메뉴 건너뛰기




Volumn 97, Issue 21, 2013, Pages 9323-9341

L-Amino acid oxidase as biocatalyst: A dream too far?

Author keywords

Amino acid oxidases; Biocatalyst; l amino acids; Protein engineering; Substrate preference

Indexed keywords

AMINO ACID OXIDASE; BIOCHEMICAL PROPERTIES; BIOTECHNOLOGICAL APPLICATIONS; FLAVIN ADENINE DINUCLEOTIDE; L-AMINO ACIDS; POST-TRANSLATIONAL MODIFICATIONS; PROTEIN ENGINEERING; SUBSTRATE SPECIFICITY;

EID: 84886883411     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-013-5230-1     Document Type: Article
Times cited : (111)

References (79)
  • 2
    • 33745812087 scopus 로고    scopus 로고
    • Mechanisms of cell death induction by L-amino acid oxidase, a major component of ophidian venom
    • 16770529 10.1007/s10495-006-7959-9 1:CAS:528:DC%2BD28Xms1OhsL4%3D
    • Ande SR, Kommoju PR, Draxl S, Murkovic M, Macheroux P, Ghisla S, Ferrando-May E (2006) Mechanisms of cell death induction by L-amino acid oxidase, a major component of ophidian venom. Apoptosis 11(8):1439-1451
    • (2006) Apoptosis , vol.11 , Issue.8 , pp. 1439-1451
    • Ande, S.R.1    Kommoju, P.R.2    Draxl, S.3    Murkovic, M.4    Macheroux, P.5    Ghisla, S.6    Ferrando-May, E.7
  • 3
    • 1342346743 scopus 로고    scopus 로고
    • Recombinant expression, biochemical characterization and stabilization through proteolysis of an l-glutamate oxidase from Streptomyces sp. X-119-6
    • 14769868 10.1093/jb/mvg206 1:CAS:528:DC%2BD2cXis1Kksrg%3D
    • Arima J, Tamura T, Kusakabe H, Ashiuchi M, Yagi T, Tanaka H, Inagaki K (2003) Recombinant expression, biochemical characterization and stabilization through proteolysis of an l-glutamate oxidase from Streptomyces sp. X-119-6. J Biochem 134(6):805-812
    • (2003) J Biochem , vol.134 , Issue.6 , pp. 805-812
    • Arima, J.1    Tamura, T.2    Kusakabe, H.3    Ashiuchi, M.4    Yagi, T.5    Tanaka, H.6    Inagaki, K.7
  • 4
    • 67650693780 scopus 로고    scopus 로고
    • Structural characterization of l-glutamate oxidase from Streptomyces sp. X-119-6
    • 19531050 10.1111/j.1742-4658.2009.07103.x 1:CAS:528:DC%2BD1MXovV2ltrs%3D
    • Arima J, Sasaki C, Sakaguchi C, Mizuno H, Tamura T, Kashima A, Kusakabe H, Sugio S, Inagaki K (2009) Structural characterization of l-glutamate oxidase from Streptomyces sp. X-119-6. FEBS J 276(14):3894-3903
    • (2009) FEBS J , vol.276 , Issue.14 , pp. 3894-3903
    • Arima, J.1    Sasaki, C.2    Sakaguchi, C.3    Mizuno, H.4    Tamura, T.5    Kashima, A.6    Kusakabe, H.7    Sugio, S.8    Inagaki, K.9
  • 5
    • 84881261506 scopus 로고    scopus 로고
    • A thermostable L-aspartate oxidase: A new tool for biotechnological applications
    • 23371294 10.1007/s00253-013-4688-1 1:CAS:528:DC%2BC3sXhtFyjtrnO
    • Bifulco D, Pollegioni L, Tessaro D, Servi S, Molla G (2013) A thermostable L-aspartate oxidase: a new tool for biotechnological applications. Appl Microbiol Biotechnol 97(16):7285-7295
    • (2013) Appl Microbiol Biotechnol , vol.97 , Issue.16 , pp. 7285-7295
    • Bifulco, D.1    Pollegioni, L.2    Tessaro, D.3    Servi, S.4    Molla, G.5
  • 6
    • 34548519907 scopus 로고    scopus 로고
    • A 30-angstrom-long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase
    • Binda C, Coda A, Angelini R, Federico R, Ascenzi P, Mattevi A (1999) A 30-angstrom-long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase. Structure. 7(3):265-276
    • (1999) Structure , vol.7 , Issue.3 , pp. 265-276
    • Binda, C.1    Coda, A.2    Angelini, R.3    Federico, R.4    Ascenzi, P.5    Mattevi, A.6
  • 7
    • 0024371013 scopus 로고
    • A novel l-glutamate oxidase from Streptomyces endus. Purification and properties
    • 2737205 10.1111/j.1432-1033.1989.tb14834.x
    • Böhmer A, Müller A, Passarge M, Liebs P, Honeck H, Müller HG (1989) A novel l-glutamate oxidase from Streptomyces endus. Purification and properties. Eur J Biochem 182(2):327-332
    • (1989) Eur J Biochem , vol.182 , Issue.2 , pp. 327-332
    • Böhmer, A.1    Müller, A.2    Passarge, M.3    Liebs, P.4    Honeck, H.5    Müller, H.G.6
  • 8
    • 0037022788 scopus 로고    scopus 로고
    • Structure of FAD-bound l-aspartate oxidase: Insight into substrate specificity and catalysis
    • 11863440 10.1021/bi015939r 1:CAS:528:DC%2BD38XhtVKis74%3D
    • Bossi RT, Negri A, Tedeschi G, Mattevi A (2002) Structure of FAD-bound l-aspartate oxidase: insight into substrate specificity and catalysis. Biochemistry 41(9):3018-3024
    • (2002) Biochemistry , vol.41 , Issue.9 , pp. 3018-3024
    • Bossi, R.T.1    Negri, A.2    Tedeschi, G.3    Mattevi, A.4
  • 9
    • 0028145168 scopus 로고
    • Purification and partial characterization of a broad range l-amino acid oxidase from Bacillus carotarum 2Pfa isolated from soil
    • 10.1007/BF00167283 1:CAS:528:DyaK2MXitleks7g%3D
    • Brearley GM, Price CP, Atkinson T, Hammond PM (1994) Purification and partial characterization of a broad range l-amino acid oxidase from Bacillus carotarum 2Pfa isolated from soil. Appl Microbiol Biotechnol 41:670-676
    • (1994) Appl Microbiol Biotechnol , vol.41 , pp. 670-676
    • Brearley, G.M.1    Price, C.P.2    Atkinson, T.3    Hammond, P.M.4
  • 10
    • 84877832924 scopus 로고    scopus 로고
    • Glutaraldehyde cross-linked glutamate oxidase coated microelectrode arrays: Selectivity and resting levels of glutamate in the CNS
    • 23650904 10.1021/cn4000555 1:CAS:528:DC%2BC3sXntFWntLw%3D
    • Burmeister JJ, Davis VA, Quintero JE, Pomerleau F, Huettl P, Gerhardt GA (2013) Glutaraldehyde cross-linked glutamate oxidase coated microelectrode arrays: selectivity and resting levels of glutamate in the CNS. ACS Chem Neurosci 4(5):721-728
    • (2013) ACS Chem Neurosci , vol.4 , Issue.5 , pp. 721-728
    • Burmeister, J.J.1    Davis, V.A.2    Quintero, J.E.3    Pomerleau, F.4    Huettl, P.5    Gerhardt, G.A.6
  • 11
    • 0035063043 scopus 로고    scopus 로고
    • A common precursor for the three subunits of L-glutamate oxidase encoded by gox gene from Streptomyces platensis NTU3304
    • 11315118 1:CAS:528:DC%2BD3MXisFWgtrc%3D
    • Chen CY, Wu WT, Huang CJ, Lin MH, Chang CK, Huang HJ, Liao JM, Chen LY, Liu YT (2001) A common precursor for the three subunits of L-glutamate oxidase encoded by gox gene from Streptomyces platensis NTU3304. Can J Microbiol 47(3):269-275
    • (2001) Can J Microbiol , vol.47 , Issue.3 , pp. 269-275
    • Chen, C.Y.1    Wu, W.T.2    Huang, C.J.3    Lin, M.H.4    Chang, C.K.5    Huang, H.J.6    Liao, J.M.7    Chen, L.Y.8    Liu, Y.T.9
  • 12
    • 77953617386 scopus 로고    scopus 로고
    • Involvement of an l-amino acid oxidase in the activity of the marine bacterium Pseudoalteromonas flavipulchra against methicillin-resistant Staphylococcus aureus
    • 10.1016/j.enzmictec.2010.03.008 1:CAS:528:DC%2BC3cXntVOrtbo%3D
    • Chen WM, Lin CY, Chen CA, Wang JT, Sheu SY (2010) Involvement of an l-amino acid oxidase in the activity of the marine bacterium Pseudoalteromonas flavipulchra against methicillin-resistant Staphylococcus aureus. Enzym Microb Technol 47:52-58
    • (2010) Enzym Microb Technol , vol.47 , pp. 52-58
    • Chen, W.M.1    Lin, C.Y.2    Chen, C.A.3    Wang, J.T.4    Sheu, S.Y.5
  • 14
    • 0036234815 scopus 로고    scopus 로고
    • Snake venom l-amino acid oxidases
    • 12175601 10.1016/S0041-0101(02)00102-2 1:CAS:528:DC%2BD38XivFOhsbs%3D
    • Du XY, Clemetson KJ (2002) Snake venom l-amino acid oxidases. Toxicon 40(6):659-665
    • (2002) Toxicon , vol.40 , Issue.6 , pp. 659-665
    • Du, X.Y.1    Clemetson, K.J.2
  • 15
    • 0034854206 scopus 로고    scopus 로고
    • Sequence-structure analysis of FAD-containing proteins
    • 11514662 10.1110/ps.12801 1:CAS:528:DC%2BD3MXmsFSgtb4%3D
    • Dym O, Eisenberg D (2001) Sequence-structure analysis of FAD-containing proteins. Protein Sci 10(9):1712-1728
    • (2001) Protein Sci , vol.10 , Issue.9 , pp. 1712-1728
    • Dym, O.1    Eisenberg, D.2
  • 16
    • 0035807435 scopus 로고    scopus 로고
    • Engineering, expression and purification of a His-tagged chimeric D-amino acid oxidase from Rhodotorula gracilis
    • 10.1016/S0141-0229(01)00400-8
    • Fantinato S, Pollegioni L, Pilone MS (2001) Engineering, expression and purification of a His-tagged chimeric D-amino acid oxidase from Rhodotorula gracilis. Enzyme Microb Technol 29:407-412
    • (2001) Enzyme Microb Technol , vol.29 , pp. 407-412
    • Fantinato, S.1    Pollegioni, L.2    Pilone, M.S.3
  • 17
    • 33847013408 scopus 로고    scopus 로고
    • The structure of a bacterial L-amino acid oxidase from Rhodococcus opacus gives new evidence for the hydride mechanism for dehydrogenation
    • 17234209 10.1016/j.jmb.2006.11.071 1:CAS:528:DC%2BD2sXitFCjsrs%3D
    • Faust A, Niefind K, Hummel W, Schomburg D (2007) The structure of a bacterial L-amino acid oxidase from Rhodococcus opacus gives new evidence for the hydride mechanism for dehydrogenation. J Mol Biol 367(1):234-248
    • (2007) J Mol Biol , vol.367 , Issue.1 , pp. 234-248
    • Faust, A.1    Niefind, K.2    Hummel, W.3    Schomburg, D.4
  • 18
    • 27444431578 scopus 로고    scopus 로고
    • Modelling of l-DOPA enzymatic oxidation catalyzed by l-amino acid oxidases from Crotalus adamanteus and Rhodococcus opacus
    • 10.1016/j.bej.2005.08.022 1:CAS:528:DC%2BD2MXhtFKmsrjI
    • Findrik Z, Geueke B, Hummel W, Vasić-Rački D (2006) Modelling of l-DOPA enzymatic oxidation catalyzed by l-amino acid oxidases from Crotalus adamanteus and Rhodococcus opacus. Biochem Eng J 27:275-286
    • (2006) Biochem Eng J , vol.27 , pp. 275-286
    • Findrik, Z.1    Geueke, B.2    Hummel, W.3    Vasić-Rački, D.4
  • 19
    • 0036644230 scopus 로고    scopus 로고
    • A new bacterial l-amino acid oxidase with a broad substrate specificity: Purification and characterization
    • 10.1016/S0141-0229(02)00072-8 1:CAS:528:DC%2BD38XksVansbo%3D
    • Geueke B, Hummel W (2002) A new bacterial l-amino acid oxidase with a broad substrate specificity: purification and characterization. Enzym Microb Technol 31:77-87
    • (2002) Enzym Microb Technol , vol.31 , pp. 77-87
    • Geueke, B.1    Hummel, W.2
  • 20
    • 0038395864 scopus 로고    scopus 로고
    • Heterologous expression of Rhodococcus opacus l-amino acid oxidase in Streptomyces lividans
    • 12699695 10.1016/S1046-5928(02)00701-5 1:CAS:528:DC%2BD3sXivV2lsL4%3D
    • Geueke B, Hummel W (2003) Heterologous expression of Rhodococcus opacus l-amino acid oxidase in Streptomyces lividans. Protein Expr Purif 28(2):303-309
    • (2003) Protein Expr Purif , vol.28 , Issue.2 , pp. 303-309
    • Geueke, B.1    Hummel, W.2
  • 21
    • 46149107274 scopus 로고    scopus 로고
    • The macromolecule with antimicrobial activity synthesized by Pseudoalteromonas luteoviolacea strains is an l-amino acid oxidase
    • 18504575 10.1007/s00253-008-1499-x
    • Gómez D, Espinosa E, Bertazzo M, Lucas-Elío P, Solano F, Sanchez-Amat A (2008) The macromolecule with antimicrobial activity synthesized by Pseudoalteromonas luteoviolacea strains is an l-amino acid oxidase. Appl Microbiol Biotechnol 79(6):925-930
    • (2008) Appl Microbiol Biotechnol , vol.79 , Issue.6 , pp. 925-930
    • Gómez, D.1    Espinosa, E.2    Bertazzo, M.3    Lucas-Elío, P.4    Solano, F.5    Sanchez-Amat, A.6
  • 22
    • 84861917868 scopus 로고    scopus 로고
    • Past decade study of snake venom l-amino acid oxidase
    • 22579637 10.1016/j.toxicon.2012.05.001 1:CAS:528:DC%2BC38XptVKrt7Y%3D
    • Guo C, Liu S, Yao Y, Zhang Q, Sun MZ (2012) Past decade study of snake venom l-amino acid oxidase. Toxicon 60(3):302-311
    • (2012) Toxicon , vol.60 , Issue.3 , pp. 302-311
    • Guo, C.1    Liu, S.2    Yao, Y.3    Zhang, Q.4    Sun, M.Z.5
  • 23
    • 0026616885 scopus 로고
    • Transformation of Nε-CBZ-l-lysine to CBZ-l-oxylysine using l-amino acid oxidase from Providencia alcalifaciens and l-2-hydroxy-isocaproate dehydrogenase from Lactobacillus confusus
    • 1368913 10.1007/BF00240733 1:CAS:528:DyaK38Xmtlaisrg%3D
    • Hanson RL, Bembenek KS, Patel RN, Szarka LJ (1992) Transformation of Nε-CBZ-l-lysine to CBZ-l-oxylysine using l-amino acid oxidase from Providencia alcalifaciens and l-2-hydroxy-isocaproate dehydrogenase from Lactobacillus confusus. Appl Microbiol Biotechnol 37(5):599-603
    • (1992) Appl Microbiol Biotechnol , vol.37 , Issue.5 , pp. 599-603
    • Hanson, R.L.1    Bembenek, K.S.2    Patel, R.N.3    Szarka, L.J.4
  • 24
    • 47749098551 scopus 로고    scopus 로고
    • Structural basis of proteolytic activation of l-phenylalanine oxidase from Pseudomonas sp. P-501
    • 18417467 10.1074/jbc.M800366200 1:CAS:528:DC%2BD1cXmslOju74%3D
    • Ida K, Kurabayashi M, Suguro M, Hiruma Y, Hikima T, Yamomoto M, Suzuki H (2008) Structural basis of proteolytic activation of l-phenylalanine oxidase from Pseudomonas sp. P-501. J Biol Chem 283(24):16584-16590
    • (2008) J Biol Chem , vol.283 , Issue.24 , pp. 16584-16590
    • Ida, K.1    Kurabayashi, M.2    Suguro, M.3    Hiruma, Y.4    Hikima, T.5    Yamomoto, M.6    Suzuki, H.7
  • 25
    • 82955224974 scopus 로고    scopus 로고
    • High resolution X-ray crystal structures of L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501. Structures of the enzyme-ligand complex and catalytic mechanism
    • 21841183 10.1093/jb/mvr103 1:CAS:528:DC%2BC3MXhsFygtLbK
    • Ida K, Suguro M, Suzuki H (2011) High resolution X-ray crystal structures of L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501. Structures of the enzyme-ligand complex and catalytic mechanism. J Biochem 150(6):659-669
    • (2011) J Biochem , vol.150 , Issue.6 , pp. 659-669
    • Ida, K.1    Suguro, M.2    Suzuki, H.3
  • 26
    • 35348991525 scopus 로고    scopus 로고
    • α-benzyloxycarbonyl-l-lysine oxidizing enzyme from Rhodococcus sp. AIU Z-35-1
    • 17964487 10.1263/jbb.104.218 1:CAS:528:DC%2BD2sXhtlGmsr3N
    • α- benzyloxycarbonyl-l-lysine oxidizing enzyme from Rhodococcus sp. AIU Z-35-1. J Biosci Bioeng 104(3):218-223
    • (2007) J Biosci Bioeng , vol.104 , Issue.3 , pp. 218-223
    • Isobe, K.1    Nagasawa, S.2
  • 27
    • 77953893068 scopus 로고    scopus 로고
    • α-[(benzyloxy)carbonyl]-d- aminoadipic acid by Rhodococcus sp. AIU Z-35-1
    • 20564569 10.1002/cbdv.200900251 1:CAS:528:DC%2BC3cXot1ant70%3D
    • α-[(benzyloxy)carbonyl]-d-aminoadipic acid by Rhodococcus sp. AIU Z-35-1. Chem Biodivers 7(6):1549-1554
    • (2010) Chem Biodivers , vol.7 , Issue.6 , pp. 1549-1554
    • Isobe, K.1    Fukuda, N.2    Nagasawa, S.3    Saitou, K.4
  • 28
    • 84876956556 scopus 로고    scopus 로고
    • Characterization and application of a l-specific amino acid oxidase from Rhodococcus sp. AIU LAB-3
    • 10.1016/j.jbiosc.2012.12.003
    • Isobe K, Satou S, Matsumoto E, Yoshida S, Yamada M, Hibi M, Ogawa J (2012a) Characterization and application of a l-specific amino acid oxidase from Rhodococcus sp. AIU LAB-3. J Biosci Bioeng 115(6):613-617
    • (2012) J Biosci Bioeng , vol.115 , Issue.6 , pp. 613-617
    • Isobe, K.1    Satou, S.2    Matsumoto, E.3    Yoshida, S.4    Yamada, M.5    Hibi, M.6    Ogawa, J.7
  • 29
    • 84864608862 scopus 로고    scopus 로고
    • Purification and characterization of an l-amino acid oxidase from Pseudomonas sp. AIU 813
    • 22704811 10.1016/j.jbiosc.2012.04.020 1:CAS:528:DC%2BC38XhvVOiurjE
    • Isobe K, Sugawara A, Domon H, Fukuta Y, Asano Y (2012b) Purification and characterization of an l-amino acid oxidase from Pseudomonas sp. AIU 813. J Biosci Bioeng 114(3):257-261
    • (2012) J Biosci Bioeng , vol.114 , Issue.3 , pp. 257-261
    • Isobe, K.1    Sugawara, A.2    Domon, H.3    Fukuta, Y.4    Asano, Y.5
  • 30
    • 0020571866 scopus 로고
    • L-glutamate oxidase from Streptomyces violascens. I. Production, isolation and some properties
    • 10.1248/cpb.31.1307 1:CAS:528:DyaL3sXksV2gurg%3D
    • Kamei T, Asano K, Suzuki H, Matsuzaki M, Nakamura S (1983) L-glutamate oxidase from Streptomyces violascens. I. Production, isolation and some properties. Chem Pharm Bull 31(4):1307-1314
    • (1983) Chem Pharm Bull , vol.31 , Issue.4 , pp. 1307-1314
    • Kamei, T.1    Asano, K.2    Suzuki, H.3    Matsuzaki, M.4    Nakamura, S.5
  • 31
    • 0032438290 scopus 로고    scopus 로고
    • A new interference-free lysine biosensor using a non-conducting polymer film
    • 9883557 10.1016/S0956-5663(98)00075-X 1:STN:280:DyaK1M7gtVSisg%3D%3D
    • Kelly S, Curulli A, O'Sullivan C, Guilbault GG, Palleschi G (1998) A new interference-free lysine biosensor using a non-conducting polymer film. Biosens Bioelectron 13(12):1245-1250
    • (1998) Biosens Bioelectron , vol.13 , Issue.12 , pp. 1245-1250
    • Kelly, S.1    Curulli, A.2    O'Sullivan, C.3    Guilbault, G.G.4    Palleschi, G.5
  • 32
    • 0021478112 scopus 로고
    • Oxidation and oxygenation of l-amino acids catalyzed by a l-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501
    • 6501250 1:CAS:528:DyaL2cXlsVKltLg%3D
    • Koyama H (1984) Oxidation and oxygenation of l-amino acids catalyzed by a l-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501. J Biochem 96(2):421-427
    • (1984) J Biochem , vol.96 , Issue.2 , pp. 421-427
    • Koyama, H.1
  • 33
    • 0018585095 scopus 로고
    • Occurrence of a novel enzyme, l-lysine oxidase with anti-tumor activity in culture of Trichoderma viridae
    • 10.1271/bbb1961.43.337 1:CAS:528:DyaE1MXhvFOltrc%3D
    • Kusakabe H, Kodama K, Machida H, Midorikawa Y, Kuninaka A, Misono H, Soda K (1979) Occurrence of a novel enzyme, l-lysine oxidase with anti-tumor activity in culture of Trichoderma viridae. Agric Biol Chem 43:337-343
    • (1979) Agric Biol Chem , vol.43 , pp. 337-343
    • Kusakabe, H.1    Kodama, K.2    Machida, H.3    Midorikawa, Y.4    Kuninaka, A.5    Misono, H.6    Soda, K.7
  • 34
    • 0019151796 scopus 로고
    • A new antitumor enzyme, l-lysine alpha-oxidase from Trichoderma viride. Purification and enzymological properties
    • 6101334 1:CAS:528:DyaL3cXht1eqsLs%3D
    • Kusakabe H, Kodama K, Kuninaka A, Yoshino H, Misono H, Soda K (1980) A new antitumor enzyme, l-lysine alpha-oxidase from Trichoderma viride. Purification and enzymological properties. J Biol Chem 255(3):976-981
    • (1980) J Biol Chem , vol.255 , Issue.3 , pp. 976-981
    • Kusakabe, H.1    Kodama, K.2    Kuninaka, A.3    Yoshino, H.4    Misono, H.5    Soda, K.6
  • 35
    • 84872410953 scopus 로고    scopus 로고
    • L-amino acid biosensor based on L-amino acid oxidase immobilized onto NiHCNFe/c-MWCNT/PPy/GC electrode
    • 23237796 10.1016/j.ijbiomac.2012.12.004 1:CAS:528:DC%2BC3sXhslChtr0%3D
    • Lata S, Pundir CS (2013) L-amino acid biosensor based on L-amino acid oxidase immobilized onto NiHCNFe/c-MWCNT/PPy/GC electrode. Int J Biol Macromol 54:250-257
    • (2013) Int J Biol Macromol , vol.54 , pp. 250-257
    • Lata, S.1    Pundir, C.S.2
  • 36
    • 84865650221 scopus 로고    scopus 로고
    • Cloning, expression, characterisation and mutational analysis of l-aspartate oxidase from Pseudomonas putida
    • Leese C, Fotheringham I, Escalettes F, Speight R, Grogan G (2013) Cloning, expression, characterisation and mutational analysis of l-aspartate oxidase from Pseudomonas putida. J Mol Catal B: Enzymatic 85-86:7-22
    • (2013) J Mol Catal B: Enzymatic , vol.85-86 , pp. 7-22
    • Leese, C.1    Fotheringham, I.2    Escalettes, F.3    Speight, R.4    Grogan, G.5
  • 37
    • 0036817580 scopus 로고    scopus 로고
    • L-Lysine alpha-oxidase: Physicochemical and biological properties
    • 10.1023/A:1020967408229 1:CAS:528:DC%2BD38XosVClsbY%3D
    • Lukasheva EV, Berezov TT (2002) l-Lysine alpha-oxidase: physicochemical and biological properties. Biochemistry (Mosc) 67(10):1152-1158
    • (2002) Biochemistry (Mosc) , vol.67 , Issue.10 , pp. 1152-1158
    • Lukasheva, E.V.1    Berezov, T.T.2
  • 40
    • 0029839452 scopus 로고    scopus 로고
    • Crystal structure of d-amino acid oxidase: A case of active site mirror-image convergent evolution with flavocytochrome b2
    • 8755502 10.1073/pnas.93.15.7496 1:CAS:528:DyaK28XksFSku7k%3D
    • Mattevi A, Vanoni MA, Todone F, Rizzi M, Teplyakov A, Coda A, Bolognesi M, Curti B (1996) Crystal structure of d-amino acid oxidase: a case of active site mirror-image convergent evolution with flavocytochrome b2. Proc Natl Acad Sci U S A 93(15):7496-7501
    • (1996) Proc Natl Acad Sci U S A , vol.93 , Issue.15 , pp. 7496-7501
    • Mattevi, A.1    Vanoni, M.A.2    Todone, F.3    Rizzi, M.4    Teplyakov, A.5    Coda, A.6    Bolognesi, M.7    Curti, B.8
  • 41
    • 0001406338 scopus 로고    scopus 로고
    • Structure of l-aspartate oxidase: Implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family
    • 10425677 10.1016/S0969-2126(99)80099-9 1:CAS:528:DyaK1MXkslGgsrc%3D
    • Mattevi A, Tedeschi G, Bacchella L, Coda A, Negri A, Ronchi S (1999) Structure of l-aspartate oxidase: implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family. Structure 7(7):745-756
    • (1999) Structure , vol.7 , Issue.7 , pp. 745-756
    • Mattevi, A.1    Tedeschi, G.2    Bacchella, L.3    Coda, A.4    Negri, A.5    Ronchi, S.6
  • 42
    • 0034628488 scopus 로고    scopus 로고
    • A new model for protein stereospecificity
    • 10688187 1:CAS:528:DC%2BD3cXht1Oru7Y%3D
    • Mesecar AD, Koshland DE Jr (2000) A new model for protein stereospecificity. Nature 403(6770):614-615
    • (2000) Nature , vol.403 , Issue.6770 , pp. 614-615
    • Mesecar, A.D.1    Koshland, Jr.D.E.2
  • 43
    • 0030018052 scopus 로고    scopus 로고
    • L-Aspartate oxidase from Escherichia coli. I. Characterization of coenzyme binding and product inhibition
    • 8706749 10.1111/j.1432-1033.1996.0418u.x 1:CAS:528:DyaK28Xks1ertro%3D
    • Mortarino M, Negri A, Tedeschi G, Simonic T, Duga S, Gassen HG, Ronchi S (1996) l-Aspartate oxidase from Escherichia coli. I. Characterization of coenzyme binding and product inhibition. Eur J Biochem 239(2):418-426
    • (1996) Eur J Biochem , vol.239 , Issue.2 , pp. 418-426
    • Mortarino, M.1    Negri, A.2    Tedeschi, G.3    Simonic, T.4    Duga, S.5    Gassen, H.G.6    Ronchi, S.7
  • 44
    • 33751117995 scopus 로고    scopus 로고
    • Crystal structure of LAAO from Calloselasma rhodostoma with an l-phenylalanine substrate: Insights into structure and mechanism
    • 17046020 10.1016/j.jmb.2006.09.032 1:CAS:528:DC%2BD28Xht1equr7M
    • Moustafa IM, Foster S, Lyubimov AY, Vrielink A (2006) Crystal structure of LAAO from Calloselasma rhodostoma with an l-phenylalanine substrate: insights into structure and mechanism. J Mol Biol 364(5):991-1002
    • (2006) J Mol Biol , vol.364 , Issue.5 , pp. 991-1002
    • Moustafa, I.M.1    Foster, S.2    Lyubimov, A.Y.3    Vrielink, A.4
  • 46
    • 78650297006 scopus 로고    scopus 로고
    • Visible wavelength spectrophotometric assays of l-aspartate and d-aspartate using hyperthermophilic enzyme systems
    • 20951671 10.1016/j.ab.2010.10.016 1:CAS:528:DC%2BC3cXhsFGhs7bK
    • Mutaguchi Y, Ohmori T, Sakuraba H, Yoneda K, Doi K, Ohshima T (2011) Visible wavelength spectrophotometric assays of l-aspartate and d-aspartate using hyperthermophilic enzyme systems. Anal Biochem 409(1):1-6
    • (2011) Anal Biochem , vol.409 , Issue.1 , pp. 1-6
    • Mutaguchi, Y.1    Ohmori, T.2    Sakuraba, H.3    Yoneda, K.4    Doi, K.5    Ohshima, T.6
  • 47
    • 14644432391 scopus 로고    scopus 로고
    • Molecular analysis of the rebeccamycin L-amino acid oxidase from Lechevalieria aerocolonigenes ATCC 39243
    • 15743957 10.1128/JB.187.6.2084-2092.2005 1:CAS:528:DC%2BD2MXisVOgu70%3D
    • Nishizawa T, Aldrich CC, Sherman DH (2005) Molecular analysis of the rebeccamycin L-amino acid oxidase from Lechevalieria aerocolonigenes ATCC 39243. J Bacteriol 187(6):2084-2092
    • (2005) J Bacteriol , vol.187 , Issue.6 , pp. 2084-2092
    • Nishizawa, T.1    Aldrich, C.C.2    Sherman, D.H.3
  • 48
    • 84855218271 scopus 로고    scopus 로고
    • L-Amino acid oxidase of the fungus Hebeloma cylindrosporum displays substrate preference towards glutamate
    • 21998160 10.1099/mic.0.054486-0 1:CAS:528:DC%2BC38XitVKms7c%3D
    • Nuutinen JT, Marttinen E, Soliymani R, Hildén K, Timonen S (2012) L-Amino acid oxidase of the fungus Hebeloma cylindrosporum displays substrate preference towards glutamate. Microbiology 158:272-283
    • (2012) Microbiology , vol.158 , pp. 272-283
    • Nuutinen, J.T.1    Marttinen, E.2    Soliymani, R.3    Hildén, K.4    Timonen, S.5
  • 49
    • 0035931396 scopus 로고    scopus 로고
    • Purification and characterization of an l-amino acid deaminase used to prepare unnatural amino acids
    • 10.1016/S1381-1177(00)00155-7 1:CAS:528:DC%2BD3MXptlWhug%3D%3D
    • Pantaleone DP, Geller AM, Taylor PP (2001) Purification and characterization of an l-amino acid deaminase used to prepare unnatural amino acids. J Mol Catal B 11:795-803
    • (2001) J Mol Catal B , vol.11 , pp. 795-803
    • Pantaleone, D.P.1    Geller, A.M.2    Taylor, P.P.3
  • 50
    • 0034663814 scopus 로고    scopus 로고
    • The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site
    • 10944103 10.1093/emboj/19.16.4204 1:CAS:528:DC%2BD3cXnt1yrsbw%3D
    • Pawelek PD, Cheah J, Coulombe R, Macheroux P, Ghisla S, Vrielink A (2000) The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site. EMBO J 19(16):4204-4215
    • (2000) EMBO J , vol.19 , Issue.16 , pp. 4204-4215
    • Pawelek, P.D.1    Cheah, J.2    Coulombe, R.3    Macheroux, P.4    Ghisla, S.5    Vrielink, A.6
  • 51
    • 79956146208 scopus 로고    scopus 로고
    • New biotech applications from evolved D-amino acid oxidases
    • 21397351 10.1016/j.tibtech.2011.01.010 1:CAS:528:DC%2BC3MXmsVCjurc%3D
    • Pollegioni L, Molla G (2011) New biotech applications from evolved D-amino acid oxidases. Trends Biotechnol 29(6):276-283
    • (2011) Trends Biotechnol , vol.29 , Issue.6 , pp. 276-283
    • Pollegioni, L.1    Molla, G.2
  • 52
    • 18744385215 scopus 로고    scopus 로고
    • Yeast D-amino acid oxidase: Structural basis of its catalytic properties
    • 12445787 10.1016/S0022-2836(02)01062-8 1:CAS:528:DC%2BD38XovVyhsrc%3D
    • Pollegioni L, Diederichs K, Molla G, Umhau S, Welte W, Ghisla S, Pilone MS (2002) Yeast D-amino acid oxidase: structural basis of its catalytic properties. J Mol Biol 324(3):535-546
    • (2002) J Mol Biol , vol.324 , Issue.3 , pp. 535-546
    • Pollegioni, L.1    Diederichs, K.2    Molla, G.3    Umhau, S.4    Welte, W.5    Ghisla, S.6    Pilone, M.S.7
  • 53
    • 34250002745 scopus 로고    scopus 로고
    • Physiological functions of d-amino acid oxidases: From yeast to humans
    • 17396222 10.1007/s00018-007-6558-4 1:CAS:528:DC%2BD2sXntVOgsrk%3D
    • Pollegioni L, Piubelli L, Sacchi S, Pilone MS, Molla G (2007) Physiological functions of d-amino acid oxidases: from yeast to humans. Cell Mol Life Sci 64(11):1373-1394
    • (2007) Cell Mol Life Sci , vol.64 , Issue.11 , pp. 1373-1394
    • Pollegioni, L.1    Piubelli, L.2    Sacchi, S.3    Pilone, M.S.4    Molla, G.5
  • 54
    • 38349152169 scopus 로고    scopus 로고
    • Properties and applications of microbial d-amino acid oxidases: Current state and perspectives
    • 18084756 10.1007/s00253-007-1282-4 1:CAS:528:DC%2BD1cXot1KmtA%3D%3D
    • Pollegioni L, Molla G, Sacchi S, Rosini E, Verga R, Pilone MS (2008) Properties and applications of microbial d-amino acid oxidases: current state and perspectives. Appl Microbiol Biotechnol 78(1):1-16
    • (2008) Appl Microbiol Biotechnol , vol.78 , Issue.1 , pp. 1-16
    • Pollegioni, L.1    Molla, G.2    Sacchi, S.3    Rosini, E.4    Verga, R.5    Pilone, M.S.6
  • 55
    • 0027989688 scopus 로고
    • Purification and properties of the L-amino acid oxidase from Malayan pit viper (Calloselasma rhodostoma) venom
    • 8080286 10.1006/abbi.1994.1401 1:CAS:528:DyaK2cXmsV2is7Y%3D
    • Ponnudurai G, Chung MC, Tan NH (1994) Purification and properties of the L-amino acid oxidase from Malayan pit viper (Calloselasma rhodostoma) venom. Arch Biochem Biophys 313(2):373-378
    • (1994) Arch Biochem Biophys , vol.313 , Issue.2 , pp. 373-378
    • Ponnudurai, G.1    Chung, M.C.2    Tan, N.H.3
  • 57
    • 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
    • 15310841 10.1093/protein/gzh064 1:CAS:528:DC%2BD2cXos1Gisb8%3D
    • Sacchi S, Rosini E, Molla G, Pilone MS, Pollegioni L (2004) 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 17(6):517-525
    • (2004) Protein Eng des Sel , vol.17 , Issue.6 , pp. 517-525
    • Sacchi, S.1    Rosini, E.2    Molla, G.3    Pilone, M.S.4    Pollegioni, L.5
  • 58
    • 0036688941 scopus 로고    scopus 로고
    • L-Aspartate oxidase is present in the anaerobic hyperthermophilic archaeon Pyrococcus horikoshii OT-3: Characteristics and role in the de novo biosynthesis of nicotinamide adenine dinucleotide proposed by genome sequencing
    • 12215812 10.1007/s00792-001-0254-3 1:CAS:528:DC%2BD38XnsVSnsLg%3D
    • Sakuraba H, Satomura T, Kawakami R, Yamamoto S, Kawarabayasi Y, Kikuchi H, Ohshima T (2002) l-Aspartate oxidase is present in the anaerobic hyperthermophilic archaeon Pyrococcus horikoshii OT-3: characteristics and role in the de novo biosynthesis of nicotinamide adenine dinucleotide proposed by genome sequencing. Extremophiles 6(4):275-281
    • (2002) Extremophiles , vol.6 , Issue.4 , pp. 275-281
    • Sakuraba, H.1    Satomura, T.2    Kawakami, R.3    Yamamoto, S.4    Kawarabayasi, Y.5    Kikuchi, H.6    Ohshima, T.7
  • 59
    • 43049099608 scopus 로고    scopus 로고
    • Structure of l-aspartate oxidase from the hyperthermophilic archaeon Sulfolobus tokodaii
    • 18226609 10.1016/j.bbapap.2007.12.012 1:CAS:528:DC%2BD1cXitlensLw%3D
    • Sakuraba H, Yoneda K, Asai I, Tsuge H, Katunuma N, Ohshima T (2008) Structure of l-aspartate oxidase from the hyperthermophilic archaeon Sulfolobus tokodaii. Biochim Biophys Acta 1784(3):563-571
    • (2008) Biochim Biophys Acta , vol.1784 , Issue.3 , pp. 563-571
    • Sakuraba, H.1    Yoneda, K.2    Asai, I.3    Tsuge, H.4    Katunuma, N.5    Ohshima, T.6
  • 60
    • 0344609654 scopus 로고    scopus 로고
    • Amperometric determination of lysine using a lysine oxidase biosensor based on rigid-conducting composites
    • 10101842 10.1016/S0956-5663(98)00119-5 1:CAS:528:DyaK1MXhsVejtr4%3D
    • Saurina J, Hernández-Cassou S, Alegret S, Fàbregas E (1999) Amperometric determination of lysine using a lysine oxidase biosensor based on rigid-conducting composites. Biosens Bioelectron 14(2):211-220
    • (1999) Biosens Bioelectron , vol.14 , Issue.2 , pp. 211-220
    • Saurina, J.1    Hernández-Cassou, S.2    Alegret, S.3    Fàbregas, E.4
  • 61
    • 0025364212 scopus 로고
    • Expression of the E. coli nadB gene and characterization of the gene product L-aspartate oxidase
    • 2187483 10.1515/bchm3.1990.371.1.239 1:CAS:528:DyaK3cXkslWqurc%3D
    • Seifert J, Kunz N, Flachmann R, Läufer A, Jany KD, Gassen HG (1990) Expression of the E. coli nadB gene and characterization of the gene product L-aspartate oxidase. Biol Chem Hoppe Seyler 371(3):239-248
    • (1990) Biol Chem Hoppe Seyler , vol.371 , Issue.3 , pp. 239-248
    • Seifert, J.1    Kunz, N.2    Flachmann, R.3    Läufer, A.4    Jany, K.D.5    Gassen, H.G.6
  • 62
    • 70349765719 scopus 로고    scopus 로고
    • Optimization of medium and cultivation conditions for L-amino acid oxidase production by Aspergillus fumigatus
    • 19898552 10.1139/W09-068 1:CAS:528:DC%2BD1MXht1ant7nE
    • Singh S, Gogoi BK, Bezbaruah RL (2009) Optimization of medium and cultivation conditions for L-amino acid oxidase production by Aspergillus fumigatus. Can J Microbiol 55(9):1096-1102
    • (2009) Can J Microbiol , vol.55 , Issue.9 , pp. 1096-1102
    • Singh, S.1    Gogoi, B.K.2    Bezbaruah, R.L.3
  • 63
    • 79959755723 scopus 로고    scopus 로고
    • Racemic resolution of some dl-amino acids using Aspergillus fumigatus l-amino acid oxidase
    • 10.1007/s00284-011-9955-8 21590326 10.1007/s00284-011-9955-8 1:CAS:528:DC%2BC3MXmslahurg%3D
    • Singh S, Gogoi BK, Bezbaruah RL (2011) Racemic resolution of some dl-amino acids using Aspergillus fumigatus l-amino acid oxidase. Curr Microbiol 63(1):94-99. doi: 10.1007/s00284-011-9955-8
    • (2011) Curr Microbiol , vol.63 , Issue.1 , pp. 94-99
    • Singh, S.1    Gogoi, B.K.2    Bezbaruah, R.L.3
  • 64
    • 3142773545 scopus 로고    scopus 로고
    • Properties and prospects of practical use of extracellular l-glutamate oxidase from Streptomyces sp. Z-11-6
    • 10.1023/B:ABIM.0000018917.04795.d9 1:CAS:528:DC%2BD2cXhvFCnsLk%3D
    • Sukhacheva MV, Zhuravleva NI (2004) Properties and prospects of practical use of extracellular l-glutamate oxidase from Streptomyces sp. Z-11-6. Appl Biochem Microbiol 40(2):146-150
    • (2004) Appl Biochem Microbiol , vol.40 , Issue.2 , pp. 146-150
    • Sukhacheva, M.V.1    Zhuravleva, N.I.2
  • 65
    • 14944361293 scopus 로고    scopus 로고
    • Sequencing and expression of the L-phenylalanine oxidase gene from Pseudomonas sp. P-501. Proteolytic activation of the proenzyme
    • 15632301 10.1093/jb/mvh169 1:CAS:528:DC%2BD2MXislehtbo%3D
    • Suzuki H, Higashi Y, Asano M, Suguro M, Kigawa M, Maeda M, Katayama S, Mukouyama EB, Uchiyama K (2004) Sequencing and expression of the L-phenylalanine oxidase gene from Pseudomonas sp. P-501. Proteolytic activation of the proenzyme. J Biochem 136(5):617-627
    • (2004) J Biochem , vol.136 , Issue.5 , pp. 617-627
    • Suzuki, H.1    Higashi, Y.2    Asano, M.3    Suguro, M.4    Kigawa, M.5    Maeda, M.6    Katayama, S.7    Mukouyama, E.B.8    Uchiyama, K.9
  • 66
    • 0030037614 scopus 로고    scopus 로고
    • L-aspartate oxidase from Escherichia coli. II. Interaction with C4 dicarboxylic acids and identification of a novel L-aspartate:fumarate oxidoreductase activity
    • 8706750 10.1111/j.1432-1033.1996.0427u.x 1:CAS:528:DyaK28Xks1ertrs%3D
    • Tedeschi G, Negri A, Mortarino M, Ceciliani F, Simonic T, Faotto L, Ronchi S (1996) L-aspartate oxidase from Escherichia coli. II. Interaction with C4 dicarboxylic acids and identification of a novel L-aspartate:fumarate oxidoreductase activity. Eur J Biochem 239(2):427-433
    • (1996) Eur J Biochem , vol.239 , Issue.2 , pp. 427-433
    • Tedeschi, G.1    Negri, A.2    Mortarino, M.3    Ceciliani, F.4    Simonic, T.5    Faotto, L.6    Ronchi, S.7
  • 67
    • 0035901492 scopus 로고    scopus 로고
    • Probing the active site of l-aspartate oxidase by site-directed mutagenesis: Role of basic residues in fumarate reduction
    • 11294641 10.1021/bi002406u 1:CAS:528:DC%2BD3MXitVyrsr0%3D
    • Tedeschi G, Ronchi S, Simonic T, Treu C, Mattevi A, Negri A (2001) Probing the active site of l-aspartate oxidase by site-directed mutagenesis: role of basic residues in fumarate reduction. Biochemistry 40(15):4738-4744
    • (2001) Biochemistry , vol.40 , Issue.15 , pp. 4738-4744
    • Tedeschi, G.1    Ronchi, S.2    Simonic, T.3    Treu, C.4    Mattevi, A.5    Negri, A.6
  • 68
    • 77957163782 scopus 로고    scopus 로고
    • On the catalytic role of the active site residue E121 of E. coli l-aspartate oxidase
    • 10.1016/j.biochi.2010.06.015 20600565 10.1016/j.biochi.2010.06.015 1:CAS:528:DC%2BC3cXht1Clsr3F
    • Tedeschi G, Nonnis S, Strumbo B, Cruciani G, Carosati E, Negri A (2010) On the catalytic role of the active site residue E121 of E. coli l-aspartate oxidase. Biochimie 92(10):1335-1342. doi: 10.1016/j.biochi.2010.06.015
    • (2010) Biochimie , vol.92 , Issue.10 , pp. 1335-1342
    • Tedeschi, G.1    Nonnis, S.2    Strumbo, B.3    Cruciani, G.4    Carosati, E.5    Negri, A.6
  • 69
    • 65749098398 scopus 로고    scopus 로고
    • A microelectrode biosensor for real time monitoring of l-glutamate release
    • 19481635 10.1016/j.aca.2009.04.048 1:CAS:528:DC%2BD1MXms1eqs74%3D
    • Tian F, Gourine AV, Huckstepp RT, Dale N (2009) A microelectrode biosensor for real time monitoring of l-glutamate release. Anal Chim Acta 645(1-2):86-91
    • (2009) Anal Chim Acta , vol.645 , Issue.1-2 , pp. 86-91
    • Tian, F.1    Gourine, A.V.2    Huckstepp, R.T.3    Dale, N.4
  • 70
    • 84860325647 scopus 로고    scopus 로고
    • Structural insights into selectivity and cofactor binding in snake venom l-amino acid oxidases
    • 22490662 10.1016/j.bbrc.2012.03.129 1:CAS:528:DC%2BC38XlvVSnt7Y%3D
    • Ullah A, Souza TA, Abrego JR, Betzel C, Murakami MT, Arni RK (2012) Structural insights into selectivity and cofactor binding in snake venom l-amino acid oxidases. Biochem Biophys Res Commun 421(1):124-128
    • (2012) Biochem Biophys Res Commun , vol.421 , Issue.1 , pp. 124-128
    • Ullah, A.1    Souza, T.A.2    Abrego, J.R.3    Betzel, C.4    Murakami, M.T.5    Arni, R.K.6
  • 71
    • 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
    • 11070076 10.1073/pnas.97.23.12463 1:CAS:528:DC%2BD3cXotFyhsr4%3D
    • Umhau S, Pollegioni L, Molla G, Diederichs K, Welte W, Pilone MS, Ghisla S (2000) 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 97(23):12463-12468
    • (2000) Proc Natl Acad Sci U S A , vol.97 , Issue.23 , pp. 12463-12468
    • Umhau, S.1    Pollegioni, L.2    Molla, G.3    Diederichs, K.4    Welte, W.5    Pilone, M.S.6    Ghisla, S.7
  • 72
    • 33748753325 scopus 로고    scopus 로고
    • Performance characterization of recombinant l-glutamate oxidase in a micro GOT/GPT sensing system
    • 10.1016/j.snb.2006.01.008 1:CAS:528:DC%2BD28XpvFejt7s%3D
    • Upadhyay S, Ohgami N, Kusakabe H, Mizuno H, Arima J, Tamura T, Inagaki K, Suzuki H (2006) Performance characterization of recombinant l-glutamate oxidase in a micro GOT/GPT sensing system. Sens Actuators B 119:570-576
    • (2006) Sens Actuators B , vol.119 , pp. 570-576
    • Upadhyay, S.1    Ohgami, N.2    Kusakabe, H.3    Mizuno, H.4    Arima, J.5    Tamura, T.6    Inagaki, K.7    Suzuki, H.8
  • 73
    • 84856012530 scopus 로고    scopus 로고
    • Arg305 of Streptomyces l-glutamate oxidase plays a crucial role for substrate recognition
    • 22197816 10.1016/j.bbrc.2011.12.033 1:CAS:528:DC%2BC38XhtFKrsrg%3D
    • Utsumi T, Arima J, Sakaguchi C, Tamura T, Sasaki C, Kusakabe H, Sugio S, Inagaki K (2012) Arg305 of Streptomyces l-glutamate oxidase plays a crucial role for substrate recognition. Biochem Biophys Res Commun 417(3):951-955
    • (2012) Biochem Biophys Res Commun , vol.417 , Issue.3 , pp. 951-955
    • Utsumi, T.1    Arima, J.2    Sakaguchi, C.3    Tamura, T.4    Sasaki, C.5    Kusakabe, H.6    Sugio, S.7    Inagaki, K.8
  • 74
    • 79956341467 scopus 로고    scopus 로고
    • Covalent enzyme immobilization by poly(ethylene glycol) diglycidyl ether (PEGDE) for microelectrode biosensor preparation
    • 21546239 10.1016/j.bios.2011.03.012 1:CAS:528:DC%2BC3MXmvFWjsbg%3D
    • Vasylieva N, Barnych B, Meiller A, Maucler C, Pollegioni L, Lin JS, Barbier D, Marinesco S (2011) Covalent enzyme immobilization by poly(ethylene glycol) diglycidyl ether (PEGDE) for microelectrode biosensor preparation. Biosens Bioelectron 26(10):3993-4000
    • (2011) Biosens Bioelectron , vol.26 , Issue.10 , pp. 3993-4000
    • Vasylieva, N.1    Barnych, B.2    Meiller, A.3    Maucler, C.4    Pollegioni, L.5    Lin, J.S.6    Barbier, D.7    Marinesco, S.8
  • 75
    • 80052504283 scopus 로고    scopus 로고
    • Identification of antibacterial mechanism of l-amino acid oxidase derived from Trichoderma harzianum ETS 323
    • 21781279 10.1111/j.1742-4658.2011.08262.x 1:CAS:528:DC%2BC3MXht1SitrbE
    • Yang CA, Cheng CH, Liu SY, Lo CT, Lee JW, Peng KC (2011a) Identification of antibacterial mechanism of l-amino acid oxidase derived from Trichoderma harzianum ETS 323. FEBS J 278(18):3381-3394
    • (2011) FEBS J , vol.278 , Issue.18 , pp. 3381-3394
    • Yang, C.A.1    Cheng, C.H.2    Liu, S.Y.3    Lo, C.T.4    Lee, J.W.5    Peng, K.C.6
  • 76
    • 79955695549 scopus 로고    scopus 로고
    • A novel l-amino acid oxidase from Trichoderma harzianum ETS 323 associated with antagonism of Rhizoctonia solani
    • 21456553 10.1021/jf104603w 1:CAS:528:DC%2BC3MXktFens7s%3D
    • Yang CA, Cheng CH, Lo CT, Liu SY, Lee JW, Peng KC (2011b) A novel l-amino acid oxidase from Trichoderma harzianum ETS 323 associated with antagonism of Rhizoctonia solani. J Agric Food Chem 59(9):4519-4526
    • (2011) J Agric Food Chem , vol.59 , Issue.9 , pp. 4519-4526
    • Yang, C.A.1    Cheng, C.H.2    Lo, C.T.3    Liu, S.Y.4    Lee, J.W.5    Peng, K.C.6
  • 77
    • 84857261898 scopus 로고    scopus 로고
    • Advances in non-snake venom L-amino acid oxidase
    • 22367642 10.1007/s12010-012-9611-1 1:CAS:528:DC%2BC38Xnt1ait7c%3D
    • Yu Z, Qiao H (2012) Advances in non-snake venom L-amino acid oxidase. Appl Biochem Biotechnol 167(1):1-13
    • (2012) Appl Biochem Biotechnol , vol.167 , Issue.1 , pp. 1-13
    • Yu, Z.1    Qiao, H.2
  • 78
    • 84946388376 scopus 로고
    • Uber eine neue l-aminosaüre-oxydase
    • 10.1002/hlca.194402701241 1:CAS:528:DyaH28XhtFCrtg%3D%3D
    • Zeller EA, Maritz A (1944) Uber eine neue l-aminosaüre-oxydase. Helv Chim Acta 27:1888-1902
    • (1944) Helv Chim Acta , vol.27 , pp. 1888-1902
    • Zeller, E.A.1    Maritz, A.2
  • 79
    • 12344308486 scopus 로고    scopus 로고
    • Purification, partial characterization, crystallization and structural determination of AHP-LAAO, a novel l-amino-acid oxidase with cell apoptosis-inducing activity from Agkistrodon halys pallas venom
    • 15103157 10.1107/S0907444904000046
    • Zhang H, Teng M, Niu L, Wang Y, Wang Y, Liu Q, Huang Q, Hao Q, Dong Y, Liu P (2004) Purification, partial characterization, crystallization and structural determination of AHP-LAAO, a novel l-amino-acid oxidase with cell apoptosis-inducing activity from Agkistrodon halys pallas venom. Acta Crystallogr D Biol Crystallogr 60(5):974-977
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , Issue.5 , pp. 974-977
    • Zhang, H.1    Teng, M.2    Niu, L.3    Wang, Y.4    Wang, Y.5    Liu, Q.6    Huang, Q.7    Hao, Q.8    Dong, Y.9    Liu, P.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.