of meta-cleavage pathway operon genes of the TOL plasmid of Pseudomonas putida mt-2. J. Bacteriol. 160:251-255.
    • (1984) J. Bacteriol. , vol.160 , pp. 251-255
    • Harayama, S.1    Lehrbach, P.R.2    Timmis, K.N.3
  • 24
    • 0024451702 scopus 로고
    • Bacterial aromatic ring-cleavage enzymes are classified into two different gene families
    • Harayama, S., and M. Rekik. 1989. Bacterial aromatic ring-cleavage enzymes are classified into two different gene families. J. Biol. Chem. 264:15328-15333.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15328-15333
    • Harayama, S.1    Rekik, M.2
  • 25
    • 0024457019 scopus 로고
    • Physically associated enzymes produce and metabolize 2-hydroxy-2,4- dienoate, a chemically unstable intermediate formed in catechol metabolism via meta cleavage in Pseudomonas putida
    • Harayama, S., M. Rekik, K. L. Ngai, and L. N. Ornston. 1989. Physically associated enzymes produce and metabolize 2-hydroxy-2,4-dienoate, a chemically unstable intermediate formed in catechol metabolism via meta cleavage in Pseudomonas putida. J. Bacteriol. 171:6251-6258. (Pubitemid 19266947)
    • (1989) Journal of Bacteriology , vol.171 , Issue.11 , pp. 6251-6258
    • Harayama, S.1    Rekik, M.2    Ngai, K.-L.3    Ornston, L.N.4
  • 26
    • 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
  • 27
    • 0025020696 scopus 로고
    • Pseudomonas putida KF715 bphABCD operon encoding biphenyl and polychlorinated biphenyl degradation: Cloning, analysis, and expression in soil bacteria
    • Hayase, N., K. Taira, and K. Furukawa. 1990. Pseudomonas putida KF715 bphABCD operon encoding biphenyl and polychlorinated biphenyl degradation: cloning, analysis, and expression in soil bacteria. J. Bacteriol. 172:1160-1164.
    • (1990) J. Bacteriol. , vol.172 , pp. 1160-1164
    • Hayase, N.1    Taira, K.2    Furukawa, K.3
  • 28
    • 38349179297 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of a 4-hydroxybenzoate hydroxylase from Corynebacterium glutamicum
    • Huang, Y., K. X. Zhao, X. H. Shen, C. Y. Jiang, and S. J. Liu. 2008. Genetic and biochemical characterization of a 4-hydroxybenzoate hydroxylase from Corynebacterium glutamicum. Appl. Microbiol. Biotechnol. 78:75-83.
    • (2008) Appl. Microbiol. Biotechnol. , vol.78 , pp. 75-83
    • Huang, Y.1    Zhao, K.X.2    Shen, X.H.3    Jiang, C.Y.4    Liu, S.J.5
  • 29
    • 3242810505 scopus 로고    scopus 로고
    • Characterization of the 3-O-methylgallate dioxygenase gene and evidence of multiple 3-O-methylgallate catabolic pathways in Sphingomonas paucimobilis SYK-6
    • Kasai, D., E. Masai, K. Miyauchi, Y. Katayama, and M. Fukuda. 2004. Characterization of the 3-O-methylgallate dioxygenase gene and evidence of multiple 3-O-methylgallate catabolic pathways in Sphingomonas paucimobilis SYK-6. J. Bacteriol. 186:4951-4959.
    • (2004) J. Bacteriol. , vol.186 , pp. 4951-4959
    • Kasai, D.1    Masai, E.2    Miyauchi, K.3    Katayama, Y.4    Fukuda, M.5
  • 30
    • 22544457598 scopus 로고    scopus 로고
    • Characterization of the gallate dioxygenase gene: Three distinct ring cleavage dioxygenases are involved in syringate degradation by Sphingomonas paucimobilis SYK-6
    • DOI 10.1128/JB.187.15.5067-5074.2005
    • Kasai, D., E. Masai, K. Miyauchi, Y. Katayama, and M. Fukuda. 2005. Characterization of the gallate dioxygenase gene: three distinct ring cleavage dioxygenases are involved in syringate degradation by Sphingomonas paucimobilis SYK-6. J. Bacteriol. 187:5067-5074. (Pubitemid 41022923)
    • (2005) Journal of Bacteriology , vol.187 , Issue.15 , pp. 5067-5074
    • Kasai, D.1    Masai, E.2    Miyauchi, K.3    Katayama, Y.4    Fukuda, M.5
  • 31
    • 17644413773 scopus 로고    scopus 로고
    • The 2-His-1-carboxylate facial triad: A versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes
    • Koehntop, K. D., J. P. Emerson, and L. Que, Jr. 2005. The 2-His-1-carboxylate facial triad: a versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes. J. Biol. Inorg. Chem. 10:87-93.
    • (2005) J. Biol. Inorg. Chem. , vol.10 , pp. 87-93
    • Koehntop, K.D.1    Emerson, J.P.2    Que Jr., L.3
  • 32
    • 33744728709 scopus 로고    scopus 로고
    • α-amino-β-carboxymuconic-ε-semialdehyde decarboxylase (ACMSD) is a new member of the amidohydrolase superfamily
    • DOI 10.1021/bi060108c
    • Li, T., H. Iwaki, R. Fu, Y. Hasegawa, H. Zhang, and A. Liu. 2006. α-Amino-β-carboxymuconic-ε-semialdehyde decarboxylase (ACMSD) is a new member of the amidohydrolase superfamily. Biochemistry 45:6628-6634. (Pubitemid 43825363)
    • (2006) Biochemistry , vol.45 , Issue.21 , pp. 6628-6634
    • Li, T.1    Iwaki, H.2    Fu, R.3    Hasegawa, Y.4    Zhang, H.5    Liu, A.6
  • 33
    • 33748257672 scopus 로고    scopus 로고
    • Transition metal-catalyzed nonoxidative decarboxylation reactions
    • DOI 10.1021/bi061031v
    • Liu, A., and H. Zhang. 2006. Transition metal-catalyzed nonoxidative decarboxylation reactions. Biochemistry 45:10407-10411. (Pubitemid 44320457)
    • (2006) Biochemistry , vol.45 , Issue.35 , pp. 10407-10411
    • Liu, A.1    Zhang, H.2
  • 34
    • 33748250307 scopus 로고    scopus 로고
    • Crystal structure of α-amino-β-carboxymuconate-ε- Semialdeliyde decarboxylase: Insight into the active site and catalytic mechanism of a novel decarboxylation reaction
    • DOI 10.1021/bi060903q
    • Martynowski, D., Y. Eyobo, T. Li, K. Yang, A. Liu, and H. Zhang. 2006. Crystal structure of α-amino-β-carboxymuconate-ε-semialdehyde decarboxylase: insight into the active site and catalytic mechanism of a novel decarboxylation reaction. Biochemistry 45:10412-10421. (Pubitemid 44320458)
    • (2006) Biochemistry , vol.45 , Issue.35 , pp. 10412-10421
    • Martynowski, D.1    Eyobo, Y.2    Li, T.3    Yang, K.4    Liu, A.5    Zhang, H.6
  • 35
    • 11244352142 scopus 로고    scopus 로고
    • Cloning and characterization of the genes encoding enzymes for the protocatechuate meta-degradation pathway of Pseudomonas ochraceae NGJ1
    • Maruyama, K., T. Shibayama, A. Ichikawa, Y. Sakou, S. Yamada, and H. Sugisaki. 2004. Cloning and characterization of the genes encoding enzymes for the protocatechuate meta-degradation pathway of Pseudomonas ochraceae NGJ1. Biosci. Biotechnol. Biochem. 68:1434-1441.
    • (2004) Biosci. Biotechnol. Biochem. , vol.68 , pp. 1434-1441
    • Maruyama, K.1    Shibayama, T.2    Ichikawa, A.3    Sakou, Y.4    Yamada, S.5    Sugisaki, H.6
  • 36
    • 33846485037 scopus 로고    scopus 로고
    • Genetic and biochemical investigations on bacterial catabolic pathways for lignin-derived aromatic compounds
    • Masai, E., Y. Katayama, and M. Fukuda. 2007. Genetic and biochemical investigations on bacterial catabolic pathways for lignin-derived aromatic compounds. Biosci. Biotechnol. Biochem. 71:1-15.
    • (2007) Biosci. Biotechnol. Biochem. , vol.71 , pp. 1-15
    • Masai, E.1    Katayama, Y.2    Fukuda, M.3
  • 37
    • 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
    • DOI 10.1128/JB.182.23.6651-6658.2000
    • 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. (Pubitemid 32249246)
    • (2000) Journal of Bacteriology , vol.182 , Issue.23 , pp. 6651-6658
    • Masai, E.1    Momose, K.2    Hara, H.3    Nishikawa, S.4    Katayama, Y.5    Fukuda, M.6
  • 39
    • 0037338581 scopus 로고    scopus 로고
    • Prokaryotic homologs of the eukaryotic 3-hydroxyanthranilate 3,4-dioxygenase and 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase in the 2-nitrobenzoate degradation pathway of Pseudomonas fluorescens strain KU-7
    • Muraki, T., M. Taki, Y. Hasegawa, H. Iwaki, and P. C. Lau. 2003. Prokaryotic homologs of the eukaryotic 3-hydroxyanthranilate 3,4-dioxygenase and 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase in the 2-nitrobenzoate degradation pathway of Pseudomonas fluorescens strain KU-7. Appl. Environ. Microbiol. 69:1564-1572.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 1564-1572
    • Muraki, T.1    Taki, M.2    Hasegawa, Y.3    Iwaki, H.4    Lau, P.C.5
  • 40
    • 0020560883 scopus 로고
    • Complete nucleotide sequence of the metapyrocatechase gene on the TOL plasmid of Pseudomonas putida mt-2
    • Nakai, C., H. Kagamiyama, M. Nozaki, T. Nakazawa, S. Inouye, Y. Ebina, and A. Nakazawa. 1983. Complete nucleotide sequence of the metapyrocatechase gene on the TOL plasmid of Pseudomonas putida mt-2. J. Biol. Chem. 258:2923-2928.
    • (1983) J. Biol. Chem. , vol.258 , pp. 2923-2928
    • Nakai, C.1    Kagamiyama, H.2    Nozaki, M.3    Nakazawa, T.4    Inouye, S.5    Ebina, Y.6    Nakazawa, A.7
  • 42
    • 27444438472 scopus 로고    scopus 로고
    • Molecular characterization of the gallate dioxygenase from Pseudomonas putida KT2440. The prototype of a new subgroup of extradiol dioxygenases
    • Nogales, J., Á. Canales, J. Jiménez-Barbero, J. L. García, and E. Díaz. 2005. Molecular characterization of the gallate dioxygenase from Pseudomonas putida KT2440. The prototype of a new subgroup of extradiol dioxygenases. J. Biol. Chem. 280:35382-35390.
    • (2005) J. Biol. Chem. , vol.280 , pp. 35382-35390
    • Nogales, J.1    Canales, Á.2    Jiménez-Barbero, J.3    García, J.L.4    Díaz, E.5
  • 43
    • 0025363368 scopus 로고
    • Nucleotide sequences of the meta-cleavage pathway enzymes 2-hydroxymuconic semialdehyde dehydrogenase and 2-hydroxymuconic semialdehyde hydrolase from Pseudomonas CF600
    • DOI 10.1016/0167-4781(90)90046-5
    • Nordlund, I., and V. Shingler. 1990. Nucleotide sequences of the meta-cleavage pathway enzymes 2-hydroxymuconic semialdehyde dehydrogenase and 2-hydroxymuconic semialdehyde hydrolase from Pseudomonas CF600. Biochim. Biophys. Acta 1049:227-230. (Pubitemid 20183663)
    • (1990) Biochimica et Biophysica Acta - Gene Structure and Expression , vol.1049 , Issue.2 , pp. 227-230
    • Nordlund, I.1    Shingler, V.2
  • 44
    • 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
  • 45
    • 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. (Pubitemid 129526331)
    • (1999) Applied and Environmental Microbiology , vol.65 , Issue.6 , pp. 2789-2793
    • Peng, X.1    Masai, E.2    Katayama, Y.3    Fukuda, M.4
  • 46
    • 0036731753 scopus 로고    scopus 로고
    • Characterization of the 5-carboxyvanillate decarboxylase gene and its role in lignin-related biphenyl catabolism in Sphingomonas paucimobilis SYK-6
    • Peng, X., E. Masai, H. Kitayama, K. Harada, Y. Katayama, and M. Fukuda. 2002. Characterization of the 5-carboxyvanillate decarboxylase gene and its role in lignin-related biphenyl catabolism in Sphingomonas paucimobilis SYK-6. Appl. Environ. Microbiol. 68:4407-4415.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 4407-4415
    • Peng, X.1    Masai, E.2    Kitayama, H.3    Harada, K.4    Katayama, Y.5    Fukuda, M.6
  • 47
    • 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
  • 48
    • 0027937565 scopus 로고
    • Characterization of the pcaR regulatory gene from Pseudomonas putida, which is required for the complete degradation of p-hydroxybenzoate
    • Romero-Steiner, S., R. E. Parales, C. S. Harwood, and J. E. Houghton. 1994. Characterization of the pcaR regulatory gene from Pseudomonas putida, which is required for the complete degradation of p-hydroxybenzoate. J. Bacteriol. 176:5771-5779. (Pubitemid 24280511)
    • (1994) Journal of Bacteriology , vol.176 , Issue.18 , pp. 5771-5779
    • Romero-Steiner, S.1    Parales, R.E.2    Harwood, C.S.3    Houghton, J.E.4
  • 49
    • 0025115933 scopus 로고
    • Subcloning and nucleotide sequence of the 3,4-dihydroxyphenylacetate (homoprotocatechuate) 2,3-dioxygenase gene from Escherichia coli C
    • Roper, D. I., and R. A. Cooper. 1990. Subcloning and nucleotide sequence of the 3,4-dihydroxyphenylacetate (homoprotocatechuate) 2,3-dioxygenase gene from Escherichia coli C. FEBS Lett. 275:53-57.
    • (1990) FEBS Lett. , vol.275 , pp. 53-57
    • Roper, D.I.1    Cooper, R.A.2
  • 50
    • 0342516720 scopus 로고
    • Charomids: Cosmid vectors for efficient cloning and mapping of large or small restriction fragments
    • Saito, I., and G. R. Stark. 1986. Charomids: cosmid vectors for efficient cloning and mapping of large or small restriction fragments. Proc. Natl. Acad. Sci. USA 83:8664-8668.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8664-8668
    • Saito, I.1    Stark, G.R.2
  • 51
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou, N., and M. Nei. 1987. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4:406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 52
    • 0015219756 scopus 로고
    • The meta cleavage of catechol by Azotobacter species. 4-Oxalocrotonate pathway
    • Sala-Trepat, J. M., and W. C. Evans. 1971. The meta cleavage of catechol by Azotobacter species. 4-Oxalocrotonate pathway. Eur. J. Biochem. 20:400-413.
    • (1971) Eur. J. Biochem. , vol.20 , pp. 400-413
    • Sala-Trepat, J.M.1    Evans, W.C.2
  • 55
    • 0026567783 scopus 로고
    • Nucleotide sequence and functional analysis of the complete phenol/3,4-dimethylphenol catabolic pathway of Pseudomonas sp. strain CF600
    • Shingler, V., J. Powlowski, and U. Marklund. 1992. Nucleotide sequence and functional analysis of the complete phenol/3,4-dimethylphenol catabolic pathway of Pseudomonas sp. strain CF600. J. Bacteriol. 174:711-724.
    • (1992) J. Bacteriol. , vol.174 , pp. 711-724
    • Shingler, V.1    Powlowski, J.2    Marklund, U.3
  • 56
    • 0024284551 scopus 로고
    • λ ZAP: A bacteriophage λ expression vector with in vivo excision properties
    • Short, J. M., J. M. Fernandez, J. A. Sorge, and W. D. Huse. 1988. λ ZAP: 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.D.4
  • 57
    • 19744376088 scopus 로고    scopus 로고
    • Genes of the thymidine salvage pathway: Thymine-7-hydroxylase from a Rhodotorula glutinis cDNA library and iso-orotate decarboxylase from Neurospora crassa
    • Smiley, J. A., M. Kundracik, D. A. Landfried, V. R. Barnes, Sr., and A. A. Axhemi. 2005. Genes of the thymidine salvage pathway: thymine-7-hydroxylase from a Rhodotorula glutinis cDNA library and iso-orotate decarboxylase from Neurospora crassa. Biochim. Biophys. Acta 1723:256-264.
    • (2005) Biochim. Biophys. Acta , vol.1723 , pp. 256-264
    • Smiley, J.A.1    Kundracik, M.2    Landfried, D.A.3    Barnes Sr., V.R.4    Axhemi, A.A.5
  • 58
    • 33744718828 scopus 로고    scopus 로고
    • Genomic and functional analysis of the IncP-9 naphthalene-catabolic plasmid NAH7 and its transposon Tn4655 suggests catabolic gene spread by a tyrosine recombinase
    • DOI 10.1128/JB.00185-06
    • Sota, M., H. Yano, A. Ono, R. Miyazaki, H. Ishii, H. Genka, E. M. Top, and M. Tsuda. 2006. Genomic and functional analysis of the IncP-9 naphthalene-catabolic plasmid NAH7 and its transposon Tn4655 suggests catabolic gene spread by a tyrosine recombinase. J. Bacteriol. 188:4057-4067. (Pubitemid 43825409)
    • (2006) Journal of Bacteriology , vol.188 , Issue.11 , pp. 4057-4067
    • Sota, M.1    Yano, H.2    Ono, A.3    Miyazaki, R.4    Ishii, H.5    Genka, H.6    Top, E.M.7    Tsuda, M.8
  • 59
    • 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
  • 60
    • 0033566802 scopus 로고    scopus 로고
    • Crystal structure of an aromatic ring opening dioxygenase LigAB, a protocatechuate 4,5-dioxygenase, under aerobic conditions
    • Sugimoto, K., T. Senda, H. Aoshima, E. Masai, M. Fukuda, and Y. Mitsui. 1999. Crystal structure of an aromatic ring opening dioxygenase LigAB, a protocatechuate 4,5-dioxygenase, under aerobic conditions. Structure Fold. Des. 7:953-965.
    • (1999) Structure Fold. Des. , vol.7 , pp. 953-965
    • Sugimoto, K.1    Senda, T.2    Aoshima, H.3    Masai, E.4    Fukuda, M.5    Mitsui, Y.6
  • 61
    • 0030990383 scopus 로고    scopus 로고
    • Novel genes encoding 2-aminophenol 1,6-dioxygenase from Pseudomonas species AP-3 growing on 2-aminophenol and catalytic properties of the purified enzyme
    • Takenaka, S., S. Murakami, R. Shinke, K. Hatakeyama, H. Yukawa, and K. Aoki. 1997. Novel genes encoding 2-aminophenol 1,6-dioxygenase from Pseudomonas species AP-3 growing on 2-aminophenol and catalytic properties of the purified enzyme. J. Biol. Chem. 272:14727-14732.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14727-14732
    • Takenaka, S.1    Murakami, S.2    Shinke, R.3    Hatakeyama, K.4    Yukawa, H.5    Aoki, K.6
  • 62
    • 0036471973 scopus 로고    scopus 로고
    • Purification and molecular cloning of rat 2-amino-3-carboxymuconate-6- semialdehyde decarboxylase
    • DOI 10.1042/0264-6021:3610567
    • Tanabe, A., Y. Egashira, S. Fukuoka, K. Shibata, and H. Sanada. 2002. Purification and molecular cloning of rat 2-amino-3-carboxymuconate-6- semialdehyde decarboxylase. Biochem. J. 361:567-575. (Pubitemid 34177826)
    • (2002) Biochemical Journal , vol.361 , Issue.3 , pp. 567-575
    • Tanabe, A.1    Egashira, Y.2    Fukuoka, S.-I.3    Shibata, K.4    Sanada, H.5
  • 64
    • 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
  • 65
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • DOI 10.1016/0378-1119(85)90120-9
    • 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. (Pubitemid 15122816)
    • (1985) Gene , vol.33 , Issue.1 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 66
    • 4944251045 scopus 로고    scopus 로고
    • Thermophilic, reversible γ-resorcylate decarboxylase from Rhizobium sp. strain MTP-10005: Purification, molecular characterization, and expression
    • Yoshida, M., N. Fukuhara, and T. Oikawa. 2004. Thermophilic, reversible γ-resorcylate decarboxylase from Rhizobium sp. strain MTP-10005: purification, molecular characterization, and expression. J. Bacteriol. 186:6855-6863.
    • (2004) J. Bacteriol. , vol.186 , pp. 6855-6863
    • Yoshida, M.1    Fukuhara, N.2    Oikawa, T.3
  • 67
    • 33947411285 scopus 로고    scopus 로고
    • Biochemical and genetic analysis of the γ-resorcylate (2,6-dihydroxybenzoate) catabolic pathway in Rhizobium sp. strain MTP-10005: Identification and functional analysis of its gene cluster
    • Yoshida, M., T. Oikawa, H. Obata, K. Abe, H. Mihara, and N. Esaki. 2007. Biochemical and genetic analysis of the γ-resorcylate (2,6- dihydroxybenzoate) catabolic pathway in Rhizobium sp. strain MTP-10005: identification and functional analysis of its gene cluster. J. Bacteriol. 189:1573-1581.
    • (2007) J. Bacteriol. , vol.189 , pp. 1573-1581
    • Yoshida, M.1    Oikawa, T.2    Obata, H.3    Abe, K.4    Mihara, H.5    Esaki, N.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.