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Volumn 90, Issue 6, 2011, Pages 1953-1962

A novel L-aspartate dehydrogenase from the mesophilic bacterium Pseudomonas aeruginosa PAO1: Molecular characterization and application for L-aspartate production

Author keywords

Amino acid dehydrogenase; L Aspartate dehydrogenase; L Aspartate production; Mesophilic L AspDH; Pseudomonas aeruginosa; Thermostability

Indexed keywords

L-ASPARTATE DEHYDROGENASE; L-ASPARTATE PRODUCTION; MESOPHILIC; PSEUDOMONAS AERUGINOSA; THERMOSTABILITY;

EID: 79958202386     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-011-3208-4     Document Type: Article
Times cited : (14)

References (32)
  • 2
    • 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
  • 4
    • 0344258317 scopus 로고    scopus 로고
    • Enhanced conversion rate of L-phenylalanine by coupling reactions of aminotransferases and phosphoenolpyruvate carboxykinase in Escherichia coli K-12
    • DOI 10.1021/bp990044f
    • Chao YP, Lai ZJ, Chen P, Chern JT (1999) Enhanced conversion rate of L-phenylalanine by coupling reactions of aminotransferases and phosphoenolpyruvate carboxykinase in Escherichia coli K-12. Biotechnol Prog 15:453-458 (Pubitemid 29270689)
    • (1999) Biotechnology Progress , vol.15 , Issue.3 , pp. 453-458
    • Chao, Y.-P.1    Lai, Z.J.2    Chen, P.3    Chern, J.-T.4
  • 5
    • 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
  • 6
    • 0005594143 scopus 로고
    • Properties of alanine dehydrogenase and aspartase from Propionibacterium freudenreichii subsp. shermanii
    • 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
  • 7
    • 0025024177 scopus 로고
    • Synthesis of L-hydrohyvaline from keto hydroxyisovalerate using LeuDH from Bacillus species
    • 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
    • (1990) Bioorg Chem , vol.18 , 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
  • 8
    • 0025300483 scopus 로고
    • Membrane alteration is necessary but not sufficient for effective glutamate secretion in Corynebacterium glutamicum
    • Hoischen C, Kramer R (1990) Membrane alteration is necessary but not sufficient for effective glutamate secretion in Corynebacterium glutamicum. J Bacteriol 172:3409-3416 (Pubitemid 20179800)
    • (1990) Journal of Bacteriology , vol.172 , Issue.6 , pp. 3409-3416
    • Hoischen, C.1    Kramer, R.2
  • 9
    • 0031178552 scopus 로고    scopus 로고
    • Relationship between the Glutamate Production and the Activity of 2-Oxoglutarate Dehydrogenase in Brevibacterium lactofermentum
    • Kawahara Y, Takahashi-Fuke K, Shimizu E, Nakamatsu T, Nakamori S (1997) Relationship between the glutamate production and the activity of 2-oxoglutarate dehydrogenase in Brevibacterium lactofermentum. Biosci Biotechnol Biochem 61:1109-1112 (Pubitemid 127473029)
    • (1997) Bioscience, Biotechnology and Biochemistry , vol.61 , Issue.7 , pp. 1109-1112
    • Kawahara, Y.1    Takahashi-fuke, K.2    Shimizu, E.3    Nakamatsu, T.4    Nakamori, S.5
  • 10
    • 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 (2005a) 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, M..I.H.1    Kim, H.2    Ashida, H.3    Ishikawa, T.4    Shibata, H.5    Sawa, Y.6
  • 11
    • 27644547321 scopus 로고    scopus 로고
    • Molecular properties and enhancement of thermostability by random mutagenesis of glutamate dehydrogenase from Bacillus subtilis
    • Khan MI, Ito K, Kim H, Ashida H, Ishikawa T, Shibata H, Sawa Y (2005b) Molecular properties and enhancement of thermostability by random mutagenesis of glutamate dehydrogenase from Bacillus subtilis. Biosci Biotechnol Biochem 69:1861-1870
    • (2005) Biosci Biotechnol Biochem , vol.69 , pp. 1861-1870
    • Khan, M.I.1    Ito, K.2    Kim, H.3    Ashida, H.4    Ishikawa, T.5    Shibata, H.6    Sawa, Y.7
  • 12
    • 0036965818 scopus 로고    scopus 로고
    • Triggering mechanism of L-glutamate overproduction by DtsR1 in coryneform bacteria
    • Kimura E (2002) Triggering mechanism of L-glutamate overproduction by DtsR1 in coryneform bacteria. J Biosci Bioeng 94:545-551
    • (2002) J Biosci Bioeng , vol.94 , pp. 545-551
    • Kimura, E.1
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 34247593085 scopus 로고    scopus 로고
    • L-Tyrosine production by deregulated strains of Escherichia coli
    • DOI 10.1007/s00253-006-0792-9
    • Lutke-Eversloh T, Stephanopoulos G (2007) L-tyrosine production by deregulated strains of Escherichia coli. Appl Microbiol Biotechnol 75:103-110 (Pubitemid 46669219)
    • (2007) Applied Microbiology and Biotechnology , vol.75 , Issue.1 , pp. 103-110
    • Lutke-Eversloh, T.1    Stephanopoulos, G.2
  • 16
    • 85004570526 scopus 로고
    • Production of aspartic acid and enzymatic alteration in pyruvate kinase mutants of Brevibacterimu flavum
    • Mori M, Shiio I (1984) Production of aspartic acid and enzymatic alteration in pyruvate kinase mutants of Brevibacterimu flavum. Agric Biol Chem 48:1181-1197
    • (1984) Agric Biol Chem , vol.48 , pp. 1181-1197
    • Mori, M.1    Shiio, I.2
  • 18
    • 0000688302 scopus 로고
    • Production of L-phenylalanine from phenylpyruvate by Paracoccus denitrificans containing aminotransferase activity
    • Nakamiehi K, Nabe K, Nishida Y, Tosa T (1989) Production of L-phenylalanine from phenylpyruvate by Paracoccus denitrificans containing aminotransferase activity. Appl Microbiol Biotechnol 30:4
    • (1989) Appl Microbiol Biotechnol , vol.30 , pp. 4
    • Nakamiehi, K.1    Nabe, K.2    Nishida, Y.3    Tosa, T.4
  • 19
    • 34547211797 scopus 로고    scopus 로고
    • Mutations of the Corynebacterium glutamicum NCgl1221 gene, encoding a mechanosensitive channel homolog, induce L-glutamic acid production
    • DOI 10.1128/AEM.02446-06
    • Nakamura J, Hirano S, Ito H, Wachi M (2007) Mutations of the Corynebacterium glutamicum NCgl1221 gene, encoding a mechanosensitive channel homolog, induce L-glutamic acid production. Appl Environ Microbiol 73:4491-4498 (Pubitemid 47122593)
    • (2007) Applied and Environmental Microbiology , vol.73 , Issue.14 , pp. 4491-4498
    • Nakamura, J.1    Hirano, S.2    Ito, H.3    Wachi, M.4
  • 21
    • 0025617067 scopus 로고
    • Biochemistry and biotechnology of amino acid dehydrogenases
    • 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
  • 22
    • 0017897436 scopus 로고
    • Properties of crystalline leucine dehydrogenase from Bacillus sphaericus
    • Ohshima T, Misono H, Soda K (1978) Properties of crystalline leucine dehydrogenase from Bacillus sphaericus. J Biol Chem 253:5719-5725 (Pubitemid 8403706)
    • (1978) Journal of Biological Chemistry , vol.253 , Issue.16 , pp. 5719-5725
    • Ohshima, T.1    Misono, H.2    Soda, K.3
  • 23
    • 33947275439 scopus 로고    scopus 로고
    • Production of tyrosine from sucrose or glucose achieved by rapid genetic changes to phenylalanine-producing Escherichia coli strains
    • DOI 10.1007/s00253-006-0746-2
    • Olson MM, Templeton LJ, Suh W, Youderian P, Sariaslani FS, Gatenby AA, Van Dyk TK (2007) Production of tyrosine from sucrose or glucose achieved by rapid genetic changes to phenylalanine-producing Escherichia coli strains. Appl Microbiol Biotechnol 74:1031-1040 (Pubitemid 46434754)
    • (2007) Applied Microbiology and Biotechnology , vol.74 , Issue.5 , pp. 1031-1040
    • Olson, M.M.1    Templeton, L.J.2    Suh, W.3    Youderian, P.4    Sariaslani, F.S.5    Gatenby, A.A.6    Van Dyk, T.K.7
  • 24
    • 39549091527 scopus 로고    scopus 로고
    • L-tyrosine production by recombinant Escherichia coli: Fermentation optimization and recovery
    • DOI 10.1002/bit.21765
    • Patnaik R, Zolandz RR, Green DA, Kraynie DF (2008) L-tyrosine production by recombinant Escherichia coli: fermentation optimization and recovery. Biotechnol Bioeng 99:741-752 (Pubitemid 351316616)
    • (2008) Biotechnology and Bioengineering , vol.99 , Issue.4 , pp. 741-752
    • Patnaik, R.1    Zolandz, R.R.2    Green, D.A.3    Kraynie, D.F.4
  • 25
    • 0027762355 scopus 로고
    • Pressure stability of proteins
    • Silva JL, Weber G (1993) Pressure stability of proteins. Annu Rev Phys Chem 44:89-113
    • (1993) Annu Rev Phys Chem , vol.44 , pp. 89-113
    • Silva, J.L.1    Weber, G.2
  • 27
    • 0032926175 scopus 로고    scopus 로고
    • Pressure-induced thermostabilization of glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus
    • Sun MM, Tolliday N, Vetriani C, Robb FT, Clark DS (1999) Pressure-induced thermostabilization of glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus. Protein Sci 8:1056-1063 (Pubitemid 29211743)
    • (1999) Protein Science , vol.8 , Issue.5 , pp. 1056-1063
    • Sun, M.M.C.1    Tolliday, N.2    Vetriani, C.3    Robb, F.T.4    Clark, D.S.5
  • 28
    • 0020393389 scopus 로고
    • A new approach for molecular cloning in Cyanobacteria: Cloning of an Anacystis nidulans met gene using a Tn901-induced mutant
    • DOI 10.1016/0378-1119(82)90092-0
    • Tandeau de Marsac N, Borrias WE, Kuhlemeier CJ, Castets AM, van Arkel GA, van den Hondel CA (1982) A new approach for molecular cloning in cyanobacteria: cloning of an Anacystis nidulans met gene using a Tn901-induced mutant. Gene 20:111-119 (Pubitemid 13187088)
    • (1982) Gene , vol.20 , Issue.1 , pp. 111-119
    • Tandeau De, M.N.1    Borrias, W.E.2    Kuhlemeier, C.J.3
  • 30
  • 31
    • 33745218027 scopus 로고    scopus 로고
    • The first archaeal L-aspartate dehydrogenase from the hyperthermophile Archaeoglobus fulgidus: Gene cloning and enzymological characterization
    • 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
  • 32
    • 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


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