메뉴 건너뛰기




Volumn 93, Issue 2, 2012, Pages 503-516

L-Aspartate dehydrogenase: Features and applications

Author keywords

Applications; Characteristics; Functions; l Amino acid dehydrogenase; l Aspartate dehydrogenase; NAD biosynthesis

Indexed keywords

BIOTECHNOLOGICAL APPLICATIONS; CATALYTIC PROPERTIES; CHARACTERISTICS; COENZYME REGENERATION SYSTEMS; COFACTORS; DIAGNOSTIC KIT; IN-VIVO; INDUSTRIAL PROCESSS; L-AMINO ACID DEHYDROGENASE; L-AMINO ACIDS; L-ASPARTATE DEHYDROGENASE; MESOPHILIC; NEW MEMBERS; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATES; NICOTINAMIDE ADENINE DINUCLEOTIDES; OXIDATIVE DEAMINATION; PHARMACEUTICAL PEPTIDES; POTENTIAL APPLICATIONS; ROOM TEMPERATURE;

EID: 84856300030     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-011-3730-4     Document Type: Review
Times cited : (21)

References (103)
  • 1
    • 0034608289 scopus 로고    scopus 로고
    • Production of recombinant L-leucine dehydrogenase from Bacillus cereus in pilot scale using the runaway replication system E. coli[pIET98]
    • DOI 10.1002/(SICI)1097-0290(20000605)68:5<557::AID-BIT10>3.0.CO;2-J
    • Ansorge MB, Kula MR (2000) Production of recombinant L-leucine dehydrogenase from Bacillus cereus in pilot scale using the runaway replication system E. coli [pIET98]. Biotechnol Bioeng 68:557-562 (Pubitemid 30307726)
    • (2000) Biotechnology and Bioengineering , vol.68 , Issue.5 , pp. 557-562
    • Ansorge, M.B.1    Kula, M.-R.2
  • 2
    • 0031935432 scopus 로고    scopus 로고
    • Thermostable phenylalanine dehydrogenase from a mesophilic Microbacterium sp. strain DM 86-1
    • DOI 10.1007/s002030050564
    • Asano Y, Tanetani M (1998) Thermostable phenylalanine dehydrogenase from a mesophilic Microbacterium sp. strain DM 86-1. Arch Microbiol 169:220-224 (Pubitemid 28098693)
    • (1998) Archives of Microbiology , vol.169 , Issue.3 , pp. 220-224
    • Asano, Y.1    Tanetani, M.2
  • 3
    • 0023664631 scopus 로고
    • Novel phenylalanine dehydrogenases from Sporosarcina ureae and Bacillus sphaericus. Purification and characterization
    • 1:CAS:528:DyaL2sXlt12ltb8%3D
    • Asano Y, Nakazawa A, Endo K (1987a) Novel phenylalanine dehydrogenases from Sporosarcina ureae and Bacillus sphaericus. Purification and characterization. J Biol Chem 262:10346-10354
    • (1987) J Biol Chem , vol.262 , pp. 10346-10354
    • Asano, Y.1    Nakazawa, A.2    Endo, K.3
  • 4
    • 0023424838 scopus 로고
    • Phenylalanine dehydrogenase of Bacillus badius. Purification, characterization and gene cloning
    • 1:CAS:528:DyaL2sXlvFWqtbk%3D
    • Asano Y, Nakazawa A, Endo K, Hibino Y, Ohmori M, Numao N, Kondo K (1987b) Phenylalanine dehydrogenase of Bacillus badius. Purification, characterization and gene cloning. Eur J Biochem 168:153-159
    • (1987) Eur J Biochem , vol.168 , pp. 153-159
    • Asano, Y.1    Nakazawa, A.2    Endo, K.3    Hibino, Y.4    Ohmori, M.5    Numao, N.6    Kondo, K.7
  • 6
    • 0029645116 scopus 로고
    • A role for quaternary structure in the substrate specificity of leucine dehydrogenase
    • 1:CAS:528:DyaK2MXntF2rsr0%3D
    • Baker PJ, Turnbull AP, Sedelnikova SE, Stillman TJ, Rice DW (1995) A role for quaternary structure in the substrate specificity of leucine dehydrogenase. Structure 3:693-705
    • (1995) Structure , vol.3 , pp. 693-705
    • Baker, P.J.1    Turnbull, A.P.2    Sedelnikova, S.E.3    Stillman, T.J.4    Rice, D.W.5
  • 7
    • 0031846232 scopus 로고    scopus 로고
    • Analysis of the structure and substrate binding of Phormidium lapideum alanine dehydrogenase
    • 1:CAS:528:DyaK1cXks1entLc%3D
    • Baker PJ, Sawa Y, Shibata H, Sedelnikova SE, Rice DW (1998) Analysis of the structure and substrate binding of Phormidium lapideum alanine dehydrogenase. Nat Struct Biol 5:561-567
    • (1998) Nat Struct Biol , vol.5 , pp. 561-567
    • Baker, P.J.1    Sawa, Y.2    Shibata, H.3    Sedelnikova, S.E.4    Rice, D.W.5
  • 8
    • 0019363132 scopus 로고
    • Amino acid degradation by anaerobic bacteria
    • 1:CAS:528:DyaL3MXkvFentL4%3D
    • Barker HA (1981) Amino acid degradation by anaerobic bacteria. Annu Rev Biochem 50:23-40
    • (1981) Annu Rev Biochem , vol.50 , pp. 23-40
    • Barker, H.A.1
  • 11
    • 9644294199 scopus 로고    scopus 로고
    • The first crystal structure of hyperthermostable NAD-dependent glutamate dehydrogenase from Pyrobaculum islandicum
    • DOI 10.1016/j.jmb.2004.10.063, PII S0022283604013695
    • Bhuiya MW, Sakuraba H, Ohshima T, Imagawa T, Katunuma N, Tsuge H (2005) The first crystal structure of hyperthermostable NAD-dependent glutamate dehydrogenase from Pyrobaculum islandicum. J Mol Biol 345:325-337 (Pubitemid 39574854)
    • (2005) Journal of Molecular Biology , vol.345 , Issue.2 , pp. 325-337
    • Bhuiya, M.W.1    Sakuraba, H.2    Ohshima, T.3    Imagawa, T.4    Katunuma, N.5    Tsuge, H.6
  • 12
    • 0032530505 scopus 로고    scopus 로고
    • Biocatalysis to amino acid-based chiral pharmaceuticals - Examples and perspectives
    • DOI 10.1016/S1381-1177(98)00009-5, PII S1381117798000095
    • Bommarius AS, Schwarm M, Drauz K (1998) Biocatalysis to amino acid-based chiral pharmaceuticals-examples and perspectives. J Mol Catal B: Enzym 5:1-11 (Pubitemid 28429167)
    • (1998) Journal of Molecular Catalysis - B Enzymatic , vol.5 , Issue.1-4 , pp. 1-11
    • Bommarius, A.S.1    Schwarm, M.2    Drauz, K.3
  • 13
    • 0027755179 scopus 로고
    • Evolution of substrate diversity in the superfamily of amino acid dehydrogenases. Prospects for rational chiral synthesis
    • 1:CAS:528:DyaK2cXhtVShtLo%3D
    • Britton KL, Baker PJ, Engel PC, Rice DW, Stillman TJ (1993) Evolution of substrate diversity in the superfamily of amino acid dehydrogenases. Prospects for rational chiral synthesis. J Mol Biol 234:938-945
    • (1993) J Mol Biol , vol.234 , pp. 938-945
    • Britton, K.L.1    Baker, P.J.2    Engel, P.C.3    Rice, D.W.4    Stillman, T.J.5
  • 15
    • 0028587754 scopus 로고
    • The biochemistry and enzymology of amino acid dehydrogenases
    • 1:CAS:528:DyaK2MXktFKksL8%3D
    • Brunhuber NM, Blanchard JS (1994) The biochemistry and enzymology of amino acid dehydrogenases. Crit Rev Biochem Mol Biol 29:415-467
    • (1994) Crit Rev Biochem Mol Biol , vol.29 , pp. 415-467
    • Brunhuber, N.M.1    Blanchard, J.S.2
  • 16
    • 4744341276 scopus 로고    scopus 로고
    • Enantioselective synthesis of non-natural amino acids using phenylalanine dehydrogenases modified by site-directed mutagenesis
    • 1:CAS:528:DC%2BD2cXnt1Grsrc%3D
    • Busca P, Paradisi F, Moynihan E, Maguirem AR, Engel PC (2004) Enantioselective synthesis of non-natural amino acids using phenylalanine dehydrogenases modified by site-directed mutagenesis. Org Biomol Chem 2:2684-2691
    • (2004) Org Biomol Chem , vol.2 , pp. 2684-2691
    • Busca, P.1    Paradisi, F.2    Moynihan, E.3    Maguirem, A.R.4    Engel, P.C.5
  • 18
    • 0034237491 scopus 로고    scopus 로고
    • Selective production of L-aspartic acid and L-phenylalanine by coupling reactions of aspartase and aminotransferase in Escherichia coli
    • DOI 10.1016/S0141-0229(00)00149-6, PII S0141022900001496
    • Chao Y, Lo T, Luo N (2000) Selective production of L-aspartic acid and L-phenylalanine by coupling reactions of aspartase and aminotransferase in Escherichia coli. Enzyme Microb Technol 27:19-25 (Pubitemid 30345482)
    • (2000) Enzyme and Microbial Technology , vol.27 , Issue.1-2 , pp. 19-25
    • Chao, Y.-P.1    Lo, T.-E.2    Luo, N.-S.3
  • 19
    • 33847653796 scopus 로고    scopus 로고
    • An engineered mutant, L307V of phenylalanine dehydrogenase from Bacillus sphaericus: high activity and stability in organic-aqueous solvent mixtures and utility for synthesis of non-natural l-amino acids
    • DOI 10.1016/j.enzmictec.2006.10.021, PII S0141022906005229
    • Chen S, Engel PC (2007) An engineered mutant, L307V of phenylalanine dehydrogenase from Bacillus sphaericus: high activity and stability in organic-aqueous solvent mixtures and utility for synthesis of non-natural l-amino acids. Enzyme Microb Technol 40:1407-1411 (Pubitemid 46356553)
    • (2007) Enzyme and Microbial Technology , vol.40 , Issue.5 , pp. 1407-1411
    • Chen, S.1    Engel, P.C.2
  • 20
    • 0005594143 scopus 로고
    • Properties of alanine dehydrogenase and aspartase from Propionibacterium freudenreichii subsp. shermanii
    • 1:CAS:528:DyaL2sXlt12ltbo%3D
    • Crow VL (1987) Properties of alanine dehydrogenase and aspartase from Propionibacterium freudenreichii subsp. shermanii. Appl Environ Microbiol 53:1885-1892
    • (1987) Appl Environ Microbiol , vol.53 , pp. 1885-1892
    • Crow, V.L.1
  • 22
    • 0028833474 scopus 로고
    • Expression and in vitro assembly of recombinant glutamate dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus
    • 1:CAS:528:DyaK2MXivValu7s%3D
    • Diruggiero J, Robb FT (1995) Expression and in vitro assembly of recombinant glutamate dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus. Appl Environ Microbiol 61:159-164
    • (1995) Appl Environ Microbiol , vol.61 , pp. 159-164
    • Diruggiero, J.1    Robb, F.T.2
  • 23
    • 0026698896 scopus 로고
    • Enzymatic method for phenylketonuria screening using phenylalanine dehydrogenase
    • 1:CAS:528:DyaK3sXjtFOm
    • Dooley KC (1992) Enzymatic method for phenylketonuria screening using phenylalanine dehydrogenase. Clin Biochem 25:271-275
    • (1992) Clin Biochem , vol.25 , pp. 271-275
    • Dooley, K.C.1
  • 25
    • 0025213163 scopus 로고
    • Preparation of stereoselectively-deuterated NADH and NADPH by coupling of glutamate racemase and glutamate dehydrogenase
    • Esaki N, Nakajima N, Nakamura K, Yonaha K, Tanaka H, Soda K (1990) Preparation of stereoselectively-deuterated NADH and NADPH by coupling of glutamate racemase and glutamate dehydrogenase. Biotechnol Lett 12:105-110 (Pubitemid 20116576)
    • (1990) Biotechnology Letters , vol.12 , Issue.2 , pp. 105-110
    • Esaki, N.1    Nakajima, N.2    Nakamura, K.3    Yonaha, K.4    Tanaka, H.5    Soda, K.6
  • 26
    • 0037144592 scopus 로고    scopus 로고
    • Identification and expression of a cDNA encoding human alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD). A key enzyme for the tryptophan-niacine pathway and "quinolinate hypothesis"
    • 1:CAS:528:DC%2BD38Xnt1Wnsro%3D
    • Fukuoka S, Ishiguro K, Yanagihara K, Tanabe A, Egashira Y, Sanada H, Shibata K (2002) Identification and expression of a cDNA encoding human alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD). A key enzyme for the tryptophan-niacine pathway and "quinolinate hypothesis". J Biol Chem 277:35162-35167
    • (2002) J Biol Chem , vol.277 , pp. 35162-35167
    • Fukuoka, S.1    Ishiguro, K.2    Yanagihara, K.3    Tanabe, A.4    Egashira, Y.5    Sanada, H.6    Shibata, K.7
  • 27
    • 0025024177 scopus 로고
    • Synthesis of L-β-hydroxyvaline from α-keto-β- hydroxyisovalerate using leucine dehydrogenase from bacillus species
    • DOI 10.1016/0045-2068(90)90033-2
    • Hanson RL, Singh J, Kissick TP, Patel RN, Szarka LJ, Mueller RH (1990) Synthesis of L-hydrohyvaline from keto hydroxyisovalerate using LeuDH from Bacillus species. Bioorg Chem 18:116-130 (Pubitemid 20285506)
    • (1990) Bioorganic Chemistry , vol.18 , Issue.2 , pp. 116-130
    • Hanson, R.L.1    Singh, J.2    Kissick, T.P.3    Patel, R.N.4    Szarka, L.J.5    Mueller, R.H.6
  • 28
    • 0021212133 scopus 로고
    • Characterization of Peptostreptococcus asaccharolyticus glutamate dehydrogenase purified by dye-ligand chromatography
    • Hornby DP, Engel PC (1984) Characterization of Peptostreptococcus asaccharolyticus glutamate dehydrogenase purified by dye-ligand chromatography. J Gen Microbiol 130:2385-2394 (Pubitemid 14007215)
    • (1984) Journal of General Microbiology , vol.130 , Issue.9 , pp. 2385-2394
    • Hornby, D.P.1    Engel, P.C.2
  • 29
    • 0027333040 scopus 로고
    • L-Glutamate dehydrogenases: Distribution, properties and mechanism
    • 1:STN:280:DyaK2c7jtVGhsQ%3D%3D
    • Hudson RC, Daniel RM (1993) L-Glutamate dehydrogenases: distribution, properties and mechanism. Comp Biochem Physiol 106:767-792
    • (1993) Comp Biochem Physiol , vol.106 , pp. 767-792
    • Hudson, R.C.1    Daniel, R.M.2
  • 30
    • 0021325176 scopus 로고
    • Isolation and characterization of a bacterium possessing L-phenylalanine dehydrogenase activity
    • Hummel W, Weiss N, Kula MR (1984) Isolation and characterization of a bacterium possessing L-phenylalanine dehydrogenase activity. Arch Microbiol 137:47-52 (Pubitemid 14191495)
    • (1984) Archives of Microbiology , vol.137 , Issue.1 , pp. 47-52
    • Hummel, W.1    Weiss, N.2    Kula, M.R.3
  • 31
    • 0000798607 scopus 로고
    • Isolation of L-phenylalanine dehydrogenase from Rhodococcus sp. M4 and its application for the production of L-phenylalanine
    • 1:CAS:528:DyaL2sXltlamt74%3D
    • Hummel W, Schuette H, Schmidt E, Wandrey C, Kula MR (1987) Isolation of L-phenylalanine dehydrogenase from Rhodococcus sp. M4 and its application for the production of L-phenylalanine. Appl Microbiol Biotechnol 26:409-416
    • (1987) Appl Microbiol Biotechnol , vol.26 , pp. 409-416
    • Hummel, W.1    Schuette, H.2    Schmidt, E.3    Wandrey, C.4    Kula, M.R.5
  • 32
    • 0142074820 scopus 로고    scopus 로고
    • An efficient and selective enzymatic oxidation system for the synthesis of enantiomerically pure D-tert-Leucine
    • DOI 10.1021/ol035314g
    • Hummel W, Kuzu M, Geueke B (2003) An efficient and selective enzymatic oxidation system for the synthesis of enantiomerically pure D-tert-leucine. Org Lett 5:3649-3650 (Pubitemid 37289546)
    • (2003) Organic Letters , vol.5 , Issue.20 , pp. 3649-3650
    • Hummel, W.1    Kuzu, M.2    Geueke, B.3
  • 33
    • 0033988539 scopus 로고    scopus 로고
    • Valine dehydrogenase from Streptomyces albus: Gene cloning, heterologous expression and identification of active site by site-directed mutagenesis
    • DOI 10.1016/S0378-1097(99)00561-3, PII S0378109799005613
    • Hyun CG, Kim SS, Park KH, Suh JW (2000) Valine dehydrogenase from Streptomyces albus: gene cloning, heterologous expression and identification of active site by site-directed mutagenesis. FEMS Microbiol Lett 182:29-34 (Pubitemid 30001560)
    • (2000) FEMS Microbiology Letters , vol.182 , Issue.1 , pp. 29-34
    • Hyun, C.-G.1    Kim, S.S.2    Park, K.-H.3    Suh, J.-W.4
  • 34
    • 0347337722 scopus 로고    scopus 로고
    • Alanine dehydrogenase from the psychrophilic bacterium strain PA-43: Overexpression, molecular characterization, and sequence analysis
    • DOI 10.1007/s00792-002-0305-4
    • Irwin JA, Lynch SV, Coughlan S, Baker PJ, Gudmundsson HM, Alfredsson GA, Rice DW, Engel PC (2003) Alanine dehydrogenase from the psychrophilic bacterium strain PA-43: overexpression, molecular characterization, and sequence analysis. Extremophiles 7:135-143 (Pubitemid 40924483)
    • (2003) Extremophiles , vol.7 , Issue.2 , pp. 135-143
    • Irwin, J.A.1    Lynch, S.V.2    Coughlan, S.3    Baker, P.J.4    Gudmundsson, H.M.5    Alfredsson, G.A.6    Rice, D.W.7    Engel, P.C.8
  • 35
    • 0015352684 scopus 로고
    • Purification and characterization of glutamic acid dehydrogenase and alphaketoglutaric acid reductase from Peptococcus aerogenes
    • 1:CAS:528:DyaE38XksVCks70%3D
    • Johnson WM, Westlake DWS (1972) Purification and characterization of glutamic acid dehydrogenase and alphaketoglutaric acid reductase from Peptococcus aerogenes. Can J Microbiol 18:881-892
    • (1972) Can J Microbiol , vol.18 , pp. 881-892
    • Johnson, W.M.1    Westlake, D.W.S.2
  • 36
    • 0014226311 scopus 로고
    • Soluble valine dehydrogeaase from roots of plant seedlings
    • 1:CAS:528:DyaF1cXhtVajsL4%3D
    • Kagan ZS, Poliakov VA, Kretovich VL (1968) Soluble valine dehydrogeaase from roots of plant seedlings. Biokhimiia 33:89-96
    • (1968) Biokhimiia , vol.33 , pp. 89-96
    • Kagan, Z.S.1    Poliakov, V.A.2    Kretovich, V.L.3
  • 37
    • 0014459715 scopus 로고
    • Purification and properties of valine dehydrogenase
    • 1:CAS:528:DyaF1MXhtVeisbc%3D
    • Kagan ZS, Poliakov VA, Kretovich VL (1969) Purification and properties of valine dehydrogenase. Biokhimiia 34:59-65
    • (1969) Biokhimiia , vol.34 , pp. 59-65
    • Kagan, Z.S.1    Poliakov, V.A.2    Kretovich, V.L.3
  • 39
    • 0042433514 scopus 로고    scopus 로고
    • Alteration of substrate specificity of leucine dehydrogenase by site-directed mutagenesis
    • DOI 10.1016/S1381-1177(03)00093-6
    • Kataoka K, Tanizawa K (2003) Alteration of substrate specificity of leucine dehydrogenase by site-directed mutagenesis. J Mol Catal B: Enzym 23:299-309 (Pubitemid 37011205)
    • (2003) Journal of Molecular Catalysis B: Enzymatic , vol.23 , Issue.2-6 , pp. 299-309
    • Kataoka, K.1    Tanizawa, K.2
  • 40
    • 2442687050 scopus 로고    scopus 로고
    • Molecular biology of pyridine nucleotide and nicotine biosynthesis
    • d1500-1993
    • Katoh A, Hashimoto T (2004) Molecular biology of pyridine nucleotide and nicotine biosynthesis. Front Biosci 9:1577-1586 (Pubitemid 38918616)
    • (2004) Frontiers in Bioscience , vol.9 , pp. 1577-1586
    • Katoh, A.1    Hashimoto, T.2
  • 41
    • 0042433532 scopus 로고    scopus 로고
    • Purification and characterization of leucine dehydrogenase from an alkaliphilic halophile, Natronobacterium magadii MS-3
    • DOI 10.1016/S1381-1177(03)00085-7
    • Katoh R, Ngata S, Ozawa A, Ohshima T, Kamekura M, Misono H (2003) Purification and characterization of leucine dehydrogenase from an alkalophilic halophile, Natronobacterium magadii MS-3. J Mol Catal B: Enzym 23:231-238 (Pubitemid 37011197)
    • (2003) Journal of Molecular Catalysis B: Enzymatic , vol.23 , Issue.2-6 , pp. 231-238
    • Katoh, R.1    Ngata, S.2    Ozawa, A.3    Ohshima, T.4    Kamekura, M.5    Misono, H.6
  • 42
    • 27644547321 scopus 로고    scopus 로고
    • Molecular properties and enhancement of thermostability by random mutagenesis of glutamate dehydrogenase from Bacillus subtilis
    • DOI 10.1271/bbb.69.1861
    • Khan IH, Ito K, Kim H, Ashida H, Ishikawa T, Shibata H, Sawa Y (2005a) Molecular properties and enhancement of thermostability by random mutagenesis of glutamate dehydrogenase from Bacillus subtilis. Biosci Biotechnol Biochem 69:1861-1870 (Pubitemid 41558849)
    • (2005) Bioscience, Biotechnology and Biochemistry , vol.69 , Issue.10 , pp. 1861-1870
    • Khan, Md.I.H.1    Ito, K.2    Kim, H.3    Ashida, H.4    Ishikawa, T.5    Shibata, H.6    Sawa, Y.7
  • 43
    • 25844449629 scopus 로고    scopus 로고
    • Altering the substrate specificity of glutamate dehydrogenase from Bacillus subtilis by site-directed mutagenesis
    • DOI 10.1271/bbb.69.1802
    • Khan IH, Kim H, Ashida H, Ishikawa T, Shibata H, Sawa Y (2005b) Altering the substrate specificity of glutamate dehydrogenase from Bacillus subtilis by site-directed mutagenesis. Biosci Biotechnol Biochem 69:1802-1805 (Pubitemid 41390176)
    • (2005) Bioscience, Biotechnology and Biochemistry , vol.69 , Issue.9 , pp. 1802-1805
    • Khan, Md.I.H.1    Kim, H.2    Ashida, H.3    Ishikawa, T.4    Shibata, H.5    Sawa, Y.6
  • 44
    • 0031564613 scopus 로고    scopus 로고
    • Crystal structure of glutamate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima at 3.0 A resolution
    • DOI 10.1006/jmbi.1996.0900
    • Knapp S, de Vos WM, Rice D, Ladenstein R (1997) Crystal structure of glutamate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima at 3.0A resolution. J Mol Biol 267:916-932 (Pubitemid 27192663)
    • (1997) Journal of Molecular Biology , vol.267 , Issue.4 , pp. 916-932
    • Knapp, S.1    De Vos, W.M.2    Rice, D.3    Ladenstein, R.4
  • 45
    • 0029891893 scopus 로고    scopus 로고
    • Continuous production of L-tert-leucine in series of two enzyme membrane reactors-modelling and computer simulation
    • 1:CAS:528:DyaK28Xjt1yju7c%3D
    • Kragl U, Vasic-Racki D, Wandrey C (1996) Continuous production of L-tert-leucine in series of two enzyme membrane reactors-modelling and computer simulation. Bioprocess Eng 14:291-297
    • (1996) Bioprocess Eng , vol.14 , pp. 291-297
    • Kragl, U.1    Vasic-Racki, D.2    Wandrey, C.3
  • 48
    • 70349320054 scopus 로고    scopus 로고
    • Cloning, protein sequence clarification, and substrate specificity of a leucine dehydrogenase from Bacillus sphaericus ATCC4525
    • Li H, Zhu D, Hyatt BA, Malik FM, Biehl ER, Hua L (2008) Cloning, protein sequence clarification, and substrate specificity of a leucine dehydrogenase from Bacillus sphaericus ATCC4525. Appl Biochem Biotechnol 158:343-351
    • (2008) Appl Biochem Biotechnol , vol.158 , pp. 343-351
    • Li, H.1    Zhu, D.2    Hyatt, B.A.3    Malik, F.M.4    Biehl, E.R.5    Hua, L.6
  • 49
    • 80052006833 scopus 로고    scopus 로고
    • A non-NadB type L-aspartate dehydrogenase from Ralstonia eutropha strain JMP134: Molecular characterization and physiological functions
    • 1:CAS:528:DC%2BC3MXhtFeqs7zP
    • Li Y, Ishida M, Ashida H, Ishikawa T, Shibata H, Sawa Y (2011a) A non-NadB type L-aspartate dehydrogenase from Ralstonia eutropha strain JMP134: molecular characterization and physiological functions. Biosci Biotechnol Biochem 75:1524-1532
    • (2011) Biosci Biotechnol Biochem , vol.75 , pp. 1524-1532
    • Li, Y.1    Ishida, M.2    Ashida, H.3    Ishikawa, T.4    Shibata, H.5    Sawa, Y.6
  • 50
    • 79958202386 scopus 로고    scopus 로고
    • A novel L-aspartate dehydrogenase from the mesophilic bacterium Pseudomonas aeruginosa PAO1: Molecular characterization and application for L-aspartate production
    • 1:CAS:528:DC%2BC3MXmsFCrt74%3D
    • Li Y, Kawakami N, Ogola HJO, Ashida H, Ishikawa T, Shibata H, Sawa Y (2011b) A novel L-aspartate dehydrogenase from the mesophilic bacterium Pseudomonas aeruginosa PAO1: molecular characterization and application for L-aspartate production. Appl Microbiol Biotechnol 90:1953-1962
    • (2011) Appl Microbiol Biotechnol , vol.90 , pp. 1953-1962
    • Li, Y.1    Kawakami, N.2    Ogola, H.J.O.3    Ashida, H.4    Ishikawa, T.5    Shibata, H.6    Sawa, Y.7
  • 51
    • 0024245620 scopus 로고
    • Determination of branched-chain amino and keto acids with leucine dehydrogenase
    • DOI 10.1016/S0076-6879(88)66003-4
    • Livesey G, Lund P (1988) Determination of branched-chain amino and keto acids with leucine dehydrogenase. Methods Enzymol 166:3-10 (Pubitemid 19048571)
    • (1988) Methods in Enzymology , vol.166 , pp. 3-10
    • Livesey, G.1    Lund, P.2
  • 53
    • 0017163169 scopus 로고
    • Branched-chain amino acid catabolism in bacteria
    • 1:CAS:528:DyaE28XhslKgsb4%3D
    • Massey LK, Sokatch JR, Conrad RS (1976) Branched-chain amino acid catabolism in bacteria. Bacteriol Rev 40:42-54
    • (1976) Bacteriol Rev , vol.40 , pp. 42-54
    • Massey, L.K.1    Sokatch, J.R.2    Conrad, R.S.3
  • 54
    • 33745815337 scopus 로고    scopus 로고
    • A close look at NAD biosynthesis
    • DOI 10.1038/nsmb0706-563, PII NSMB0706563
    • Mattevi A (2006) A close look at NAD biosynthesis. Nat Struct Mol Biol 13:563-564 (Pubitemid 44036461)
    • (2006) Nature Structural and Molecular Biology , vol.13 , Issue.7 , pp. 563-564
    • Mattevi, A.1
  • 55
    • 0001406338 scopus 로고    scopus 로고
    • Structure of L-aspartate oxidase: Implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family
    • DOI 10.1016/S0969-2126(99)80099-9
    • 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 7:745-756 (Pubitemid 29329846)
    • (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
  • 57
    • 0028865193 scopus 로고
    • Nitrogen control in bacteria
    • 1:CAS:528:DyaK28XmvFWiug%3D%3D
    • Merrick MJ, Edwards RA (1995) Nitrogen control in bacteria. Microbiol Rev 59:604-622
    • (1995) Microbiol Rev , vol.59 , pp. 604-622
    • Merrick, M.J.1    Edwards, R.A.2
  • 58
    • 0023390213 scopus 로고
    • Use of bio-reactor consisting of sequentially aligned L-glutamate dehydrogenase and L-glutamate oxidase for the determination of ammonia by chemiluminescence
    • 1:CAS:528:DyaL2sXlslWksL4%3D
    • Murachi T, Tabata M (1987) Use of bio-reactor consisting of sequentially aligned L-glutamate dehydrogenase and L-glutamate oxidase for the determination of ammonia by chemiluminescence. Biotechnol Appl Biochem 9:303-309
    • (1987) Biotechnol Appl Biochem , vol.9 , pp. 303-309
    • Murachi, T.1    Tabata, M.2
  • 60
    • 78650297006 scopus 로고    scopus 로고
    • Visible wavelength spectrophotometric assays of L-aspartate and D-aspartate using hyperthermophilic enzyme systems
    • 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 409:1-6
    • (2011) Anal Biochem , vol.409 , pp. 1-6
    • Mutaguchi, Y.1    Ohmori, T.2    Sakuraba, H.3    Yoneda, K.4    Doi, K.5    Ohshima, T.6
  • 62
  • 63
    • 0020080252 scopus 로고
    • L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase
    • Nasu S, Wicks FD, Gholson RK (1982) L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase. J Biol Chem 257:626-632 (Pubitemid 12110193)
    • (1982) Journal of Biological Chemistry , vol.257 , Issue.2 , pp. 626-632
    • Nasu, S.1    Wicks, F.D.2    Gholson, R.K.3
  • 64
    • 0025092074 scopus 로고
    • Purification of an inducible L-valine dehydrogenase of Streptomyces coelicolor A3(2)
    • Navarrete RM, Vara JA, Hutchinson CR (1990) Purification of an inducible L-valine dehydrogenase of Streptomyces coelicolor A3(2). J Gen Microbiol 136:273-281 (Pubitemid 20059108)
    • (1990) Journal of General Microbiology , vol.136 , Issue.2 , pp. 273-281
    • Navarrete, R.M.1    Vara, J.A.2    Hutchinson, C.R.3
  • 65
    • 0024711964 scopus 로고
    • Thermostable amino acid dehydrogenases: Applications and gene cloning
    • Ohshima T, Soda K (1989) Thermostable amino acid dehydrogenases: applications and gene cloning. Trends Biotechnol 7:210-214 (Pubitemid 19189285)
    • (1989) Trends in Biotechnology , vol.7 , Issue.8 , pp. 210-214
    • Ohshima, T.1    Soda, K.2
  • 66
    • 0025617067 scopus 로고
    • Biochemistry and biotechnology of amino acid dehydrogenases
    • 1:CAS:528:DyaK3MXktVemurY%3D
    • Ohshima T, Soda K (1990) Biochemistry and biotechnology of amino acid dehydrogenases. Adv Biochem Eng Biotechnol 42:187-209
    • (1990) Adv Biochem Eng Biotechnol , vol.42 , pp. 187-209
    • Ohshima, T.1    Soda, K.2
  • 67
    • 2342601115 scopus 로고    scopus 로고
    • Stereoselective biocatalysis: Amino acid dehydrogenases and their applications
    • R.N. Patel (eds). Marcel Dekker New York, USA
    • Ohshima T, Soda K (2000) Stereoselective biocatalysis: amino acid dehydrogenases and their applications. In: Patel RN (ed) Stereoselective biocatalysis. Marcel Dekker, New York, USA, pp 877-903
    • (2000) Stereoselective Biocatalysis , pp. 877-903
    • Ohshima, T.1    Soda, K.2
  • 68
    • 0018183909 scopus 로고
    • Leucine dehydrogenase of Bacillus sphaericus: sulfhydryl groups and catalytic sites
    • Ohshima T, Yamamoto T, Misono H, Soda K (1978) Leucine dehydrogenase of Bacillus sphaericus: sulfhydryl groups and catalytic sites. Agric Biol Chem 42:1739-1743 (Pubitemid 9039425)
    • (1978) Agricultural and Biological Chemistry , vol.42 , Issue.9 , pp. 1739-1743
    • Ohshima, T.1    Yamamoto, T.2    Misono, H.3    Soda, K.4
  • 69
    • 0028360284 scopus 로고
    • The purification, characterization, cloning and sequencing of the gene for a halostable and thermostable leucine dehydrogenase from Thermoactinomyces intermedius
    • DOI 10.1111/j.1432-1033.1994.tb18869.x
    • Ohshima T, Nishida N, Bakthavatsalam S, Kataoka K, Takada H, Yoshimura T, Esaki N, Soda K (1994) The purification, characterization, cloning and sequencing of the gene for a halostable and thermostable leucine dehydrogenase from Thermoactinomyces intermedius. Eur J Biochem 222:305-312 (Pubitemid 24204899)
    • (1994) European Journal of Biochemistry , vol.222 , Issue.2 , pp. 305-312
    • Ohshima, T.1    Nishida, N.2    Bakthavatsalam, S.3    Kataoka, K.4    Takada, H.5    Yoshimura, T.6    Esaki, N.7    Soda, K.8
  • 70
    • 0034825839 scopus 로고    scopus 로고
    • Psychrophilic valine dehydrogenase of the antarctic psychrophile, Cytophaga sp. KUC-1. Purification, molecular characterization and expression
    • DOI 10.1046/j.1432-1327.2001.02353.x
    • Oikawa T, Yamanaka K, Kazuoka T, Kanzawa N, Soda K (2001) Psychrophilic valine dehydrogenase of the antarctic psychrophile, Cytophaga sp. KUC-1: purification, molecular characterization and expression. Eur J Biochem 268:4375-4383 (Pubitemid 32862846)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.16 , pp. 4375-4383
    • Oikawa, T.1    Yamanaka, K.2    Kazuoka, T.3    Kanzawa, N.4    Soda, K.5
  • 72
    • 0036788065 scopus 로고    scopus 로고
    • Cloning and expression of Bacillus sphaericus phenylalanine dehydrogenase gene in Bacillus subtilis cells: Purification and enzyme properties
    • 1:CAS:528:DC%2BD38Xms1elt7o%3D
    • Omidinia E, Samadi A, Taherkhani H, Khatami S, Moazami N, Pouraie RR, Asano Y (2002) Cloning and expression of Bacillus sphaericus phenylalanine dehydrogenase gene in Bacillus subtilis cells: purification and enzyme properties. World J Microbiol Biotechnol 18:593-597
    • (2002) World J Microbiol Biotechnol , vol.18 , pp. 593-597
    • Omidinia, E.1    Samadi, A.2    Taherkhani, H.3    Khatami, S.4    Moazami, N.5    Pouraie, R.R.6    Asano, Y.7
  • 73
    • 33846105845 scopus 로고    scopus 로고
    • Phenylalanine dehydrogenase mutants: Efficient biocatalysts for synthesis of non-natural phenylalanine derivatives
    • DOI 10.1016/j.jbiotec.2006.08.008, PII S0168165606006973
    • Paradisi F, Collins S, Maguire AR, Engel PC (2007) Phenylalanine dehydrogenase mutants: efficient biocatalysts for synthesis of non-natural phenylalanine derivatives. J Biotechnol 128:408-411 (Pubitemid 46074186)
    • (2007) Journal of Biotechnology , vol.128 , Issue.2 , pp. 408-411
    • Paradisi, F.1    Collins, S.2    Maguire, A.R.3    Engel, P.C.4
  • 74
    • 0033565447 scopus 로고    scopus 로고
    • The structure of bovine glutamate dehydrogenase provides insights into the mechanism of allostery
    • DOI 10.1016/S0969-2126(99)80101-4
    • Peterson PE, Smith TJ (1999) The structure of bovine glutamate dehydrogenase provides insights into the mechanism of allostery. Structure Fold Des 7:769-782 (Pubitemid 29329848)
    • (1999) Structure , vol.7 , Issue.7 , pp. 769-782
    • Peterson, P.E.1    Smith, T.J.2
  • 75
    • 0024323009 scopus 로고
    • Purification and catalytic properties of L-valine dehydrogenase from Streptomyces cinnamonensis
    • Priestley ND, Robinson JA (1989) Purification and catalytic properties of L-valine dehydrogenase from Streptomyces cinnamonensis. Biochem J 261:853-861 (Pubitemid 19209526)
    • (1989) Biochemical Journal , vol.261 , Issue.3 , pp. 853-861
    • Priestley, N.D.1    Robinson, J.A.2
  • 76
    • 67650680623 scopus 로고    scopus 로고
    • Molecular analyses of the rice glutamate dehydrogenase gene family and their response to nitrogen and phosphorous deprivation
    • 1:CAS:528:DC%2BD1MXnslSrurs%3D
    • Qiu X, Xie W, Lian X, Zhang Q (2009) Molecular analyses of the rice glutamate dehydrogenase gene family and their response to nitrogen and phosphorous deprivation. Plant Cell Rep 28:1115-1126
    • (2009) Plant Cell Rep , vol.28 , pp. 1115-1126
    • Qiu, X.1    Xie, W.2    Lian, X.3    Zhang, Q.4
  • 77
    • 0001526201 scopus 로고
    • L-Leucine dehydrogenase of Bacillus cereus
    • 1:CAS:528:DyaF38XptFKl
    • Sanwal BD, Zink MW (1961) L-Leucine dehydrogenase of Bacillus cereus. Arch Biochem Biophys 94:430-435
    • (1961) Arch Biochem Biophys , vol.94 , pp. 430-435
    • Sanwal, B.D.1    Zink, M.W.2
  • 78
    • 0027984543 scopus 로고
    • Purification and characterization of alanine dehydrogenase from a cyanobacterium, Phormidium lapideum
    • Sawa Y, Tani M, Murata K, Shibata H, Ochiai H (1994) Purification and characterization of alanine dehydrogenase from a cyanobacterium, Phormidium lapideum. J Biochem 116:995-1000 (Pubitemid 24354647)
    • (1994) Journal of Biochemistry , vol.116 , Issue.5 , pp. 995-1000
    • Sawa, Y.1    Tani, L.M.2    Murata, K.3    Shibata, H.4    Ochiai, H.5
  • 79
    • 4143144860 scopus 로고    scopus 로고
    • A novel archaeal alanine dehydrogenase homologous to ornithine cyclodeaminase and μ-crystallin
    • DOI 10.1128/JB.186.22.7680-7689.2004
    • Schröder I, Vadas A, Johnson E, Lim S, Monbouquette HG (2004) A novel archaeal alanine dehydrogenase homologous to ornithine cyclodeaminase and mu-crystallin. J Bacteriol 186:7680-7689 (Pubitemid 39463734)
    • (2004) Journal of Bacteriology , vol.186 , Issue.22 , pp. 7680-7689
    • Schroder, I.1    Vadas, A.2    Johnson, E.3    Lim, S.4    Monbouquette, H.G.5
  • 81
    • 0029089874 scopus 로고
    • Alteration in relative activities of phenylalanine dehydrogenase towards different substrates by site-directed mutagenesis
    • 1:CAS:528:DyaK2MXns1CqsLg%3D
    • Seah SYK, Britton KL, Baker PJ, Rice DW, Asano Y, Engel PC (1995) Alteration in relative activities of phenylalanine dehydrogenase towards different substrates by site-directed mutagenesis. FEBS Lett 370:93-96
    • (1995) FEBS Lett , vol.370 , pp. 93-96
    • Seah, S.Y.K.1    Britton, K.L.2    Baker, P.J.3    Rice, D.W.4    Asano, Y.5    Engel, P.C.6
  • 82
    • 0037167635 scopus 로고    scopus 로고
    • Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its discrimination between phenylalanine and tyrosine substrates
    • 1:CAS:528:DC%2BD38XmsFGmsrg%3D
    • Seah SYK, Britton KL, Rice DW, Asano Y, Engel PC (2002) Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its discrimination between phenylalanine and tyrosine substrates. Biochemistry 41:11390-11397
    • (2002) Biochemistry , vol.41 , pp. 11390-11397
    • Seah, S.Y.K.1    Britton, K.L.2    Rice, D.W.3    Asano, Y.4    Engel, P.C.5
  • 83
    • 85007862532 scopus 로고
    • Leucine dehydrogenase of a thermophilic anaerobe, Clostridium thermoaceticum: Gene cloning, purification and characterization
    • 1:CAS:528:DyaL1cXptVKiug%3D%3D
    • Shimoi H, Nagata S, Esaki N, Tanaka H, Soda K (1987) Leucine dehydrogenase of a thermophilic anaerobe, Clostridium thermoaceticum: gene cloning, purification and characterization. Agric Biol Chem 51:3375-3381
    • (1987) Agric Biol Chem , vol.51 , pp. 3375-3381
    • Shimoi, H.1    Nagata, S.2    Esaki, N.3    Tanaka, H.4    Soda, K.5
  • 84
    • 0027180051 scopus 로고
    • Alanine dehydrogenase from soybean nodule bacteroids: Purification and properties
    • DOI 10.1006/abbi.1993.1365
    • Smith MT, Emerich DW (1993) Alanine dehydrogenase from soybean nodule bacteroids: purification and properties. Arch Biochem Biophys 304:379-385 (Pubitemid 23232951)
    • (1993) Archives of Biochemistry and Biophysics , vol.304 , Issue.2 , pp. 379-385
    • Smith, M.T.1    Emerich, D.W.2
  • 85
    • 0036304611 scopus 로고    scopus 로고
    • The structure of apo human glutamate dehydrogenase details subunit communication and allostery
    • DOI 10.1016/S0022-2836(02)00161-4
    • Smith TJ, Schmidt T, Fang J, Wu J, Siuzdak G, Stanley CA (2002) The structure of apo human glutamate dehydrogenase details subunit communication and allostery. J Mol Biol 318:765-777 (Pubitemid 34729367)
    • (2002) Journal of Molecular Biology , vol.318 , Issue.3 , pp. 765-777
    • Smith, T.J.1    Schmidt, T.2    Fang, J.3    Wu, J.4    Siuzdak, G.5    Stanley, C.A.6
  • 86
    • 0027769953 scopus 로고
    • Conformational flexibility in glutamate dehydrogenase. Role of water in substrate recognition and catalysis
    • 1:CAS:528:DyaK2cXhtVSnsb0%3D
    • Stillman TJ, Baker PJ, Britton KL, Rice DW (1993) Conformational flexibility in glutamate dehydrogenase. Role of water in substrate recognition and catalysis. J Mol Biol 234:1131-1139
    • (1993) J Mol Biol , vol.234 , pp. 1131-1139
    • Stillman, T.J.1    Baker, P.J.2    Britton, K.L.3    Rice, D.W.4
  • 87
    • 50449113127 scopus 로고
    • Crystallization of L-glutamic acid dehydrogenase from liver
    • 1:CAS:528:DyaG38XovVGn
    • Strecker HJ (1951) Crystallization of L-glutamic acid dehydrogenase from liver. Arch Biochem Biophys 32:448-449
    • (1951) Arch Biochem Biophys , vol.32 , pp. 448-449
    • Strecker, H.J.1
  • 88
    • 0026101712 scopus 로고
    • Thermostable phenylalanine dehydrogenase of Thermoactinomyces intermedius: Cloning, expression, and sequencing of its gene
    • 1:CAS:528:DyaK3MXltVOht7Y%3D
    • Takada H, Yoshimura T, Ohshima T, Esaki N, Soda K (1991) Thermostable phenylalanine dehydrogenase of Thermoactinomyces intermedius: cloning, expression, and sequencing of its gene. J Biochem 109:371-376
    • (1991) J Biochem , vol.109 , pp. 371-376
    • Takada, H.1    Yoshimura, T.2    Ohshima, T.3    Esaki, N.4    Soda, K.5
  • 89
    • 79957613599 scopus 로고    scopus 로고
    • doi: 10.1093/molbev/msr121
    • Tamura K, Peterson D, Stecher G, Nei M, Kumar S (2011) MEGA: Molecular evolutionary genetic analysis using maximum likelihood, evolutionary distance and maximum parsimony method. Mol Biol Evol. doi: 10.1093/molbev/msr121
  • 90
    • 0001005516 scopus 로고
    • NAD biosynthesis and recycling
    • F.C. Neidhart J.L. Ingraham K.B. Low B. Magasanik M. Schaechter H.E. Umbarger (eds). American Society for Microbiology Washington
    • Tritz GJ (1987) NAD biosynthesis and recycling. In: Neidhart FC, Ingraham JL, Low KB, Magasanik B, Schaechter M, Umbarger HE (eds) In Escherichia coli and Salmonella typhimurium: cellular and molecular biology. American Society for Microbiology, Washington, pp 557-563
    • (1987) In Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , pp. 557-563
    • Tritz, G.J.1
  • 91
    • 0030808441 scopus 로고    scopus 로고
    • Analysis of the quaternary structure, substrate specificity, and catalytic mechanism of valine dehydrogenase
    • DOI 10.1074/jbc.272.40.25105
    • Turnbull AP, Baker PJ, Rice DW (1997) Analysis of the quaternary structure, substrate specificity, and catalytic mechanism of valine dehydrogenase. J Biol Chem 272:25105-25111 (Pubitemid 27415693)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.40 , pp. 25105-25111
    • Turnbull, A.P.1    Baker, P.J.2    Rice, D.W.3
  • 95
    • 0033596724 scopus 로고    scopus 로고
    • Phenylalanine dehydrogenase from Rhodococcus sp. M4: High-resolution X-ray analyses of inhibitory ternary complexes reveal key features in the oxidative deamination mechanism
    • 1:CAS:528:DyaK1MXntlajsA%3D%3D
    • Vanhooke JL, Thoden JB, Brunhuber NM, Blanchard JS, Holden HM (1999) Phenylalanine dehydrogenase from Rhodococcus sp. M4: high-resolution X-ray analyses of inhibitory ternary complexes reveal key features in the oxidative deamination mechanism. Biochemistry 38:2326-2339
    • (1999) Biochemistry , vol.38 , pp. 2326-2339
    • Vanhooke, J.L.1    Thoden, J.B.2    Brunhuber, N.M.3    Blanchard, J.S.4    Holden, H.M.5
  • 96
    • 26444497490 scopus 로고    scopus 로고
    • Increased conformational and thermal stability properties for phenylalanine dehydrogenase by chemical glycosidation with end-group activated dextran
    • DOI 10.1007/s10529-005-3225-4
    • Villalonga R, Tachibana S, Perez Y, Asano Y (2005) Increased conformational and thermal stability properties for phenylalanine dehydrogenase by chemical glycosidation with end-group activated dextran. Biotechnol Lett 27:1311-1317 (Pubitemid 41428182)
    • (2005) Biotechnology Letters , vol.27 , Issue.17 , pp. 1311-1317
    • Villalonga, R.1    Tachibana, S.2    Perez, Y.3    Asano, Y.4
  • 97
    • 0031213672 scopus 로고    scopus 로고
    • Spectrophotometric assay of D-aspartate and D-glutamate using D- aspartate oxidase with malate dehydrogenase and glutamate dehydrogenase
    • DOI 10.1006/abio.1997.2230
    • Wakayama M, Takashima K, Tau Y, Nakashima S, Sakai K, Moriguchi M (1997) Spectrophotometric assay of D-aspartate and D-glutamate using D-aspartate oxidase with malate dehydrogenase and glutamate dehydrogenase. Anal Biochem 250:252-253 (Pubitemid 27319104)
    • (1997) Analytical Biochemistry , vol.250 , Issue.2 , pp. 252-253
    • Wakayama, M.1    Takashima, K.2    Tau, Y.3    Nakashima, S.4    Sakai, K.5    Moriguchi, M.6
  • 98
    • 19444372583 scopus 로고    scopus 로고
    • The crystal structure of Plasmodium falciparum glutamate dehydrogenase, a putative target for novel antimalarial drugs
    • DOI 10.1016/j.jmb.2005.03.077, PII S0022283605003797
    • Werner C, Stubbs MT, Krauth-Siegel RL, Klebe G (2005) The crystal structure of Plasmodium falciparum glutamate dehydrogenase, a putative target for novel antimalarial drugs. J Mol Biol 349:597-607 (Pubitemid 40724568)
    • (2005) Journal of Molecular Biology , vol.349 , Issue.3 , pp. 597-607
    • Werner, C.1    Stubbs, M.T.2    Krauth-Siegel, R.L.3    Klebe, G.4
  • 99
    • 0002903681 scopus 로고
    • Microassay system for newborn screening for phenylketonuria, maple syrup urine disease, homocystinuria, histidinemia and galactosemia with use of a fluorometric microplate reader
    • 1:CAS:528:DyaK38XmtVyhtrY%3D
    • Yamaguchi A, Mizushima Y, Fukushi M, Shimizu Y, Kikuchi Y, Takasugi N (1992) Microassay system for newborn screening for phenylketonuria, maple syrup urine disease, homocystinuria, histidinemia and galactosemia with use of a fluorometric microplate reader. Screening 1:49-62
    • (1992) Screening , vol.1 , pp. 49-62
    • Yamaguchi, A.1    Mizushima, Y.2    Fukushi, M.3    Shimizu, Y.4    Kikuchi, Y.5    Takasugi, N.6
  • 100
  • 102
    • 33745218027 scopus 로고    scopus 로고
    • The first archaeal L-aspartate dehydrogenase from the hyperthermophile Archaeoglobus fulgidus: Gene cloning and enzymological characterization
    • 1:CAS:528:DC%2BD28XmtVOjtLw%3D
    • Yoneda K, Kawakami R, Tagashira Y, Sakuraba H, Goda S, Ohshima T (2006) The first archaeal L-aspartate dehydrogenase from the hyperthermophile Archaeoglobus fulgidus: gene cloning and enzymological characterization. Biochim Biophys Acta 1764:1087-1093
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 1087-1093
    • Yoneda, K.1    Kawakami, R.2    Tagashira, Y.3    Sakuraba, H.4    Goda, S.5    Ohshima, T.6
  • 103
    • 34547798477 scopus 로고    scopus 로고
    • Crystal structure of archaeal highly thermostable L-aspartate dehydrogenase/NAD/citrate ternary complex
    • DOI 10.1111/j.1742-4658.2007.05961.x
    • Yoneda K, Sakuraba H, Tsuge H, Katunuma N, Ohshima T (2007) Crystal structure of archaeal highly thermostable L-aspartate dehydrogenase/NAD/citrate ternary complex. FEBS J 274:4315-4325 (Pubitemid 47228650)
    • (2007) FEBS Journal , vol.274 , Issue.16 , pp. 4315-4325
    • Yoneda, K.1    Sakuraba, H.2    Tsuge, H.3    Katunuma, N.4    Ohshima, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.