메뉴 건너뛰기




Volumn 87, Issue 2, 2000, Pages 59-69

Enzymes involved in the aerobic bacterial degradation of N- heteroaromatic compounds: Molybdenum hydroxylases and ring-opening 2,4- dioxygenases

Author keywords

[No Author keywords available]

Indexed keywords

HETEROCYCLIC COMPOUND; HYDROLASE; OXYGENASE; QUINALDINE;

EID: 0033982698     PISSN: 00281042     EISSN: None     Source Type: Journal    
DOI: 10.1007/s001140050011     Document Type: Review
Times cited : (48)

References (90)
  • 1
    • 0001270261 scopus 로고    scopus 로고
    • Design by directed evolution
    • Arnold FH (1998a) Design by directed evolution. Acc Chem Res 31:125-131
    • (1998) Acc Chem Res , vol.31 , pp. 125-131
    • Arnold, F.H.1
  • 2
    • 0032478172 scopus 로고    scopus 로고
    • Enzyme engineering reaches the boiling point
    • Arnold FH (1998b) Enzyme engineering reaches the boiling point. Proc Natl Acad Sci USA 95:2035-2036
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 2035-2036
    • Arnold, F.H.1
  • 4
    • 0028346612 scopus 로고
    • A novel type of oxygenolytic ring cleavage: 2,4-oxygenation and decarbonylation of 1H-3-hydroxy-4-oxoquinaldine and 1H-3-hydroxy-4-oxoquinoline
    • Bauer I, De Beyer A, Tshisuaka B, Fetzner S, Lingens F (1994) A novel type of oxygenolytic ring cleavage: 2,4-oxygenation and decarbonylation of 1H-3-hydroxy-4-oxoquinaldine and 1H-3-hydroxy-4-oxoquinoline. FEMS Microbiol Lett 117:299-304
    • (1994) FEMS Microbiol Lett , vol.117 , pp. 299-304
    • Bauer, I.1    De Beyer, A.2    Tshisuaka, B.3    Fetzner, S.4    Lingens, F.5
  • 5
    • 0029767386 scopus 로고    scopus 로고
    • 2,4-Dioxygenases catalyzing N-heterocyclic-ring cleavage and formation of carbon monoxide. Purification and some properties of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter sp. Rü61a and comparison with 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from Pseudomonas putida 33/1
    • Bauer I, Max N, Fetzner S, Lingens F (1996) 2,4-Dioxygenases catalyzing N-heterocyclic-ring cleavage and formation of carbon monoxide. Purification and some properties of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter sp. Rü61a and comparison with 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from Pseudomonas putida 33/1. Eur J Biochem 240:576-583
    • (1996) Eur J Biochem , vol.240 , pp. 576-583
    • Bauer, I.1    Max, N.2    Fetzner, S.3    Lingens, F.4
  • 6
    • 0023100333 scopus 로고
    • Microbial metabolism of homocyclic and heterocyclic aromatic compounds under anaerobic conditions
    • Berry DF, Francis AJ, Bollag J-M (1987) Microbial metabolism of homocyclic and heterocyclic aromatic compounds under anaerobic conditions. Microbiol Rev 51:43-59
    • (1987) Microbiol Rev , vol.51 , pp. 43-59
    • Berry, D.F.1    Francis, A.J.2    Bollag, J.-M.3
  • 7
    • 0026002504 scopus 로고
    • The transformation of heterocyclic aromatic compounds and their derivatives under anaerobic conditions
    • Bollag J-M, Kaiser J-P (1991) The transformation of heterocyclic aromatic compounds and their derivatives under anaerobic conditions. Crit Rev Environ Control 21:297-329
    • (1991) Crit Rev Environ Control , vol.21 , pp. 297-329
    • Bollag, J.-M.1    Kaiser, J.-P.2
  • 8
    • 0030771511 scopus 로고    scopus 로고
    • Towards the reaction mechanism of xanthine oxidase from EPR studies
    • Bray RC, Lowe DJ (1997) Towards the reaction mechanism of xanthine oxidase from EPR studies. Biochem Soc Trans 25:762-768
    • (1997) Biochem Soc Trans , vol.25 , pp. 762-768
    • Bray, R.C.1    Lowe, D.J.2
  • 11
    • 0001223385 scopus 로고
    • The microbial degradation of heterocyclic compounds
    • Callely AG (1978) The microbial degradation of heterocyclic compounds. Prog Ind Microbiol 14:205-281
    • (1978) Prog Ind Microbiol , vol.14 , pp. 205-281
    • Callely, A.G.1
  • 12
    • 0345624496 scopus 로고    scopus 로고
    • Kinetics and interactions of molybdenum and iron-sulfur centers in bacterial enzymes of the xanthine oxidase family: Mechanistic implications
    • Canne C, Lowe DJ, Fetzner S, Adams B, Smith AT, Kappl R, Bray RC, Hüttermann J (1999) Kinetics and interactions of molybdenum and iron-sulfur centers in bacterial enzymes of the xanthine oxidase family: mechanistic implications. Biochemistry 38:14077-14087
    • (1999) Biochemistry , vol.38 , pp. 14077-14087
    • Canne, C.1    Lowe, D.J.2    Fetzner, S.3    Adams, B.4    Smith, A.T.5    Kappl, R.6    Bray, R.C.7    Hüttermann, J.8
  • 13
    • 0030302162 scopus 로고    scopus 로고
    • Transformation of N-, O-, and S-heterocycles (NOSHs) in estuarine sediments: Effects of redox potential and sediment particle size
    • Catallo WJ (1996) Transformation of N-, O-, and S-heterocycles (NOSHs) in estuarine sediments: effects of redox potential and sediment particle size. Chemosphere 33:2543-2563
    • (1996) Chemosphere , vol.33 , pp. 2543-2563
    • Catallo, W.J.1
  • 15
    • 0001870115 scopus 로고
    • Tar and pitch
    • Elvers B, Hawkins S, Russey W (eds) VCH, Weinheim
    • Collin G, Höke H (1995) Tar and pitch. In: Elvers B, Hawkins S, Russey W (eds) Ullman's encyclopedia of industrial chemistry, vol A26. VCH, Weinheim, pp 91-127
    • (1995) Ullman's Encyclopedia of Industrial Chemistry , vol.A26 , pp. 91-127
    • Collin, G.1    Höke, H.2
  • 16
    • 0002727505 scopus 로고
    • Biodegradation of s-triazine xenobiotics
    • Cook AM (1987) Biodegradation of s-triazine xenobiotics. FEMS Microbiol Rev 46:93-116
    • (1987) FEMS Microbiol Rev , vol.46 , pp. 93-116
    • Cook, A.M.1
  • 17
    • 0032518266 scopus 로고    scopus 로고
    • DNA shuffling of a family of genes from diverse species accelerates directed evolution
    • Crameri A, Raillard S-A, Bermudez E, Stemmer WPC (1998) DNA shuffling of a family of genes from diverse species accelerates directed evolution. Nature 391:288-291
    • (1998) Nature , vol.391 , pp. 288-291
    • Crameri, A.1    Raillard, S.-A.2    Bermudez, E.3    Stemmer, W.P.C.4
  • 19
    • 0033178813 scopus 로고    scopus 로고
    • Chemical modification of enzymes for enhanced functionality
    • DeSantis G, Jones JB (1999) Chemical modification of enzymes for enhanced functionality. Curr Opin Biotechnol 10:324-330
    • (1999) Curr Opin Biotechnol , vol.10 , pp. 324-330
    • DeSantis, G.1    Jones, J.B.2
  • 20
    • 0033529852 scopus 로고    scopus 로고
    • Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavo-protein containing S-selanylcysteine
    • Dobbek H, Gremer L, Meyer O, Huber R (1999) Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavo-protein containing S-selanylcysteine. Proc Natl Acad Sci USA 96:8884-8889
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8884-8889
    • Dobbek, H.1    Gremer, L.2    Meyer, O.3    Huber, R.4
  • 21
    • 0031944612 scopus 로고    scopus 로고
    • Bacterial degradation of pyridine, indole, quinoline, and their derivatives under different redox conditions
    • Fetzner S (1998a) Bacterial degradation of pyridine, indole, quinoline, and their derivatives under different redox conditions. Appl Microbiol Biotechnol 49:237-250
    • (1998) Appl Microbiol Biotechnol , vol.49 , pp. 237-250
    • Fetzner, S.1
  • 22
  • 23
    • 0027620339 scopus 로고
    • Purification and some properties of the molybdenum-and iron-containing quinaldic acid 4-oxidoreductase from Serratia marcescens 2CC-1
    • Fetzner S, Lingens F (1993) Purification and some properties of the molybdenum-and iron-containing quinaldic acid 4-oxidoreductase from Serratia marcescens 2CC-1. Biol Chem Hoppe-Seyler 374:363-376
    • (1993) Biol Chem Hoppe-Seyler , vol.374 , pp. 363-376
    • Fetzner, S.1    Lingens, F.2
  • 24
    • 0031949286 scopus 로고    scopus 로고
    • Bacterial degradation of quinoline and derivatives - Pathways and their biocatalysts
    • Fetzner S, Tshisuaka B, Lingens F, Kappl R, Hüttermann J (1998) Bacterial degradation of quinoline and derivatives - pathways and their biocatalysts. Angew Chem Int Ed 37:576-597
    • (1998) Angew Chem Int Ed , vol.37 , pp. 576-597
    • Fetzner, S.1    Tshisuaka, B.2    Lingens, F.3    Kappl, R.4    Hüttermann, J.5
  • 25
    • 0008921254 scopus 로고
    • Acyl group transfer - The serine proteinases
    • Page MI, Williams A (eds) Royal Society of Chemistry, London
    • Fink AL (1987) Acyl group transfer - the serine proteinases. In: Page MI, Williams A (eds) Enzyme mechanisms. Royal Society of Chemistry, London, pp 159-177
    • (1987) Enzyme Mechanisms , pp. 159-177
    • Fink, A.L.1
  • 26
    • 0344172698 scopus 로고    scopus 로고
    • Bacterial 2,4-dioxygenases: New members of the α/β hydrolase-fold superfamily of enzymes functionally related to serine hydrolases
    • Fischer F, Künne S, Fetzner S (1999) Bacterial 2,4-dioxygenases: new members of the α/β hydrolase-fold superfamily of enzymes functionally related to serine hydrolases. J Bacteriol 181:5725-5733
    • (1999) J Bacteriol , vol.181 , pp. 5725-5733
    • Fischer, F.1    Künne, S.2    Fetzner, S.3
  • 27
    • 0029959052 scopus 로고    scopus 로고
    • Pathway engineering for the production of aromatic compounds in Escherichia coli
    • Flores N, Xiao J, Berry A, Bolivar F, Valle F (1996) Pathway engineering for the production of aromatic compounds in Escherichia coli. Nat Biotechnol 14:620-623
    • (1996) Nat Biotechnol , vol.14 , pp. 620-623
    • Flores, N.1    Xiao, J.2    Berry, A.3    Bolivar, F.4    Valle, F.5
  • 28
    • 0008914410 scopus 로고    scopus 로고
    • Oxidation of organic compounds
    • Lengeier JW, Drews G, Schlegel HG (eds) Thieme, Stuttgart New York
    • Fuchs G (1999) Oxidation of organic compounds. In: Lengeier JW, Drews G, Schlegel HG (eds) Biology of the prokaryotes. Thieme, Stuttgart New York, pp 187-233
    • (1999) Biology of the Prokaryotes , pp. 187-233
    • Fuchs, G.1
  • 30
    • 0032079684 scopus 로고    scopus 로고
    • Altered specificity mutations define residues essential for substrate positioning in xanthine dehydrogenase
    • Glatigny A, Hof P, Romão MJ, Huber R, Scazzocchio C (1998) Altered specificity mutations define residues essential for substrate positioning in xanthine dehydrogenase. J Mol Biol 278:431-438
    • (1998) J Mol Biol , vol.278 , pp. 431-438
    • Glatigny, A.1    Hof, P.2    Romão, M.J.3    Huber, R.4    Scazzocchio, C.5
  • 31
    • 0029682807 scopus 로고    scopus 로고
    • Characterization of xanthine dehydrogenase from the anaerobic bacterium Veillonella atypica and identification of a molybdopterin-cytosine-dinucleotide-containing molybdenum cofactor
    • Gremer L, Meyer O (1996) Characterization of xanthine dehydrogenase from the anaerobic bacterium Veillonella atypica and identification of a molybdopterin-cytosine-dinucleotide-containing molybdenum cofactor. Eur J Biochem 238:862-866
    • (1996) Eur J Biochem , vol.238 , pp. 862-866
    • Gremer, L.1    Meyer, O.2
  • 32
    • 0026805891 scopus 로고
    • Functional and evolutionary relationships among diverse oxygenases
    • Harayama S, Kok M, Neidle EL (1992) Functional and evolutionary relationships among diverse oxygenases. Annu Rev Microbiol 46:565-601
    • (1992) Annu Rev Microbiol , vol.46 , pp. 565-601
    • Harayama, S.1    Kok, M.2    Neidle, E.L.3
  • 33
    • 0032838778 scopus 로고    scopus 로고
    • Chemical engineering of enzymes: Altered catalytic activity, predictable selectivity and exceptional stability of the semisynthetic peroxidase seleno-subtilisin
    • Häring D, Schreier P (1999) Chemical engineering of enzymes: altered catalytic activity, predictable selectivity and exceptional stability of the semisynthetic peroxidase seleno-subtilisin. Naturwissenschaften 86:307-312
    • (1999) Naturwissenschaften , vol.86 , pp. 307-312
    • Häring, D.1    Schreier, P.2
  • 35
    • 0027240483 scopus 로고
    • Monitoring the efficacy of bioremediation
    • Heitzer A, Sayler GS (1993) Monitoring the efficacy of bioremediation. Trends Biotechnol 11:334-343
    • (1993) Trends Biotechnol , vol.11 , pp. 334-343
    • Heitzer, A.1    Sayler, G.S.2
  • 36
    • 0000273676 scopus 로고    scopus 로고
    • The mononuclear molybdenum enzymes
    • Hille R (1996a) The mononuclear molybdenum enzymes. Chem Rev 96:2757-2816
    • (1996) Chem Rev , vol.96 , pp. 2757-2816
    • Hille, R.1
  • 37
    • 0002913203 scopus 로고    scopus 로고
    • Structure and function of mononuclear molybdenum enzymes
    • Hille R (1996b) Structure and function of mononuclear molybdenum enzymes. J Biol Inorg Chem 1:397-404
    • (1996) J Biol Inorg Chem , vol.1 , pp. 397-404
    • Hille, R.1
  • 38
    • 0000250341 scopus 로고    scopus 로고
    • Mechanistic aspects of the mononuclear molybdenum enzymes
    • Hille R (1997) Mechanistic aspects of the mononuclear molybdenum enzymes. J Biol Inorg Chem 2:804-809
    • (1997) J Biol Inorg Chem , vol.2 , pp. 804-809
    • Hille, R.1
  • 39
    • 0031722845 scopus 로고    scopus 로고
    • Reply to further comments on enzymes of the xanthine oxidase family
    • Hille R (1998) Reply to further comments on enzymes of the xanthine oxidase family. J Biol Inorg Chem 3:559-560
    • (1998) J Biol Inorg Chem , vol.3 , pp. 559-560
    • Hille, R.1
  • 46
    • 0033578095 scopus 로고    scopus 로고
    • Laboratory evolution of peroxide-mediated cytochrome P450 hydroxylation
    • Joo H, Lin Z, Arnold FH (1999) Laboratory evolution of peroxide-mediated cytochrome P450 hydroxylation. Nature 399:670-673
    • (1999) Nature , vol.399 , pp. 670-673
    • Joo, H.1    Lin, Z.2    Arnold, F.H.3
  • 47
    • 0021130487 scopus 로고
    • Chemical mutation of enzyme active sites
    • Kaiser ET, Lawrence DS (1984) Chemical mutation of enzyme active sites. Science 226:505-511
    • (1984) Science , vol.226 , pp. 505-511
    • Kaiser, E.T.1    Lawrence, D.S.2
  • 48
    • 0029811543 scopus 로고    scopus 로고
    • Microbial metabolism of pyridine, quinoline, acridine, and their derivatives under aerobic and anaerobic conditions
    • Kaiser J-P, Feng Y, Bollag J-M (1996) Microbial metabolism of pyridine, quinoline, acridine, and their derivatives under aerobic and anaerobic conditions. Microbiol Rev 60:483-498
    • (1996) Microbiol Rev , vol.60 , pp. 483-498
    • Kaiser, J.-P.1    Feng, Y.2    Bollag, J.-M.3
  • 49
    • 0008881664 scopus 로고
    • Aerobic and anaerobic degradation of heterocyclic aromatic compounds by bacteria
    • in German
    • Koenig K, Andreesen JR (1992) Aerobic and anaerobic degradation of heterocyclic aromatic compounds by bacteria. Bioengineering 8:78-84 (in German)
    • (1992) Bioengineering , vol.8 , pp. 78-84
    • Koenig, K.1    Andreesen, J.R.2
  • 51
    • 0031543435 scopus 로고    scopus 로고
    • Directed evolution of enzyme catalysts
    • Kuchner O, Arnold FH (1997) Directed evolution of enzyme catalysts. Trends Biotechnol 15:523-530
    • (1997) Trends Biotechnol , vol.15 , pp. 523-530
    • Kuchner, O.1    Arnold, F.H.2
  • 52
    • 0002626094 scopus 로고
    • Enzymatic hydroxylations in industrial application
    • Kulla HG (1991) Enzymatic hydroxylations in industrial application. Chimia 45:81-85
    • (1991) Chimia , vol.45 , pp. 81-85
    • Kulla, H.G.1
  • 53
    • 0030855080 scopus 로고    scopus 로고
    • Stabilization of protein structures
    • Lee B, Vasmatzis G (1997) Stabilization of protein structures. Curr Opin Biotechnol 8:423-428
    • (1997) Curr Opin Biotechnol , vol.8 , pp. 423-428
    • Lee, B.1    Vasmatzis, G.2
  • 54
    • 0028286779 scopus 로고
    • Purification and characterization of isoquinoline 1-oxidoreductase from Pseudomonas diminuta 7, a novel molybdenum-containing hydroxylase
    • Lehmann M, Tshisuaka B, Fetzner S, Roger P, Lingens F (1994) Purification and characterization of isoquinoline 1-oxidoreductase from Pseudomonas diminuta 7, a novel molybdenum-containing hydroxylase. J Biol Chem 269:11254-11260
    • (1994) J Biol Chem , vol.269 , pp. 11254-11260
    • Lehmann, M.1    Tshisuaka, B.2    Fetzner, S.3    Roger, P.4    Lingens, F.5
  • 56
    • 0031783994 scopus 로고    scopus 로고
    • Further comments on enzymes of the xanthine oxidase family
    • Lowe DJ, Richards RL, Bray RC (1998) Further comments on enzymes of the xanthine oxidase family. J Biol Inorg Chem 3:557-558
    • (1998) J Biol Inorg Chem , vol.3 , pp. 557-558
    • Lowe, D.J.1    Richards, R.L.2    Bray, R.C.3
  • 57
    • 0030457185 scopus 로고    scopus 로고
    • Rational approach to improving reductive catalysis by cytochrome P450cam
    • Manchester JI, Ornstein RL (1996) Rational approach to improving reductive catalysis by cytochrome P450cam. Biochimie 78:714-722
    • (1996) Biochimie , vol.78 , pp. 714-722
    • Manchester, J.I.1    Ornstein, R.L.2
  • 58
    • 0030824631 scopus 로고    scopus 로고
    • In situ microcosms in aquifer bioremediation studies
    • Mandelbaum RT, Shati MR, Ronen D (1997) In situ microcosms in aquifer bioremediation studies. FEMS Microbiol Rev 20:489-502
    • (1997) FEMS Microbiol Rev , vol.20 , pp. 489-502
    • Mandelbaum, R.T.1    Shati, M.R.2    Ronen, D.3
  • 59
    • 0033153175 scopus 로고    scopus 로고
    • Novel approaches for discovering industrial enzymes
    • Marrs B, Delagrave S, Murphy D (1999) Novel approaches for discovering industrial enzymes. Curr Opin Microbiol 2:241-245
    • (1999) Curr Opin Microbiol , vol.2 , pp. 241-245
    • Marrs, B.1    Delagrave, S.2    Murphy, D.3
  • 60
    • 0028108347 scopus 로고
    • Activation of molecular oxygen by flavins and flavo-proteins
    • Massey V (1994) Activation of molecular oxygen by flavins and flavo-proteins. J Biol Chem 269:22459-22462
    • (1994) J Biol Chem , vol.269 , pp. 22459-22462
    • Massey, V.1
  • 61
    • 0030824355 scopus 로고    scopus 로고
    • Milk xanthine oxidoreductase: The first one hundred years
    • Massey V, Harris CM (1997) Milk xanthine oxidoreductase: the first one hundred years. Biochem Soc Trans 25:750-755
    • (1997) Biochem Soc Trans , vol.25 , pp. 750-755
    • Massey, V.1    Harris, C.M.2
  • 62
    • 0002798821 scopus 로고
    • Biochemistry of the aerobic utilization of carbon monoxide
    • Murrell JC, Kelly DP (eds) Intercept, Andover
    • Meyer O, Frunzke K, Mörsdorf G (1993) Biochemistry of the aerobic utilization of carbon monoxide. In: Murrell JC, Kelly DP (eds) Microbial growth on C1 compounds. Intercept, Andover, pp 433-459
    • (1993) Microbial Growth on C1 Compounds , pp. 433-459
    • Meyer, O.1    Frunzke, K.2    Mörsdorf, G.3
  • 63
    • 0021107342 scopus 로고
    • Studies on the specificity toward aldehyde substrates and steady-state kinetics of xanthine oxidase
    • Morpeth FF (1983) Studies on the specificity toward aldehyde substrates and steady-state kinetics of xanthine oxidase. Biochim Biophys Acta 744:328-334
    • (1983) Biochim Biophys Acta , vol.744 , pp. 328-334
    • Morpeth, F.F.1
  • 64
    • 0018288669 scopus 로고
    • Purification and properties of xanthine dehydrogenase from Streptomyces cyanogenus
    • Ohe T, Watanabe Y (1979) Purification and properties of xanthine dehydrogenase from Streptomyces cyanogenus. J Biochem 86:45-53
    • (1979) J Biochem , vol.86 , pp. 45-53
    • Ohe, T.1    Watanabe, Y.2
  • 66
    • 0029662913 scopus 로고    scopus 로고
    • A mini-review of microbial consortia: Their roles in aquatic production and biogeochemical cycling
    • Paerl HW, Pinckney JL (1996) A mini-review of microbial consortia: their roles in aquatic production and biogeochemical cycling. Microb Ecol 31:225-247
    • (1996) Microb Ecol , vol.31 , pp. 225-247
    • Paerl, H.W.1    Pinckney, J.L.2
  • 67
    • 0028052780 scopus 로고
    • Pathway engineering in secondary metabolite-producing actinomycetes
    • Piepersberg W (1994) Pathway engineering in secondary metabolite-producing actinomycetes. Crit Rev Biotechnol 14:251-285
    • (1994) Crit Rev Biotechnol , vol.14 , pp. 251-285
    • Piepersberg, W.1
  • 68
    • 0002486743 scopus 로고
    • Biochemistry of the molybdenum cofactors
    • Stiefel EI, Coucouvanis D, Newton WE (eds) ACS symposium series 535. American Chemical Society, Washington
    • Rajagopalan KV (1993) Biochemistry of the molybdenum cofactors. In: Stiefel EI, Coucouvanis D, Newton WE (eds) Molybdenum enzymes, cofactors, and model systems. ACS symposium series 535. American Chemical Society, Washington, pp 38-49
    • (1993) Molybdenum Enzymes, Cofactors, and Model Systems , pp. 38-49
    • Rajagopalan, K.V.1
  • 69
    • 0001952918 scopus 로고    scopus 로고
    • Superior biocatalysts by directed evolution
    • Reetz MT, Jaeger K-E (1999) Superior biocatalysts by directed evolution. Top Curr Chem 200:31-57
    • (1999) Top Curr Chem , vol.200 , pp. 31-57
    • Reetz, M.T.1    Jaeger, K.-E.2
  • 70
    • 0031756487 scopus 로고    scopus 로고
    • Development of hybrid strains for the mineralization of chloroaromatics by patchwork assembly
    • Reineke W (1998) Development of hybrid strains for the mineralization of chloroaromatics by patchwork assembly. Annu Rev Microbiol 52:287-331
    • (1998) Annu Rev Microbiol , vol.52 , pp. 287-331
    • Reineke, W.1
  • 71
    • 0023644204 scopus 로고
    • Assemblage of ortho cleavage route for simultaneous degradation of chloro-and methylaromatics
    • Rojo F, Pieper DH, Engesser K-H, Knackmuss H-J, Timmis KN (1987) Assemblage of ortho cleavage route for simultaneous degradation of chloro-and methylaromatics. Science 238:1395-1398
    • (1987) Science , vol.238 , pp. 1395-1398
    • Rojo, F.1    Pieper, D.H.2    Engesser, K.-H.3    Knackmuss, H.-J.4    Timmis, K.N.5
  • 72
    • 0002155983 scopus 로고    scopus 로고
    • Structure and function of the xanthine-oxidase family of molybdenum enzymes
    • Romão MJ, Huber R (1998) Structure and function of the xanthine-oxidase family of molybdenum enzymes. Struct Bonding 90:69-95
    • (1998) Struct Bonding , vol.90 , pp. 69-95
    • Romão, M.J.1    Huber, R.2
  • 74
    • 0024802158 scopus 로고
    • Microbial enzymes for oxidation of organic molecules
    • Sariaslani FS (1989) Microbial enzymes for oxidation of organic molecules. Crit Rev Biotechnol 9:171-257
    • (1989) Crit Rev Biotechnol , vol.9 , pp. 171-257
    • Sariaslani, F.S.1
  • 75
    • 0028251976 scopus 로고
    • The purine degradation pathway, genetics, biochemistry and regulation
    • Scazzocchio C (1994) The purine degradation pathway, genetics, biochemistry and regulation. Prog Ind Microbiol 29:221-257
    • (1994) Prog Ind Microbiol , vol.29 , pp. 221-257
    • Scazzocchio, C.1
  • 76
    • 0345628018 scopus 로고    scopus 로고
    • 2-Hydroxyisonicotinate dehydrogenase isolated from Mycobacterium sp. INA1
    • Schräder T, Hillebrand C, Andreesen JR (1998) 2-Hydroxyisonicotinate dehydrogenase isolated from Mycobacterium sp. INA1. FEMS Microbiol Lett 164:311-316
    • (1998) FEMS Microbiol Lett , vol.164 , pp. 311-316
    • Schräder, T.1    Hillebrand, C.2    Andreesen, J.R.3
  • 77
    • 0030874881 scopus 로고    scopus 로고
    • Lipases and αlβ hydrolase fold
    • Schrag JD, Cygler M (1997) Lipases and αlβ hydrolase fold. Methods Enzymol 284:85-107
    • (1997) Methods Enzymol , vol.284 , pp. 85-107
    • Schrag, J.D.1    Cygler, M.2
  • 78
    • 0033577926 scopus 로고    scopus 로고
    • Picking a winner
    • Sheldon R (1999) Picking a winner. Nature 399:636-637
    • (1999) Nature , vol.399 , pp. 636-637
    • Sheldon, R.1
  • 79
    • 0002884452 scopus 로고
    • Microbial transformation of pyridine derivatives
    • Shukla OP (1984) Microbial transformation of pyridine derivatives. J Sci Ind Res 43:98-116
    • (1984) J Sci Ind Res , vol.43 , pp. 98-116
    • Shukla, O.P.1
  • 80
    • 0032412432 scopus 로고    scopus 로고
    • Assessment of the microbiological potential for the natural attenuation of petroleum hydrocarbons in a shallow aquifer system
    • Stapleton RD, Sayler GS (1998) Assessment of the microbiological potential for the natural attenuation of petroleum hydrocarbons in a shallow aquifer system. Microb Ecol 36:349-361
    • (1998) Microb Ecol , vol.36 , pp. 349-361
    • Stapleton, R.D.1    Sayler, G.S.2
  • 81
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer WPC (1994) Rapid evolution of a protein in vitro by DNA shuffling. Nature 370:389-391
    • (1994) Nature , vol.370 , pp. 389-391
    • Stemmer, W.P.C.1
  • 82
    • 0029983270 scopus 로고    scopus 로고
    • Quinaldine 4-oxidase from Arthrobacter sp. Rü61a, a versatile procaryotic molybdenum-containing hydroxylase active towards N-containing heterocyclic compounds and aromatic aldehydes
    • Stephan I, Tshisuaka B, Fetzner S, Lingens F (1996) Quinaldine 4-oxidase from Arthrobacter sp. Rü61a, a versatile procaryotic molybdenum-containing hydroxylase active towards N-containing heterocyclic compounds and aromatic aldehydes. Eur J Biochem 236:155-162
    • (1996) Eur J Biochem , vol.236 , pp. 155-162
    • Stephan, I.1    Tshisuaka, B.2    Fetzner, S.3    Lingens, F.4
  • 83
    • 0030664822 scopus 로고    scopus 로고
    • Isolation of new 6-methylnicotinic-acid-degrading bacteria, one of which catalyses the regioselective hydroxylation of nicotinic acid at position C2
    • Tinschert A, Kiener A, Heinzmann K, Tschech A (1997) Isolation of new 6-methylnicotinic-acid-degrading bacteria, one of which catalyses the regioselective hydroxylation of nicotinic acid at position C2. Arch Microbiol 168:355-361
    • (1997) Arch Microbiol , vol.168 , pp. 355-361
    • Tinschert, A.1    Kiener, A.2    Heinzmann, K.3    Tschech, A.4
  • 85
    • 0027280086 scopus 로고
    • Refined X-ray structures of haloalkane dehalogenase at pH 6.2 and pH 8.2 and implications for the reaction mechanism
    • Verschueren KHG, Franken SM, Rozeboom HJ, Kalk KH, Dijkstra BW (1993a) Refined X-ray structures of haloalkane dehalogenase at pH 6.2 and pH 8.2 and implications for the reaction mechanism. J Mol Biol 232:856-872
    • (1993) J Mol Biol , vol.232 , pp. 856-872
    • Verschueren, K.H.G.1    Franken, S.M.2    Rozeboom, H.J.3    Kalk, K.H.4    Dijkstra, B.W.5
  • 86
  • 87
    • 0032419376 scopus 로고    scopus 로고
    • Directed evolution of new enzymes and pathways for environmental biocatalysis
    • Wackett LP (1998) Directed evolution of new enzymes and pathways for environmental biocatalysis. Ann N Y Acad Sci 864:142-152
    • (1998) Ann N Y Acad Sci , vol.864 , pp. 142-152
    • Wackett, L.P.1
  • 88
    • 0343519245 scopus 로고
    • Metabolism of polyhalogenaled compounds by a genetically engineered bacterium
    • Wackett LP, Sadowsky MJ, Newman LM, Hur H-G, Li S (1994) Metabolism of polyhalogenaled compounds by a genetically engineered bacterium. Nature 368:627-629
    • (1994) Nature , vol.368 , pp. 627-629
    • Wackett, L.P.1    Sadowsky, M.J.2    Newman, L.M.3    Hur, H.-G.4    Li, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.