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Volumn 6, Issue , 2016, Pages

In vitro Characterization of Phenylacetate Decarboxylase, a Novel Enzyme Catalyzing Toluene Biosynthesis in an Anaerobic Microbial Community

Author keywords

[No Author keywords available]

Indexed keywords

4-HYDROXYPHENYLACETATE DECARBOXYLASE; AMIDE; CARBOXYLYASE; OXYGEN; RNA 16S; TOLUENE;

EID: 84982095570     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep31362     Document Type: Article
Times cited : (27)

References (21)
  • 2
    • 0022923526 scopus 로고
    • Anoxic hypolimnion is a signifcant source of biogenic toluene
    • Jüttner, F. & Henatsch, J. J. Anoxic hypolimnion is a signifcant source of biogenic toluene. Nature 323, 797-798 (1986).
    • (1986) Nature , vol.323 , pp. 797-798
    • Jüttner, F.1    Henatsch, J.J.2
  • 3
    • 33646492726 scopus 로고
    • Formation of toluene by microorganisms from anoxic freshwater sediments
    • Jüttner, F. Formation of toluene by microorganisms from anoxic freshwater sediments. Fresenius J. Anal. Chem. 339, 785-787 (1991).
    • (1991) Fresenius J. Anal. Chem. , vol.339 , pp. 785-787
    • Jüttner, F.1
  • 4
    • 18644365477 scopus 로고    scopus 로고
    • Formation and biodegradation of toluene in the anaerobic sludge digestion process
    • Mrowiec, B., Suschka, J. & Keener, T. C. Formation and biodegradation of toluene in the anaerobic sludge digestion process. Water Environ. Res. 77, 274-278 (2005).
    • (2005) Water Environ. Res. , vol.77 , pp. 274-278
    • Mrowiec, B.1    Suschka, J.2    Keener, T.C.3
  • 5
    • 0030040522 scopus 로고    scopus 로고
    • Tolumonas auensis gen. Nov., sp. Nov., a toluene-producing bacterium from anoxic sediments of a freshwater lake
    • Fischer-Romero, C., Tindall, B. J. & Juttner, F. Tolumonas auensis gen. nov., sp. nov., a toluene-producing bacterium from anoxic sediments of a freshwater lake. Int. J. Syst. Bacteriol. 46, 183-188, doi: 10.1099/00207713-46-1-183 (1996).
    • (1996) Int. J. Syst. Bacteriol. , vol.46 , pp. 183-188
    • Fischer-Romero, C.1    Tindall, B.J.2    Juttner, F.3
  • 6
    • 0021198657 scopus 로고
    • Biosynthesis of toluene in Clostridium aerofoetidum strain WS
    • Pons, J. L., Rimbault, A., Darbord, J. C. & Leluan, G. [Biosynthesis of toluene in Clostridium aerofoetidum strain WS]. Ann. Microbiol. (Paris) 135B, 219-222 (1984).
    • (1984) Ann. Microbiol. (Paris) , vol.135 B , pp. 219-222
    • Pons, J.L.1    Rimbault, A.2    Darbord, J.C.3    Leluan, G.4
  • 7
    • 0035082791 scopus 로고    scopus 로고
    • P-Hydroxyphenylacetate decarboxylase from Clostridium difcile. A novel glycyl radical enzyme catalysing the formation of p-cresol
    • Selmer, T. & Andrei, P. I. p-Hydroxyphenylacetate decarboxylase from Clostridium difcile. A novel glycyl radical enzyme catalysing the formation of p-cresol. Eur. J. Biochem. 268, 1363-1372 (2001).
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1363-1372
    • Selmer, T.1    Andrei, P.I.2
  • 8
    • 33747127816 scopus 로고    scopus 로고
    • 4-Hydroxyphenylacetate decarboxylases: Properties of a novel subclass of glycyl radical enzyme systems
    • Yu, L., Blaser, M., Andrei, P. I., Pierik, A. J. & Selmer, T. 4-Hydroxyphenylacetate decarboxylases: properties of a novel subclass of glycyl radical enzyme systems. Biochemistry 45, 9584-9592, doi: 10.1021/bi060840b (2006).
    • (2006) Biochemistry , vol.45 , pp. 9584-9592
    • Yu, L.1    Blaser, M.2    Andrei, P.I.3    Pierik, A.J.4    Selmer, T.5
  • 9
    • 2942516028 scopus 로고    scopus 로고
    • Subunit composition of the glycyl radical enzyme p-hydroxyphenylacetate decarboxylase. A small subunit, HpdC, is essential for catalytic activity
    • Andrei, P. I., Pierik, A. J., Zauner, S., Andrei-Selmer, L. C. & Selmer, T. Subunit composition of the glycyl radical enzyme p-hydroxyphenylacetate decarboxylase. A small subunit, HpdC, is essential for catalytic activity. Eur. J. Biochem. 271, 2225-2230, doi: 10.1111/j.1432-1033.2004.04152.x (2004).
    • (2004) Eur. J. Biochem. , vol.271 , pp. 2225-2230
    • Andrei, P.I.1    Pierik, A.J.2    Zauner, S.3    Andrei-Selmer, L.C.4    Selmer, T.5
  • 10
    • 80052784900 scopus 로고    scopus 로고
    • Structural basis for a Kolbe-type decarboxylation catalyzed by a glycyl radical enzyme
    • Martins, B. M. et al. Structural basis for a Kolbe-type decarboxylation catalyzed by a glycyl radical enzyme. J. Am. Chem. Soc. 133, 14666-14674, doi: 10.1021/ja203344x (2011).
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 14666-14674
    • Martins, B.M.1
  • 11
    • 84885092792 scopus 로고    scopus 로고
    • Catalytic mechanism of the glycyl radical enzyme 4-hydroxyphenylacetate decarboxylase from continuum electrostatic and QC/MM calculations
    • Feliks, M., Martins, B. M. & Ullmann, G. M. Catalytic mechanism of the glycyl radical enzyme 4-hydroxyphenylacetate decarboxylase from continuum electrostatic and QC/MM calculations. J. Am. Chem. Soc. 135, 14574-14585, doi: 10.1021/ja402379q (2013).
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 14574-14585
    • Feliks, M.1    Martins, B.M.2    Ullmann, G.M.3
  • 12
    • 80054951249 scopus 로고    scopus 로고
    • Complete genome sequence of Tolumonas auensis type strain (TA 4)
    • Chertkov, O. et al. Complete genome sequence of Tolumonas auensis type strain (TA 4). Stand. Genomic Sci. 5, 112-120, doi: 10.4056/sigs.2184986 (2011).
    • (2011) Stand. Genomic Sci. , vol.5 , pp. 112-120
    • Chertkov, O.1
  • 13
    • 63849112848 scopus 로고    scopus 로고
    • Anaerobic catabolism of aromatic compounds: A genetic and genomic view
    • Carmona, M. et al. Anaerobic catabolism of aromatic compounds: a genetic and genomic view. Microbiol. Mol. Biol. Rev. 73, 71-133, doi: 10.1128/MMBR.00021-08 (2009).
    • (2009) Microbiol. Mol. Biol. Rev. , vol.73 , pp. 71-133
    • Carmona, M.1
  • 14
    • 27644532857 scopus 로고    scopus 로고
    • New glycyl radical enzymes catalysing key metabolic steps in anaerobic bacteria
    • Selmer, T., Pierik, A. J. & Heider, J. New glycyl radical enzymes catalysing key metabolic steps in anaerobic bacteria. Biol. Chem. 386, 981-988, doi: 10.1515/BC.2005.114 (2005).
    • (2005) Biol. Chem. , vol.386 , pp. 981-988
    • Selmer, T.1    Pierik, A.J.2    Heider, J.3
  • 17
    • 84871952399 scopus 로고    scopus 로고
    • Carboxylic acid reductase is a versatile enzyme for the conversion of fatty acids into fuels and chemical commodities
    • Akhtar, M. K., Turner, N. J. & Jones, P. R. Carboxylic acid reductase is a versatile enzyme for the conversion of fatty acids into fuels and chemical commodities. Proc. Natl. Acad. Sci. USA 110, 87-92, doi: 10.1073/pnas.1216516110 (2013).
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 87-92
    • Akhtar, M.K.1    Turner, N.J.2    Jones, P.R.3
  • 18
    • 79954995511 scopus 로고    scopus 로고
    • Conversion of fatty aldehydes to alka(e)nes and formate by a cyanobacterial aldehyde decarbonylase: Cryptic redox by an unusual dimetal oxygenase
    • Li, N. et al. Conversion of fatty aldehydes to alka(e)nes and formate by a cyanobacterial aldehyde decarbonylase: cryptic redox by an unusual dimetal oxygenase. J. Am. Chem. Soc. 133, 6158-6161, doi: 10.1021/ja2013517 (2011).
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 6158-6161
    • Li, N.1
  • 19
    • 84867482224 scopus 로고    scopus 로고
    • Evidence for only oxygenative cleavage of aldehydes to alk(a/e)nes and formate by cyanobacterial aldehyde decarbonylases
    • Li, N. et al. Evidence for only oxygenative cleavage of aldehydes to alk(a/e)nes and formate by cyanobacterial aldehyde decarbonylases. Biochemistry 51, 7908-7916, doi: 10.1021/bi300912n (2012).
    • (2012) Biochemistry , vol.51 , pp. 7908-7916
    • Li, N.1
  • 20
    • 84866452468 scopus 로고    scopus 로고
    • Genetic manipulation of the obligate chemolithoautotrophic bacterium Tiobacillus denitrifcans
    • Beller, H. R., Legler, T. C. & Kane, S. R. Genetic manipulation of the obligate chemolithoautotrophic bacterium Tiobacillus denitrifcans. Methods Mol. Biol. 881, 99-136, doi: 10.1007/978-1-61779-827-6-5 (2012).
    • (2012) Methods Mol. Biol. , vol.881 , pp. 99-136
    • Beller, H.R.1    Legler, T.C.2    Kane, S.R.3
  • 21
    • 0032814964 scopus 로고    scopus 로고
    • Substrate range of benzylsuccinate synthase from Azoarcus sp. Strain T
    • Beller, H. R. & Spormann, A. M. Substrate range of benzylsuccinate synthase from Azoarcus sp. strain T. FEMS Microbiol. Lett. 178, 147-153 (1999).
    • (1999) FEMS Microbiol. Lett. , vol.178 , pp. 147-153
    • Beller, H.R.1    Spormann, A.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.