메뉴 건너뛰기




Volumn 374, Issue 2, 2008, Pages 405-410

High-throughput screening assay for d-amino acid oxidase

Author keywords

d Amino acid oxidase; High throughput screening; Membrane; Mutant library; Peroxidase reaction; Recombinant Escherichia coli cells

Indexed keywords

AMINO ACIDS; ESCHERICHIA COLI; ISOMERS; MEMBRANES;

EID: 39149097173     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2007.12.021     Document Type: Article
Times cited : (11)

References (23)
  • 1
    • 0014104819 scopus 로고
    • The utilization of d-amino acids by yeasts
    • La Rue T.A., and Spencer J.F.T. The utilization of d-amino acids by yeasts. Can. J. Microbiol. 13 (1967) 777-788
    • (1967) Can. J. Microbiol. , vol.13 , pp. 777-788
    • La Rue, T.A.1    Spencer, J.F.T.2
  • 5
    • 0037109055 scopus 로고    scopus 로고
    • The discovery of susceptibility genes for mental disorders
    • Cloninger C.R. The discovery of susceptibility genes for mental disorders. Proc. Natl. Acad. Sci. USA 99 (2002) 13365-13367
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13365-13367
    • Cloninger, C.R.1
  • 6
    • 0037308528 scopus 로고    scopus 로고
    • Genes for schizophrenia? Recent findings and their pathophysiological implications
    • Harrison P.J., and Owen M.J. Genes for schizophrenia? Recent findings and their pathophysiological implications. Lancet 361 (2003) 417-419
    • (2003) Lancet , vol.361 , pp. 417-419
    • Harrison, P.J.1    Owen, M.J.2
  • 7
    • 33947251327 scopus 로고    scopus 로고
    • Association of DAOA polymorphisms with schizophrenia and clinical symptoms or therapeutic effects
    • Yue W., Kang G., Zhang Y., Qu M., Tang F., Han Y., Ruan Y., Lu T., Zhang J., and Zhang D. Association of DAOA polymorphisms with schizophrenia and clinical symptoms or therapeutic effects. Neurosci. Lett. 416 (2007) 96-100
    • (2007) Neurosci. Lett. , vol.416 , pp. 96-100
    • Yue, W.1    Kang, G.2    Zhang, Y.3    Qu, M.4    Tang, F.5    Han, Y.6    Ruan, Y.7    Lu, T.8    Zhang, J.9    Zhang, D.10
  • 8
    • 33847133461 scopus 로고    scopus 로고
    • Structural basis of D-DOPA oxidation by d-amino acid oxidase: Alternative pathway for dopamine biosynthesis
    • Kawazoe T., Tsuge H., Imagawa T., Aki K., Kuramitsu S., and Fukui K. Structural basis of D-DOPA oxidation by d-amino acid oxidase: Alternative pathway for dopamine biosynthesis. Biochem. Biophys. Res. Commun. 355 (2007) 385-391
    • (2007) Biochem. Biophys. Res. Commun. , vol.355 , pp. 385-391
    • Kawazoe, T.1    Tsuge, H.2    Imagawa, T.3    Aki, K.4    Kuramitsu, S.5    Fukui, K.6
  • 9
    • 0033679728 scopus 로고    scopus 로고
    • d-Amino acid oxidase: New findings
    • Pilone M.S. d-Amino acid oxidase: New findings. Cell. Mol. Life Sci. 57 (2000) 1732-1747
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 1732-1747
    • Pilone, M.S.1
  • 11
    • 0035892690 scopus 로고    scopus 로고
    • Chiral analysis of amino acids using electrochemical composite bienzyme biosensors
    • Dominguez R., Serra B., Reviejo A.J., and Pingarron J.M. Chiral analysis of amino acids using electrochemical composite bienzyme biosensors. Anal. Biochem. 298 (2001) 275-282
    • (2001) Anal. Biochem. , vol.298 , pp. 275-282
    • Dominguez, R.1    Serra, B.2    Reviejo, A.J.3    Pingarron, J.M.4
  • 12
    • 0242415862 scopus 로고    scopus 로고
    • Development of a d-alanine sensor for the monitoring of a fermentation using the improved selectivity by the combination of d-amino acid oxidase and pyruvate oxidase
    • Inaba Y., Mizukami K., Hamada-Sato N., Kobayashi T., Imada C., and Watanabe E. Development of a d-alanine sensor for the monitoring of a fermentation using the improved selectivity by the combination of d-amino acid oxidase and pyruvate oxidase. Biosens. Bioelectron. 19 (2003) 423-431
    • (2003) Biosens. Bioelectron. , vol.19 , pp. 423-431
    • Inaba, Y.1    Mizukami, K.2    Hamada-Sato, N.3    Kobayashi, T.4    Imada, C.5    Watanabe, E.6
  • 13
    • 0025598210 scopus 로고
    • Continuous conversion to optically pure l-methionine from d-enantiomer contaminated preparations by an immobilized enzyme membrane reactor
    • Nakajima N., Conrad D., Sumi H., Suzuki K., Esaki N., Wandrey C., and Soda K. Continuous conversion to optically pure l-methionine from d-enantiomer contaminated preparations by an immobilized enzyme membrane reactor. J. Ferm. Bioeng. 70 (1990) 322-325
    • (1990) J. Ferm. Bioeng. , vol.70 , pp. 322-325
    • Nakajima, N.1    Conrad, D.2    Sumi, H.3    Suzuki, K.4    Esaki, N.5    Wandrey, C.6    Soda, K.7
  • 14
    • 0037034136 scopus 로고    scopus 로고
    • Deracemisation and stereoinversion of (α-amino acids using d-amino acid oxidase and hydride reducing agents
    • Beard T.M., and Turner N.J. Deracemisation and stereoinversion of (α-amino acids using d-amino acid oxidase and hydride reducing agents. Chem. Commun. (Lond.) 3 (2002) 246-247
    • (2002) Chem. Commun. (Lond.) , vol.3 , pp. 246-247
    • Beard, T.M.1    Turner, N.J.2
  • 15
    • 14844283777 scopus 로고    scopus 로고
    • d-Amino acid oxidase: Structure, catalytic mechanism, and practical application
    • Tishkov V.I., and Khoronenkova S.V. d-Amino acid oxidase: Structure, catalytic mechanism, and practical application. Biochemistry (Mosc.) 70 (2005) 51-67
    • (2005) Biochemistry (Mosc.) , vol.70 , pp. 51-67
    • Tishkov, V.I.1    Khoronenkova, S.V.2
  • 16
    • 0031543435 scopus 로고    scopus 로고
    • Directed evolution of enzyme catalysts
    • Kuchner O., and Arnold F.H. Directed evolution of enzyme catalysts. Trends Biotechnol. 15 (1997) 523-530
    • (1997) Trends Biotechnol. , vol.15 , pp. 523-530
    • Kuchner, O.1    Arnold, F.H.2
  • 17
    • 8444229656 scopus 로고    scopus 로고
    • Modulating d-amino acid oxidase substrate specificity: Production of an enzyme for analytical determination of all d-amino acids by directed evolution
    • Sacchi S., Rosini E., Molla G., Pilone M.S., and Pollegioni L. Modulating d-amino acid oxidase substrate specificity: Production of an enzyme for analytical determination of all d-amino acids by directed evolution. Prot. Eng. Des. Sel. 17 (2004) 517-525
    • (2004) Prot. Eng. Des. Sel. , vol.17 , pp. 517-525
    • Sacchi, S.1    Rosini, E.2    Molla, G.3    Pilone, M.S.4    Pollegioni, L.5
  • 18
    • 14844330150 scopus 로고    scopus 로고
    • Cloning of d-amino acid oxidase gene from yeast Trigonopsis variabilis
    • Davydova E.E., and Tishkov V.I. Cloning of d-amino acid oxidase gene from yeast Trigonopsis variabilis,. Mosc. Univ. Chem. Bull. 43 (2002) 353-355
    • (2002) Mosc. Univ. Chem. Bull. , vol.43 , pp. 353-355
    • Davydova, E.E.1    Tishkov, V.I.2
  • 19
    • 33750066051 scopus 로고    scopus 로고
    • Substrate specificity of d-amino acid oxidase from yeast Trigonopsis variabilis expressed in E. coli cells
    • Savin S.S., Chernyshov I.V., Tishkov V.I., and Khoronenkova S.V. Substrate specificity of d-amino acid oxidase from yeast Trigonopsis variabilis expressed in E. coli cells. Mosc. Univ. Chem. Bull. 47 (2006) 25-30
    • (2006) Mosc. Univ. Chem. Bull. , vol.47 , pp. 25-30
    • Savin, S.S.1    Chernyshov, I.V.2    Tishkov, V.I.3    Khoronenkova, S.V.4
  • 20
    • 0022001813 scopus 로고
    • Isolation and partial characterization of a d-amino acid oxidase active against cephalosporin C from the yeast Trigonopsis variabilis
    • Szwajcer E., and Mosbach K. Isolation and partial characterization of a d-amino acid oxidase active against cephalosporin C from the yeast Trigonopsis variabilis,. Biotechnol. Lett. 7 (1985) 1-7
    • (1985) Biotechnol. Lett. , vol.7 , pp. 1-7
    • Szwajcer, E.1    Mosbach, K.2
  • 21
    • 0034607619 scopus 로고    scopus 로고
    • Substitution of the critical methionine residues in Trigonopsis variabilis d-amino acid oxidase with leucine enhances its resistance to hydrogen peroxide
    • Ju S.-S., Lin L.-L., Chien H.R., and Hsu W.-H. Substitution of the critical methionine residues in Trigonopsis variabilis d-amino acid oxidase with leucine enhances its resistance to hydrogen peroxide. FEMS Microbiol. Lett. 186 (2000) 215-219
    • (2000) FEMS Microbiol. Lett. , vol.186 , pp. 215-219
    • Ju, S.-S.1    Lin, L.-L.2    Chien, H.R.3    Hsu, W.-H.4
  • 22
    • 0034333376 scopus 로고    scopus 로고
    • Detection and substrate selectivity of new microbial d-amino acid oxidases
    • Gabler M., Hensel M., and Fischer L. Detection and substrate selectivity of new microbial d-amino acid oxidases. Enzyme Microb. Technol. 27 (2000) 605-611
    • (2000) Enzyme Microb. Technol. , vol.27 , pp. 605-611
    • Gabler, M.1    Hensel, M.2    Fischer, L.3
  • 23
    • 0015802413 scopus 로고
    • The use of diaminobenzidine for spectrophotometric and acrylamide gel detection of sulfite oxidase and its applicability to hydrogen peroxide-generating enzymes
    • Cohen H.J. The use of diaminobenzidine for spectrophotometric and acrylamide gel detection of sulfite oxidase and its applicability to hydrogen peroxide-generating enzymes. Anal. Biochem. 53 (1973) 208-222
    • (1973) Anal. Biochem. , vol.53 , pp. 208-222
    • Cohen, H.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.