메뉴 건너뛰기




Volumn 75, Issue 2, 2009, Pages 337-344

In vivo evolution of butane oxidation by terminal alkane hydroxylases AlkB and CYP153A6

Author keywords

[No Author keywords available]

Indexed keywords

ALKANE HYDROXYLASE; ALKANOL; ALKANOLS; BUTANE OXIDATIONS; BUTANOL PRODUCTIONS; CARBON SOURCES; COMPLEMENTATION; DIRECTED EVOLUTIONS; ENHANCED GROWTHS; EVOLUTION SYSTEMS; HOST ORGANISMS; HYDROXYLASES; IN-VIVO; INTEGRAL MEMBRANES; MONOOXYGENASES; SELECTIVE OXIDATIONS;

EID: 58149383679     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.01758-08     Document Type: Article
Times cited : (73)

References (36)
  • 1
    • 0019495128 scopus 로고
    • Occurrence of cytochrome P450 in Acinetobacter strains after growth on n-hexadecane
    • Asperger, O., A. Naumann, and H. P. Kleber. 1981. Occurrence of cytochrome P450 in Acinetobacter strains after growth on n-hexadecane. FEMS Microbiol. Lett. 11:309-312.
    • (1981) FEMS Microbiol. Lett , vol.11 , pp. 309-312
    • Asperger, O.1    Naumann, A.2    Kleber, H.P.3
  • 2
    • 33645800565 scopus 로고
    • Hydrocarbon oxidation by a bacterial enzyme system. I. Products of octane oxidation
    • Baptist, J. N., R. K. Gholson, and M. J. Coon. 1963. Hydrocarbon oxidation by a bacterial enzyme system. I. Products of octane oxidation. Biochim. Biophys. Acta 73:1-6.
    • (1963) Biochim. Biophys. Acta , vol.73 , pp. 1-6
    • Baptist, J.N.1    Gholson, R.K.2    Coon, M.J.3
  • 3
    • 0141992704 scopus 로고    scopus 로고
    • Camps, M., and L. A. Loeb. 2003. Use of pol I-deficient E. coli for functional complementation of DNA polymerase, p. 11-18. In J. F. H. Arnold and G. Georgiou (ed.), Directed enzyme evolution: screening and selection methods. Humana, Totowa, NJ.
    • Camps, M., and L. A. Loeb. 2003. Use of pol I-deficient E. coli for functional complementation of DNA polymerase, p. 11-18. In J. F. H. Arnold and G. Georgiou (ed.), Directed enzyme evolution: screening and selection methods. Humana, Totowa, NJ.
  • 4
    • 0043194096 scopus 로고    scopus 로고
    • Targeted gene evolution in Escherichia coli using a highly error-prone DNA polymerase I
    • Camps, M., J. Naukkarinen, B. P. Johnson, and L. A. Loeb. 2003. Targeted gene evolution in Escherichia coli using a highly error-prone DNA polymerase I. Proc. Natl. Acad. Sci. USA 100:9727-9732.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 9727-9732
    • Camps, M.1    Naukkarinen, J.2    Johnson, B.P.3    Loeb, L.A.4
  • 5
    • 0015612808 scopus 로고
    • Genetic regulation of octane dissimilation plasmid in Pseudomonas
    • Chakrabarty, M., G. Chou, and I. C. Gunsalus. 1973. Genetic regulation of octane dissimilation plasmid in Pseudomonas. Proc. Natl. Acad. Sci. USA 70:1137-1140.
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 1137-1140
    • Chakrabarty, M.1    Chou, G.2    Gunsalus, I.C.3
  • 6
    • 1842349188 scopus 로고
    • Broad host range DNA cloning system for gram-negative bacteria: Construction of a gene bank of Rhizobium meliloti
    • Ditta, G., S. Stanfield, D. Corbin, and D. R. Helinski. 1980. Broad host range DNA cloning system for gram-negative bacteria: construction of a gene bank of Rhizobium meliloti. Proc. Natl. Acad. Sci. USA 77:7347-7351.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 7347-7351
    • Ditta, G.1    Stanfield, S.2    Corbin, D.3    Helinski, D.R.4
  • 7
    • 0035424201 scopus 로고    scopus 로고
    • Using proteins in their natural environment: Potential and limitations of microbial whole-cell hydroxylations in applied biocatalysis
    • Duetz, W. A., J. B. van Beilen, and B. Witholt. 2001. Using proteins in their natural environment: potential and limitations of microbial whole-cell hydroxylations in applied biocatalysis. Curr. Opin. Biotechnol. 12:419-425.
    • (2001) Curr. Opin. Biotechnol , vol.12 , pp. 419-425
    • Duetz, W.A.1    van Beilen, J.B.2    Witholt, B.3
  • 8
    • 36148958632 scopus 로고    scopus 로고
    • Engineered alkane-hydroxylating cytochrome P450(BM3) exhibiting nativelike catalytic properties
    • Fasan, R., M. M. Chen, N. C. Crook, and F. H. Arnold. 2007. Engineered alkane-hydroxylating cytochrome P450(BM3) exhibiting nativelike catalytic properties. Angew. Chem. Int. Ed. Engl. 46:8414-8418.
    • (2007) Angew. Chem. Int. Ed. Engl , vol.46 , pp. 8414-8418
    • Fasan, R.1    Chen, M.M.2    Crook, N.C.3    Arnold, F.H.4
  • 9
    • 33745907251 scopus 로고    scopus 로고
    • CYP153A6, a soluble P450 oxygenase catalyzing terminal-alkane hydroxylation
    • Funhoff, E. G., U. Bauer, I. García-Rubio, B. Witholt, and J. B. van Beilen. 2006. CYP153A6, a soluble P450 oxygenase catalyzing terminal-alkane hydroxylation. J. Bacteriol. 188:5220-5227.
    • (2006) J. Bacteriol , vol.188 , pp. 5220-5227
    • Funhoff, E.G.1    Bauer, U.2    García-Rubio, I.3    Witholt, B.4    van Beilen, J.B.5
  • 11
    • 0005732728 scopus 로고
    • Escherichia coli mutator mutants deficient in methylation-instructed DNA mismatch correction
    • Glickman, B. W., and M. Radman. 1980. Escherichia coli mutator mutants deficient in methylation-instructed DNA mismatch correction. Proc. Natl. Acad. Sci. USA 77:1063-1067.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 1063-1067
    • Glickman, B.W.1    Radman, M.2
  • 12
    • 33644852442 scopus 로고    scopus 로고
    • Propane and n-butane oxidation by Pseudomonas putida GPo1
    • Johnson, E. L., and M. R. Hyman. 2006. Propane and n-butane oxidation by Pseudomonas putida GPo1. Appl. Environ. Microbiol. 72:950-952.
    • (2006) Appl. Environ. Microbiol , vol.72 , pp. 950-952
    • Johnson, E.L.1    Hyman, M.R.2
  • 15
    • 0000780695 scopus 로고
    • Formation of polyester by Pseudomonas oleovorans: The effect of substrate on the formation and composition of poly-(R)-3-hydroxyalkanoates and poly-(R)-3-hydroxyalkenoates
    • Lageveen, R. G., G. W. Huisman, H. Preusting, P. E. F. Ketelaar, G. Eggink, and B. Witholt. 1988. Formation of polyester by Pseudomonas oleovorans: the effect of substrate on the formation and composition of poly-(R)-3-hydroxyalkanoates and poly-(R)-3-hydroxyalkenoates. Appl. Environ. Microbiol. 54:2924-2932.
    • (1988) Appl. Environ. Microbiol , vol.54 , pp. 2924-2932
    • Lageveen, R.G.1    Huisman, G.W.2    Preusting, H.3    Ketelaar, P.E.F.4    Eggink, G.5    Witholt, B.6
  • 16
    • 0034801865 scopus 로고    scopus 로고
    • Molecular characterization of the 56-kDa CYP153 from Acinetobacter sp. EB104
    • Maier, T., H. H. Förster, O. Asperger, and U. Hahn. 2001. Molecular characterization of the 56-kDa CYP153 from Acinetobacter sp. EB104. Biochem. Biophys. Res. Commun. 286:652-658.
    • (2001) Biochem. Biophys. Res. Commun , vol.286 , pp. 652-658
    • Maier, T.1    Förster, H.H.2    Asperger, O.3    Hahn, U.4
  • 17
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Miller, J. H. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1972) Experiments in molecular genetics
    • Miller, J.H.1
  • 18
    • 3042797206 scopus 로고    scopus 로고
    • Detection of alkanes, alcohols, and aldehydes using bioluminescence
    • Minak-Bernero, V., R. E. Bare, C. E. Haith, and M. J. Grossman. 2004. Detection of alkanes, alcohols, and aldehydes using bioluminescence. Biotechnol. Bioeng. 87:170-177.
    • (2004) Biotechnol. Bioeng , vol.87 , pp. 170-177
    • Minak-Bernero, V.1    Bare, R.E.2    Haith, C.E.3    Grossman, M.J.4
  • 19
    • 0024328202 scopus 로고
    • Purification of cytochrome P-450 from n-hexadecane-grown Acinetobacter calcoaceticus
    • Müller, R., O. Asperger, and H. P. Kleber. 1989. Purification of cytochrome P-450 from n-hexadecane-grown Acinetobacter calcoaceticus. Biomed. Biochim. Acta 48:243-254.
    • (1989) Biomed. Biochim. Acta , vol.48 , pp. 243-254
    • Müller, R.1    Asperger, O.2    Kleber, H.P.3
  • 20
    • 0016636171 scopus 로고
    • Physiological function of the Pseudomonas putida PpG6 (Pseudomonas oleovorans) alkane hydoxylase: Monoterminal oxidation of alkanes and fatty acids
    • Nieder, M., and J. Shapiro. 1975. Physiological function of the Pseudomonas putida PpG6 (Pseudomonas oleovorans) alkane hydoxylase: monoterminal oxidation of alkanes and fatty acids. J. Bacteriol. 122:93-98.
    • (1975) J. Bacteriol , vol.122 , pp. 93-98
    • Nieder, M.1    Shapiro, J.2
  • 21
    • 33745966649 scopus 로고    scopus 로고
    • Functional expression system for cytochrome P450 genes using the reductase domain of self-sufficient P450RhF from Rhodococcus sp. NCIMB 9784
    • Nodate, M., M. Kubota, and N. Misawa. 2006. Functional expression system for cytochrome P450 genes using the reductase domain of self-sufficient P450RhF from Rhodococcus sp. NCIMB 9784. Appl. Microbiol. Biotechnol. 71:455-462.
    • (2006) Appl. Microbiol. Biotechnol , vol.71 , pp. 455-462
    • Nodate, M.1    Kubota, M.2    Misawa, N.3
  • 22
    • 0242330792 scopus 로고    scopus 로고
    • Regio- and enantioselective alkane hydroxylation with engineered cytochromes P450 BM-3
    • Peters, M. W., P. Meinhold, A. Glieder, and F. H. Arnold. 2003. Regio- and enantioselective alkane hydroxylation with engineered cytochromes P450 BM-3. J. Am. Chem. Soc. 125:13442-13450.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 13442-13450
    • Peters, M.W.1    Meinhold, P.2    Glieder, A.3    Arnold, F.H.4
  • 24
    • 0038201984 scopus 로고    scopus 로고
    • Evidence linking the Pseudomonas oleovorans alkane omega-hydroxylase, an integral membrane diiron enzyme, and the fatty acid desaturase family
    • Shanklin, J., and E. Whittle. 2003. Evidence linking the Pseudomonas oleovorans alkane omega-hydroxylase, an integral membrane diiron enzyme, and the fatty acid desaturase family. FEBS Lett. 545:188-192.
    • (2003) FEBS Lett , vol.545 , pp. 188-192
    • Shanklin, J.1    Whittle, E.2
  • 25
    • 0034847356 scopus 로고    scopus 로고
    • New alkane-responsive expression vectors for E. coli and Pseudomonas
    • Smits, T. H. M., M. A. Seeger, B. Witholt, and J. B. van Beilen. 2001. New alkane-responsive expression vectors for E. coli and Pseudomonas. Plasmid 46:16-24.
    • (2001) Plasmid , vol.46 , pp. 16-24
    • Smits, T.H.M.1    Seeger, M.A.2    Witholt, B.3    van Beilen, J.B.4
  • 26
    • 0036188547 scopus 로고    scopus 로고
    • Functional analysis of alkane hydroxylases from gram-negative and gram-positive bacteria
    • Smits, T. H. M., S. B. Balada, B. Witholt, and J. B. van Beilen. 2002. Functional analysis of alkane hydroxylases from gram-negative and gram-positive bacteria. J. Bacteriol. 184:1733-1742.
    • (2002) J. Bacteriol , vol.184 , pp. 1733-1742
    • Smits, T.H.M.1    Balada, S.B.2    Witholt, B.3    van Beilen, J.B.4
  • 27
    • 0042710128 scopus 로고
    • Benzin, Petroleum, Paraffinöl und Paraffin als Kohlenstoff-und Energiequelle für Mikroben. Zentralbl. Bacteriol. Parasitenk
    • Söhngen, N. L. 1913. Benzin, Petroleum, Paraffinöl und Paraffin als Kohlenstoff-und Energiequelle für Mikroben. Zentralbl. Bacteriol. Parasitenk. 37:595-609.
    • (1913) , vol.37 , pp. 595-609
    • Söhngen, N.L.1
  • 28
    • 0034029787 scopus 로고    scopus 로고
    • Expression, stability and performance of the three-component alkane mono-oxygenase of Pseudomonas oleovorans in Escherichia coli
    • Staijen, I. E., J. B. van Beilen, and B. Witholt. 2000. Expression, stability and performance of the three-component alkane mono-oxygenase of Pseudomonas oleovorans in Escherichia coli. Eur. J. Biochem. 267:1957-1965.
    • (2000) Eur. J. Biochem , vol.267 , pp. 1957-1965
    • Staijen, I.E.1    van Beilen, J.B.2    Witholt, B.3
  • 30
    • 33846621913 scopus 로고    scopus 로고
    • Alkane hydroxylases involved in microbial alkane degradation
    • van Beilen, J. B., and E. G. Funhoff. 2007. Alkane hydroxylases involved in microbial alkane degradation. Appl. Microbiol. Biotechnol. 74:13-21.
    • (2007) Appl. Microbiol. Biotechnol , vol.74 , pp. 13-21
    • van Beilen, J.B.1    Funhoff, E.G.2
  • 32
    • 0028518694 scopus 로고
    • Substrate specificity of the alkane hydroxylase of Pseudomonas oleovorans GPo1
    • van Beilen, J. B., J. Kingma, and B. Witholt. 1994. Substrate specificity of the alkane hydroxylase of Pseudomonas oleovorans GPo1. Enzyme Microb. Technol. 16:904-911.
    • (1994) Enzyme Microb. Technol , vol.16 , pp. 904-911
    • van Beilen, J.B.1    Kingma, J.2    Witholt, B.3
  • 33
    • 17444405636 scopus 로고    scopus 로고
    • Biocatalytic production of perillyl alcohol from limonene using a novel Mycobacterium cytochrome P450 alkane hydroxylase expressed in P. putida
    • van Beilen, J. B., D. Lüscher, R. Holtacker, U. Bauer, B. Witholt, and W. A. Duetz. 2005. Biocatalytic production of perillyl alcohol from limonene using a novel Mycobacterium cytochrome P450 alkane hydroxylase expressed in P. putida. Appl. Environ. Microbiol. 71:1737-1744.
    • (2005) Appl. Environ. Microbiol , vol.71 , pp. 1737-1744
    • van Beilen, J.B.1    Lüscher, D.2    Holtacker, R.3    Bauer, U.4    Witholt, B.5    Duetz, W.A.6
  • 34
    • 0026801560 scopus 로고
    • Topology of the membrane-bound alkane hydroxylase of Pseudomonas oleovorans
    • van Beilen, J. B., D. Penninga, and B. Witholt. 1992. Topology of the membrane-bound alkane hydroxylase of Pseudomonas oleovorans. J. Biol. Chem. 267:9194-9201.
    • (1992) J. Biol. Chem , vol.267 , pp. 9194-9201
    • van Beilen, J.B.1    Penninga, D.2    Witholt, B.3
  • 35
    • 11144307432 scopus 로고    scopus 로고
    • Identification of an amino acid position that determines the substrate range of integral membrane alkane hydroxylases
    • van Beilen, J. B., T. H. M. Smits, F. F. Roos, T. Brunner, S. B. Balada, M. Röthlisberger, and B. Witholt. 2005. Identification of an amino acid position that determines the substrate range of integral membrane alkane hydroxylases. J. Bacteriol. 187:85-91.
    • (2005) J. Bacteriol , vol.187 , pp. 85-91
    • van Beilen, J.B.1    Smits, T.H.M.2    Roos, F.F.3    Brunner, T.4    Balada, S.B.5    Röthlisberger, M.6    Witholt, B.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.