메뉴 건너뛰기




Volumn 29, Issue 6, 2011, Pages 276-283

New biotech applications from evolved D-amino acid oxidases

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOCATALYSTS; BIOTECHNOLOGY; HERBICIDES; OXYGEN; PLANTS (BOTANY);

EID: 79956146208     PISSN: 01677799     EISSN: 18793096     Source Type: Journal    
DOI: 10.1016/j.tibtech.2011.01.010     Document Type: Review
Times cited : (125)

References (61)
  • 1
    • 33645986474 scopus 로고    scopus 로고
    • Preparative deracemization of unnatural amino acids
    • Fotheringham I., et al. Preparative deracemization of unnatural amino acids. Biochem. Soc. Trans. 2006, 34:287-290.
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 287-290
    • Fotheringham, I.1
  • 3
    • 34250002745 scopus 로고    scopus 로고
    • Physiological functions of d-amino acid oxidases: from yeast to humans
    • Pollegioni L., et al. Physiological functions of d-amino acid oxidases: from yeast to humans. Cell. Mol. Life Sci. 2007, 64:1373-1394.
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 1373-1394
    • Pollegioni, L.1
  • 4
    • 0033741877 scopus 로고    scopus 로고
    • The X-ray structure of d-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation
    • Umhau S., et al. The X-ray structure of d-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation. Proc. Natl. Acad. Sci. U.S.A. 2000, 97:12463-12468.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 12463-12468
    • Umhau, S.1
  • 5
    • 0033579446 scopus 로고    scopus 로고
    • Studies on the reaction mechanism of Rhodotorula gracilis d-amino-acid oxidase. Role of the highly conserved Tyr-223 on substrate binding and catalysis
    • Harris C.M., et al. Studies on the reaction mechanism of Rhodotorula gracilis d-amino-acid oxidase. Role of the highly conserved Tyr-223 on substrate binding and catalysis. J. Biol. Chem. 1999, 274:36233-36240.
    • (1999) J. Biol. Chem. , vol.274 , pp. 36233-36240
    • Harris, C.M.1
  • 6
    • 0034637448 scopus 로고    scopus 로고
    • Role of arginine 285 in the active site of Rhodotorula gracilis d-amino acid oxidase. A site-directed mutagenesis study
    • Molla G., et al. Role of arginine 285 in the active site of Rhodotorula gracilis d-amino acid oxidase. A site-directed mutagenesis study. J. Biol. Chem. 2000, 275:24715-24721.
    • (2000) J. Biol. Chem. , vol.275 , pp. 24715-24721
    • Molla, G.1
  • 7
    • 0032839957 scopus 로고    scopus 로고
    • Chemistry, nutrition, and microbiology of d-amino acids
    • Friedman M. Chemistry, nutrition, and microbiology of d-amino acids. J. Agric. Food. Chem. 1999, 47:3457-3479.
    • (1999) J. Agric. Food. Chem. , vol.47 , pp. 3457-3479
    • Friedman, M.1
  • 8
  • 9
    • 38349169149 scopus 로고    scopus 로고
    • Engineering the properties of d-amino acid oxidases by a rational and a directed evolution approach
    • Pollegioni L. Engineering the properties of d-amino acid oxidases by a rational and a directed evolution approach. Curr. Protein Pept. Sci. 2007, 8:600-618.
    • (2007) Curr. Protein Pept. Sci. , vol.8 , pp. 600-618
    • Pollegioni, L.1
  • 10
    • 38349152169 scopus 로고    scopus 로고
    • Properties and applications of microbial d-amino acid oxidases: current state and perspectives
    • Pollegioni L., et al. Properties and applications of microbial d-amino acid oxidases: current state and perspectives. Appl. Microbiol. Biotechnol. 2008, 78:1-16.
    • (2008) Appl. Microbiol. Biotechnol. , vol.78 , pp. 1-16
    • Pollegioni, L.1
  • 11
    • 77951228730 scopus 로고    scopus 로고
    • Stepwise engineering of a Pichia pastoris d-amino acid oxidase whole cell catalyst
    • Abad S., et al. Stepwise engineering of a Pichia pastoris d-amino acid oxidase whole cell catalyst. Microb. Cell Fact. 2010, 9:24.
    • (2010) Microb. Cell Fact. , vol.9 , pp. 24
    • Abad, S.1
  • 12
    • 79951772572 scopus 로고    scopus 로고
    • High-level expression of Rhodotorula gracilis d-amino acid oxidase in Pichia pastoris
    • Abad S., et al. High-level expression of Rhodotorula gracilis d-amino acid oxidase in Pichia pastoris. Biotechnol. Lett. 2010, 10.1007/s10529-010-0456-9.
    • (2010) Biotechnol. Lett.
    • Abad, S.1
  • 13
    • 0034333376 scopus 로고    scopus 로고
    • Detection and substrate selectivity of new microbial d-amino acid oxidases
    • Gabler M., et al. Detection and substrate selectivity of new microbial d-amino acid oxidases. Enzyme Microb. Technol. 2000, 27:605-611.
    • (2000) Enzyme Microb. Technol. , vol.27 , pp. 605-611
    • Gabler, M.1
  • 14
    • 78650645142 scopus 로고    scopus 로고
    • Use of enzymes in the production of semi-synthetic penicillins and cephalosporins: drawbacks and perspectives
    • Volpato G., et al. Use of enzymes in the production of semi-synthetic penicillins and cephalosporins: drawbacks and perspectives. Curr. Med. Chem. 2010, 17:3855-3873.
    • (2010) Curr. Med. Chem. , vol.17 , pp. 3855-3873
    • Volpato, G.1
  • 15
    • 28844433711 scopus 로고    scopus 로고
    • Evolution of an acylase active on cephalosporin C
    • Pollegioni L., et al. Evolution of an acylase active on cephalosporin C. Protein Sci. 2005, 14:3064-3076.
    • (2005) Protein Sci. , vol.14 , pp. 3064-3076
    • Pollegioni, L.1
  • 16
    • 77952507592 scopus 로고    scopus 로고
    • A single Phe54Tyr substitution improves the catalytic activity and thermostability of Trigonopsis variabilis d-amino acid oxidase
    • Wong K.S., et al. A single Phe54Tyr substitution improves the catalytic activity and thermostability of Trigonopsis variabilis d-amino acid oxidase. New Biotechnol. 2010, 27:78-84.
    • (2010) New Biotechnol. , vol.27 , pp. 78-84
    • Wong, K.S.1
  • 17
    • 0037457704 scopus 로고    scopus 로고
    • Fusion protein of Vitreoscilla hemoglobin with d-amino acid oxidase enhances activity and stability of biocatalyst in the bioconversion process of cephalosporin C
    • Khang Y., et al. Fusion protein of Vitreoscilla hemoglobin with d-amino acid oxidase enhances activity and stability of biocatalyst in the bioconversion process of cephalosporin C. Biotechnol. Bioeng. 2003, 82:480-488.
    • (2003) Biotechnol. Bioeng. , vol.82 , pp. 480-488
    • Khang, Y.1
  • 18
    • 70349331253 scopus 로고    scopus 로고
    • Triple fusion of d-amino acid oxidase from Trigonopsis variabilis with polyhistidine and Vitreoscilla hemoglobin
    • Ma X.-F., et al. Triple fusion of d-amino acid oxidase from Trigonopsis variabilis with polyhistidine and Vitreoscilla hemoglobin. World J. Microb. Biotechnol. 2009, 25:1353-1361.
    • (2009) World J. Microb. Biotechnol. , vol.25 , pp. 1353-1361
    • Ma, X.-F.1
  • 19
    • 77955288875 scopus 로고    scopus 로고
    • + relay system in d-amino acid oxidase
    • + relay system in d-amino acid oxidase. J. Biol. Chem. 2010, 285:24439-24446.
    • (2010) J. Biol. Chem. , vol.285 , pp. 24439-24446
    • Saam, J.1
  • 20
    • 68849129382 scopus 로고    scopus 로고
    • Optimization of d-amino acid oxidase for low substrate concentrations-towards a cancer enzyme therapy
    • Rosini E., et al. Optimization of d-amino acid oxidase for low substrate concentrations-towards a cancer enzyme therapy. FEBS J. 2009, 276:4921-4932.
    • (2009) FEBS J. , vol.276 , pp. 4921-4932
    • Rosini, E.1
  • 21
    • 78751660876 scopus 로고    scopus 로고
    • 2 diffusion pathways and enhancement of the reactivity
    • 2 diffusion pathways and enhancement of the reactivity. FEBS J. 2010, 278:482-492.
    • (2010) FEBS J. , vol.278 , pp. 482-492
    • Rosini, E.1
  • 23
    • 3342965284 scopus 로고    scopus 로고
    • Construction and application of fusion proteins of d-amino acid oxidase and glutaryl-7-aminocephalosporanic acid acylase for direct bioconversion of cephalosporin C to 7-aminocephalosporanic acid
    • Luo H., et al. Construction and application of fusion proteins of d-amino acid oxidase and glutaryl-7-aminocephalosporanic acid acylase for direct bioconversion of cephalosporin C to 7-aminocephalosporanic acid. Biotechnol. Lett. 2004, 26:939-945.
    • (2004) Biotechnol. Lett. , vol.26 , pp. 939-945
    • Luo, H.1
  • 24
    • 34147108343 scopus 로고    scopus 로고
    • Construction of recombinant Escherichia coli D11/pMSTO and its use in enzymatic preparation of 7-aminocephalosporanic acid in one-pot
    • Zheng H., et al. Construction of recombinant Escherichia coli D11/pMSTO and its use in enzymatic preparation of 7-aminocephalosporanic acid in one-pot. J. Biotechnol. 2007, 129:400-405.
    • (2007) J. Biotechnol. , vol.129 , pp. 400-405
    • Zheng, H.1
  • 25
    • 33750530198 scopus 로고    scopus 로고
    • Enzymatic conversion of unnatural amino acids by yeast d-amino acid oxidase
    • Caligiuri A., et al. Enzymatic conversion of unnatural amino acids by yeast d-amino acid oxidase. Adv. Synth. Catal. 2006, 348:2183-2190.
    • (2006) Adv. Synth. Catal. , vol.348 , pp. 2183-2190
    • Caligiuri, A.1
  • 26
    • 33845547114 scopus 로고    scopus 로고
    • Multistep enzyme catalysed deracemisation of 2-naphthyl alanine
    • Caligiuri A., et al. Multistep enzyme catalysed deracemisation of 2-naphthyl alanine. Biocatal. Biotransform. 2006, 24:409-413.
    • (2006) Biocatal. Biotransform. , vol.24 , pp. 409-413
    • Caligiuri, A.1
  • 27
    • 36749041423 scopus 로고    scopus 로고
    • Biotransformation of d-methionine into l-methionine in the cascade of four enzymes
    • Findrik Z., Vasić-Racki D. Biotransformation of d-methionine into l-methionine in the cascade of four enzymes. Biotechnol. Bioeng. 2007, 98:956-967.
    • (2007) Biotechnol. Bioeng. , vol.98 , pp. 956-967
    • Findrik, Z.1    Vasić-Racki, D.2
  • 28
    • 84860135513 scopus 로고    scopus 로고
    • A simple enzymatic method for production of a wide variety of d-amino acids using l-amino acid oxidase from Rhodococcus sp. AIU Z-35-1
    • Isobe K., et al. A simple enzymatic method for production of a wide variety of d-amino acids using l-amino acid oxidase from Rhodococcus sp. AIU Z-35-1. Enzyme Res. 2010, 10.4061/2010/567210.
    • (2010) Enzyme Res.
    • Isobe, K.1
  • 29
    • 33746362592 scopus 로고    scopus 로고
    • D-Serine signalling in the brain: friend and foe
    • Martineau M., et al. d-Serine signalling in the brain: friend and foe. Trends Neurosci. 2006, 29:481-491.
    • (2006) Trends Neurosci. , vol.29 , pp. 481-491
    • Martineau, M.1
  • 30
    • 77954584505 scopus 로고    scopus 로고
    • Metabolism of the neuromodulator d-serine
    • Pollegioni L., Sacchi S. Metabolism of the neuromodulator d-serine. Cell. Mol. Life Sci. 2010, 67:2387-2404.
    • (2010) Cell. Mol. Life Sci. , vol.67 , pp. 2387-2404
    • Pollegioni, L.1    Sacchi, S.2
  • 31
    • 0037108758 scopus 로고    scopus 로고
    • Genetic and physiological data implicating the new human gene G72 and the gene for d-amino acid oxidase in schizophrenia
    • Chumakov I., et al. Genetic and physiological data implicating the new human gene G72 and the gene for d-amino acid oxidase in schizophrenia. Proc. Natl. Acad. Sci. U.S.A. 2002, 99:13675-13680.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 13675-13680
    • Chumakov, I.1
  • 32
    • 0037977113 scopus 로고    scopus 로고
    • Decreased serum levels of d-serine in patients with schizophrenia: evidence in support of the N-methyl-d-aspartate receptor hypofunction hypothesis of schizophrenia
    • Hashimoto K., et al. Decreased serum levels of d-serine in patients with schizophrenia: evidence in support of the N-methyl-d-aspartate receptor hypofunction hypothesis of schizophrenia. Arch. Gen. Psychiatry 2003, 60:572-576.
    • (2003) Arch. Gen. Psychiatry , vol.60 , pp. 572-576
    • Hashimoto, K.1
  • 33
    • 32144442536 scopus 로고    scopus 로고
    • D-Alanine added to antipsychotics for the treatment of schizophrenia
    • Tsai G.E., et al. d-Alanine added to antipsychotics for the treatment of schizophrenia. Biol. Psychiatry 2006, 59:230-234.
    • (2006) Biol. Psychiatry , vol.59 , pp. 230-234
    • Tsai, G.E.1
  • 34
    • 33846640657 scopus 로고    scopus 로고
    • A CSF and postmortem brain study of d-serine metabolic parameters in schizophrenia
    • Bendikov I., et al. A CSF and postmortem brain study of d-serine metabolic parameters in schizophrenia. Schizophr. Res. 2007, 90:41-51.
    • (2007) Schizophr. Res. , vol.90 , pp. 41-51
    • Bendikov, I.1
  • 35
    • 52049087606 scopus 로고    scopus 로고
    • PLG72 modulates intracellular d-serine levels through its interaction with d-amino acid oxidase: effect on schizophrenia susceptibility
    • Sacchi S., et al. pLG72 modulates intracellular d-serine levels through its interaction with d-amino acid oxidase: effect on schizophrenia susceptibility. J. Biol. Chem. 2008, 283:22244-22256.
    • (2008) J. Biol. Chem. , vol.283 , pp. 22244-22256
    • Sacchi, S.1
  • 36
    • 73949129296 scopus 로고    scopus 로고
    • Spinal d-amino acid oxidase contributes to neuropathic pain in rats
    • Zhao W.J., et al. Spinal d-amino acid oxidase contributes to neuropathic pain in rats. J. Pharmacol. Exp. Ther. 2010, 332:248-254.
    • (2010) J. Pharmacol. Exp. Ther. , vol.332 , pp. 248-254
    • Zhao, W.J.1
  • 37
    • 0035892690 scopus 로고    scopus 로고
    • Chiral analysis of amino acids using electrochemical composite bienzyme biosensors
    • Dominguez R., et al. Chiral analysis of amino acids using electrochemical composite bienzyme biosensors. Anal. Biochem. 2001, 298:275-282.
    • (2001) Anal. Biochem. , vol.298 , pp. 275-282
    • Dominguez, R.1
  • 38
    • 0043093696 scopus 로고    scopus 로고
    • Biosensors for the enantioselective analysis of pipecolic acid
    • Stefan R.I., et al. Biosensors for the enantioselective analysis of pipecolic acid. Sens. Actuators B: Chem. 2003, 94:271-275.
    • (2003) Sens. Actuators B: Chem. , vol.94 , pp. 271-275
    • Stefan, R.I.1
  • 39
    • 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., et al. 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. 2003, 19:423-431.
    • (2003) Biosens. Bioelectron. , vol.19 , pp. 423-431
    • Inaba, Y.1
  • 40
    • 77955759800 scopus 로고    scopus 로고
    • Simultaneous determination of l- and d-T4 using a sequential injection analysis sensors system
    • van Staden R.I., et al. Simultaneous determination of l- and d-T4 using a sequential injection analysis sensors system. Comb. Chem. High Throughput Screen 2010, 13:497-501.
    • (2010) Comb. Chem. High Throughput Screen , vol.13 , pp. 497-501
    • van Staden, R.I.1
  • 41
    • 0242469040 scopus 로고    scopus 로고
    • Simultaneous determination of l- and d-methotrexate using a sequential injection analysis/amperometric biosensors system
    • Stefan R.I., et al. Simultaneous determination of l- and d-methotrexate using a sequential injection analysis/amperometric biosensors system. Biosens. Bioelectron. 2003, 19:261-267.
    • (2003) Biosens. Bioelectron. , vol.19 , pp. 261-267
    • Stefan, R.I.1
  • 42
    • 0037178821 scopus 로고    scopus 로고
    • Engineering the substrate specificity of d-amino acid oxidase
    • Sacchi S., et al. Engineering the substrate specificity of d-amino acid oxidase. J. Biol. Chem. 2002, 277:27510-27516.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27510-27516
    • Sacchi, S.1
  • 43
    • 47249104179 scopus 로고    scopus 로고
    • A biosensor for all d-amino acids using evolved d-amino acid oxidase
    • Rosini E., et al. A biosensor for all d-amino acids using evolved d-amino acid oxidase. J. Biotechnol. 2008, 135:377-384.
    • (2008) J. Biotechnol. , vol.135 , pp. 377-384
    • Rosini, E.1
  • 44
    • 41149095096 scopus 로고    scopus 로고
    • Characterization of a yeast d-amino acid oxidase microbiosensor for d-serine detection in the central nervous system
    • Pernot P., et al. Characterization of a yeast d-amino acid oxidase microbiosensor for d-serine detection in the central nervous system. Anal. Chem. 2008, 80:1589-1597.
    • (2008) Anal. Chem. , vol.80 , pp. 1589-1597
    • Pernot, P.1
  • 45
    • 38149040091 scopus 로고    scopus 로고
    • In vitro and in vivo pharmacological profile of AS057278, a selective d-amino acid oxidase inhibitor with potential anti-psychotic properties
    • Adage T., et al. In vitro and in vivo pharmacological profile of AS057278, a selective d-amino acid oxidase inhibitor with potential anti-psychotic properties. Eur. Neuropsychopharmacol. 2008, 18:200-214.
    • (2008) Eur. Neuropsychopharmacol. , vol.18 , pp. 200-214
    • Adage, T.1
  • 46
    • 45749091007 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of d-amino acid oxidase inhibitors
    • Ferraris D., et al. Synthesis and biological evaluation of d-amino acid oxidase inhibitors. J. Med. Chem. 2008, 51:3357-3359.
    • (2008) J. Med. Chem. , vol.51 , pp. 3357-3359
    • Ferraris, D.1
  • 47
    • 66749135202 scopus 로고    scopus 로고
    • Discovery, SAR, and pharmacokinetics of a novel 3-hydroxyquinolin-2(1H)-one series of potent d-amino acid oxidase (DAAO) inhibitors
    • Duplantier A.J., et al. Discovery, SAR, and pharmacokinetics of a novel 3-hydroxyquinolin-2(1H)-one series of potent d-amino acid oxidase (DAAO) inhibitors. J. Med. Chem. 2009, 52:3576-3585.
    • (2009) J. Med. Chem. , vol.52 , pp. 3576-3585
    • Duplantier, A.J.1
  • 48
    • 78249248949 scopus 로고    scopus 로고
    • The therapeutic potential of d-amino acid oxidase (DAAO) inhibitors
    • Smith S.M., et al. The therapeutic potential of d-amino acid oxidase (DAAO) inhibitors. Open Med. Chem. J. 2010, 4:3-9.
    • (2010) Open Med. Chem. J. , vol.4 , pp. 3-9
    • Smith, S.M.1
  • 49
    • 73649121936 scopus 로고    scopus 로고
    • Development of an implantable d-serine biosensor for in vivo monitoring using mammalian d-amino acid oxidase on a poly (o-phenylenediamine) and Nafion-modified platinum-iridium disk electrode
    • Zain Z.M., et al. Development of an implantable d-serine biosensor for in vivo monitoring using mammalian d-amino acid oxidase on a poly (o-phenylenediamine) and Nafion-modified platinum-iridium disk electrode. Biosens. Bioelectron. 2010, 25:1454-1459.
    • (2010) Biosens. Bioelectron. , vol.25 , pp. 1454-1459
    • Zain, Z.M.1
  • 50
    • 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., et al. Modulating d-amino acid oxidase substrate specificity: production of an enzyme for analytical determination of all d-amino acids by directed evolution. Protein Eng. Des. Sel. 2004, 17:517-525.
    • (2004) Protein Eng. Des. Sel. , vol.17 , pp. 517-525
    • Sacchi, S.1
  • 51
    • 61449142543 scopus 로고    scopus 로고
    • Interaction of d-amino acid oxidase with carbon nanotubes: implications in the design of biosensors
    • Mora M.F., et al. Interaction of d-amino acid oxidase with carbon nanotubes: implications in the design of biosensors. Anal Chem. 2009, 81:1016-1022.
    • (2009) Anal Chem. , vol.81 , pp. 1016-1022
    • Mora, M.F.1
  • 52
    • 1842477422 scopus 로고    scopus 로고
    • A conditional marker gene allowing both positive and negative selection in plants
    • Erikson O., et al. A conditional marker gene allowing both positive and negative selection in plants. Nat. Biotechnol. 2004, 22:455-458.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 455-458
    • Erikson, O.1
  • 53
    • 66749175825 scopus 로고    scopus 로고
    • Expression of Trigonopsis variabilis d-amino acid oxidase in transgenic rice for cephalosporin production
    • Lin S.Y., et al. Expression of Trigonopsis variabilis d-amino acid oxidase in transgenic rice for cephalosporin production. Botanical Stud. 2009, 50:181-192.
    • (2009) Botanical Stud. , vol.50 , pp. 181-192
    • Lin, S.Y.1
  • 54
    • 70350108861 scopus 로고    scopus 로고
    • Preliminary results to establish the DAAO system as an alternative selection strategy on apple
    • Hättasch C., et al. Preliminary results to establish the DAAO system as an alternative selection strategy on apple. Acta Horticulturae 2009, 814:267-272.
    • (2009) Acta Horticulturae , vol.814 , pp. 267-272
    • Hättasch, C.1
  • 55
    • 79952304262 scopus 로고    scopus 로고
    • D-Glufosinate as a male sterility agent for hybrid seed production
    • Hawkes T., et al. d-Glufosinate as a male sterility agent for hybrid seed production. Plant Biotechnol. J. 2010, 10.1111/j.1467-7652.2010.00549.x.
    • (2010) Plant Biotechnol. J.
    • Hawkes, T.1
  • 56
    • 41349085389 scopus 로고    scopus 로고
    • Glyphosate: a once-in-a-century herbicide
    • Duke S.O., Powles S.B. Glyphosate: a once-in-a-century herbicide. Pest Manag. Sci. 2008, 64:319-325.
    • (2008) Pest Manag. Sci. , vol.64 , pp. 319-325
    • Duke, S.O.1    Powles, S.B.2
  • 57
    • 58449099935 scopus 로고    scopus 로고
    • Evolution of glyphosate-resistant crop technology
    • Green J.M. Evolution of glyphosate-resistant crop technology. Weed Sci. 2009, 57:108-117.
    • (2009) Weed Sci. , vol.57 , pp. 108-117
    • Green, J.M.1
  • 58
    • 3142719169 scopus 로고    scopus 로고
    • Structure-function correlation in glycine oxidase from Bacillus subtilis
    • Mörtl M., et al. Structure-function correlation in glycine oxidase from Bacillus subtilis. J. Biol. Chem. 2004, 279:29718-29727.
    • (2004) J. Biol. Chem. , vol.279 , pp. 29718-29727
    • Mörtl, M.1
  • 59
    • 0036510613 scopus 로고    scopus 로고
    • Glycine oxidase from Bacillus subtilis. Characterization of a new flavoprotein
    • Job V., et al. Glycine oxidase from Bacillus subtilis. Characterization of a new flavoprotein. J. Biol. Chem. 2002, 277:6985-6993.
    • (2002) J. Biol. Chem. , vol.277 , pp. 6985-6993
    • Job, V.1
  • 60
    • 0037394044 scopus 로고    scopus 로고
    • Kinetic mechanisms of glycine oxidase from Bacillus subtilis
    • Molla G., et al. Kinetic mechanisms of glycine oxidase from Bacillus subtilis. Eur. J. Biochem. 2003, 270:1474-1482.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1474-1482
    • Molla, G.1
  • 61
    • 73649096562 scopus 로고    scopus 로고
    • Glyphosate resistance by engineering the flavoenzyme glycine oxidase
    • Pedotti M., et al. Glyphosate resistance by engineering the flavoenzyme glycine oxidase. J. Biol. Chem. 2009, 284:36415-36423.
    • (2009) J. Biol. Chem. , vol.284 , pp. 36415-36423
    • Pedotti, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.