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Volumn 76, Issue 21, 2010, Pages 7029-7035

Product-induced gene expression, a product-responsive reporter assay used to screen metagenomic libraries for enzyme-encoding genes

Author keywords

[No Author keywords available]

Indexed keywords

96-WELL FORMAT; AMIDASE; BENZAMIDES; E. COLI; ENCODING GENES; GREEN FLUORESCENT PROTEIN; L-AMINO ACIDS; LIBRARY CELLS; METAGENOMIC LIBRARIES; PRODUCT DETECTION; REPORTER ASSAY; SCREENING METHODS; SENSOR CELLS; TRANSCRIPTIONAL ACTIVATORS; VARIOUS SUBSTRATES;

EID: 78149437429     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.00464-10     Document Type: Article
Times cited : (112)

References (30)
  • 1
    • 0028946084 scopus 로고
    • Phylogenetic identification and in situ detection of individual microbial cells without cultivation
    • Amann, R., W. Ludwig, and K. H. Schleifer. 1995. Phylogenetic identification and in situ detection of individual microbial cells without cultivation. Microbiol. Rev. 59:143-169.
    • (1995) Microbiol. Rev. , vol.59 , pp. 143-169
    • Amann, R.1    Ludwig, W.2    Schleifer, K.H.3
  • 4
    • 0000093464 scopus 로고
    • An absorption apparatus for the microdetermination of certain volatile substances
    • I. The microdetermination of ammonia
    • Conway, E. J., and A. Byrne. 1933. An absorption apparatus for the microdetermination of certain volatile substances. I. The microdetermination of ammonia. Biochem. J. 27:419-429.
    • (1933) Biochem. J. , vol.27 , pp. 419-429
    • Conway, E.J.1    Byrne, A.2
  • 6
    • 0028096012 scopus 로고
    • Purification and characterization of an L-amino amidase from Mycobacterium neoaurum ATCC 25795
    • Hermes, H. F., R. F. Tandler, T. Sonke, L. Dijkhuizen, and E. M. Meijer. 1994. Purification and characterization of an L-amino amidase from Mycobacterium neoaurum ATCC 25795. Appl. Environ. Microbiol. 1:153-159.
    • (1994) Appl. Environ. Microbiol. , vol.1 , pp. 153-159
    • Hermes, H.F.1    Tandler, R.F.2    Sonke, T.3    Dijkhuizen, L.4    Meijer, E.M.5
  • 7
    • 0029996889 scopus 로고    scopus 로고
    • Purification and properties of an amidase from Rhodococcus erythropolis MP50 which enantioselectively hydrolyzes 2-arylpropionamides
    • Hirrlinger, B., A. Stolz, and H. J. Knackmuss. 1996. Purification and properties of an amidase from Rhodococcus erythropolis MP50 which enantioselectively hydrolyzes 2-arylpropionamides. J. Bacteriol. 178:3501-3507.
    • (1996) J. Bacteriol. , vol.178 , pp. 3501-3507
    • Hirrlinger, B.1    Stolz, A.2    Knackmuss, H.J.3
  • 8
    • 28644452655 scopus 로고    scopus 로고
    • Purification, characterization, gene cloning and nucleotide sequencing of D-stereospecific amino acid amidase from soil bacterium: Delftia acidovorans
    • Hongpattarakere, T., H. Komeda, and Y. Asano. 2005. Purification, characterization, gene cloning and nucleotide sequencing of D-stereospecific amino acid amidase from soil bacterium: Delftia acidovorans. J. Ind. Microbiol. Biotechnol. 32:567-576.
    • (2005) J. Ind. Microbiol. Biotechnol. , vol.32 , pp. 567-576
    • Hongpattarakere, T.1    Komeda, H.2    Asano, Y.3
  • 10
    • 0030700490 scopus 로고    scopus 로고
    • Identification of active sites in amidase: Evolutionary relationship between amide bond- and peptide bond-cleaving enzymes
    • Kobayashi, M., Y. Fujiwara, M. Goda, H. Komeda, and S. Shimizu. 1997. Identification of active sites in amidase: Evolutionary relationship between amide bond- and peptide bond-cleaving enzymes. Proc. Natl. Acad. Sci. U. S. A. 94:11986-11991.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 11986-11991
    • Kobayashi, M.1    Fujiwara, Y.2    Goda, M.3    Komeda, H.4    Shimizu, S.5
  • 11
    • 0034067403 scopus 로고    scopus 로고
    • Gene cloning, nucleotide sequencing, and purification and characterization of the D-stereospecific amino-acid amidase from Ochrobactrum anthropi SV3
    • Komeda, H., and Y. Asano. 2000. Gene cloning, nucleotide sequencing, and purification and characterization of the D-stereospecific amino-acid amidase from Ochrobactrum anthropi SV3. Eur. J. Biochem. 267:2028-2035.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2028-2035
    • Komeda, H.1    Asano, Y.2
  • 12
    • 0346007406 scopus 로고    scopus 로고
    • Screening for amidases: Isolation and characterization of a novel D-amidase from Variovorax paradoxus
    • Krieg, L., M. B. Ansorge-Schumacher, and M. R. Kula. 2002. Screening for amidases: Isolation and characterization of a novel D-amidase from Variovorax paradoxus. Adv. Synth. Catal. 344:965-973.
    • (2002) Adv. Synth. Catal. , vol.344 , pp. 965-973
    • Krieg, L.1    Ansorge-Schumacher, M.B.2    Kula, M.R.3
  • 13
    • 3242887157 scopus 로고    scopus 로고
    • CD-Search: Protein domain annotations on the fly
    • Marchler-Bauer, A., and S. H. Bryant. 2004. CD-Search: Protein domain annotations on the fly. Nucleic Acids Res. 32:W327-W331.
    • (2004) Nucleic Acids Res. , vol.32
    • Marchler-Bauer, A.1    Bryant, S.H.2
  • 14
    • 33644956913 scopus 로고    scopus 로고
    • Surveying biotransformations with à la carte genetic traps: Translating dehydrochlorination of lindane (gamma-hexachlorocyclohexane) into lacZ-based phenotypes
    • Mohn, W. W., J. Garmenda, T. C. Galvao, and V. de Lorenzo. 2006. Surveying biotransformations with à la carte genetic traps: Translating dehydrochlorination of lindane (gamma-hexachlorocyclohexane) into lacZ-based phenotypes. Environ. Micobiol. 8:546-555.
    • (2006) Environ. Micobiol. , vol.8 , pp. 546-555
    • Mohn, W.W.1    Garmenda, J.2    Galvao, T.C.3    De Lorenzo, V.4
  • 15
    • 71649107994 scopus 로고    scopus 로고
    • Structure and characterization of amidase from Rhodococcus sp. N-771: Insight into the molecular mechanism of substrate recognition
    • Ohtaki, A., K. Murata, Y. Sato, K. Noguchi, H. Miyatake, N. Dohmae, K. Yamada, M. Yohda, and M. Odaka. 2010. Structure and characterization of amidase from Rhodococcus sp. N-771: Insight into the molecular mechanism of substrate recognition. Biochim. Biophys. Acta 1804:184-192.
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 184-192
    • Ohtaki, A.1    Murata, K.2    Sato, Y.3    Noguchi, K.4    Miyatake, H.5    Dohmae, N.6    Yamada, K.7    Yohda, M.8    Odaka, M.9
  • 16
    • 0029853148 scopus 로고    scopus 로고
    • WWW-Query: An on-line retrieval system for biological sequence banks
    • Perrière, G., and M. Gouy. 1996. WWW-Query: An on-line retrieval system for biological sequence banks. Biochimie 78:364-369.
    • (1996) Biochimie , vol.78 , pp. 364-369
    • Perrière, G.1    Gouy, M.2
  • 17
    • 0037816429 scopus 로고    scopus 로고
    • Microplate bioassay for nisin in foods, based on nisin-induced green fluorescent protein fluorescence
    • Reunanen, J., and P. E. J. Saris. 2003. Microplate bioassay for nisin in foods, based on nisin-induced green fluorescent protein fluorescence. Appl. Environ. Microbiol. 69:4214-4218.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 4214-4218
    • Reunanen, J.1    Saris, P.E.J.2
  • 18
    • 34249942470 scopus 로고    scopus 로고
    • Biosensing environmental pollution
    • Ron, E. Z. 2007. Biosensing environmental pollution. Curr. Opin. Biotechnol. 18:252-256.
    • (2007) Curr. Opin. Biotechnol. , vol.18 , pp. 252-256
    • Ron, E.Z.1
  • 19
    • 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
  • 20
    • 0346334534 scopus 로고    scopus 로고
    • The substrate specificity of the heat-stable stereospecific amidase from Klebsiella oxytoca
    • Shaw, N. M., and A. B. Naughton. 2004. The substrate specificity of the heat-stable stereospecific amidase from Klebsiella oxytoca. Tetrahedron 60: 747-752.
    • (2004) Tetrahedron , vol.60 , pp. 747-752
    • Shaw, N.M.1    Naughton, A.B.2
  • 22
    • 34547748431 scopus 로고    scopus 로고
    • Functional screening of a metagenomic library for genes involved in microbial degradation of aromatic compounds
    • Suenaga, H., T. Ohnuki, and K. Miyazaki. 2007. Functional screening of a metagenomic library for genes involved in microbial degradation of aromatic compounds. Environ. Microbiol. 9:2289-2297.
    • (2007) Environ. Microbiol. , vol.9 , pp. 2289-2297
    • Suenaga, H.1    Ohnuki, T.2    Miyazaki, K.3
  • 23
    • 31944449023 scopus 로고    scopus 로고
    • Information from single-cell bacterial biosensors: What is it good for?
    • Tecon, R., and J. R. van der Meer. 2006. Information from single-cell bacterial biosensors: What is it good for? Curr. Opin. Biotechnol. 17:4-10.
    • (2006) Curr. Opin. Biotechnol. , vol.17 , pp. 4-10
    • Tecon, R.1    Van Der Meer, J.R.2
  • 24
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 25
    • 19144369096 scopus 로고    scopus 로고
    • Substrate-induced gene-expression screening of environmental metagenome libraries for isolation of catabolic genes
    • Uchiyama, T., T. Abe, T. Ikemura, and K. Watanabe. 2005. Substrate-induced gene-expression screening of environmental metagenome libraries for isolation of catabolic genes. Nat. Biotechnol. 23:88-93.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 88-93
    • Uchiyama, T.1    Abe, T.2    Ikemura, T.3    Watanabe, K.4
  • 26
    • 70449727646 scopus 로고    scopus 로고
    • Functional metagenomics for enzyme discovery: Challenges to efficient screening
    • Uchiyama, T., and K. Miyazaki. 2009. Functional metagenomics for enzyme discovery: Challenges to efficient screening. Curr. Opin. Biotechnol. 20:616-622.
    • (2009) Curr. Opin. Biotechnol. , vol.20 , pp. 616-622
    • Uchiyama, T.1    Miyazaki, K.2
  • 28
    • 0042433508 scopus 로고    scopus 로고
    • A novel esterase from a psychrotrophic bacterium, Acinetobacter sp. strain no. 6, that belongs to the amidase signature family
    • Wei, Y., T. Kurihara, T. Suzuki, and N. Esaki. 2003. A novel esterase from a psychrotrophic bacterium, Acinetobacter sp. strain no. 6, that belongs to the amidase signature family. J. Mol. Catal. B Enzym. 23:357-365.
    • (2003) J. Mol. Catal. B Enzym. , vol.23 , pp. 357-365
    • Wei, Y.1    Kurihara, T.2    Suzuki, T.3    Esaki, N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.