메뉴 건너뛰기




Volumn 3, Issue 1, 2014, Pages 13-20

Development of an NADPH-dependent Homophenylalanine dehydrogenase by protein engineering

Author keywords

Glutamate dehydrogenase; L homophenylalanine; Protein engineering; Reductive amination; Synthetic biology

Indexed keywords

2 OXOGLUTARIC ACID; AMINOTRANSFERASE; GLUTAMATE DEHYDROGENASE; OXIDOREDUCTASE; PHENYLPYRUVIC ACID; SULFITE REDUCTASE (NADPH); 2-AMINO-4-PHENYLBUTYRIC ACID; 2-OXO-4-PHENYL-3-BUTYNOATE; ALKYNE; ALPHA-KETOGLUTARIC ACID; AMINOBUTYRIC ACID DERIVATIVE; BUTYRIC ACID DERIVATIVE; GLUTAMATE DEHYDROGENASE (NADP); NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PHENYLALANINE DEHYDROGENASE (NAD);

EID: 84902657433     PISSN: None     EISSN: 21615063     Source Type: Journal    
DOI: 10.1021/sb400093x     Document Type: Article
Times cited : (25)

References (31)
  • 3
    • 16344393026 scopus 로고    scopus 로고
    • Asymmetrical synthesis of L-homophenylalanine using engineered Escherichia coli aspartate aminotransferase
    • Lo, H. H., Hsu, S. K., Lin, W. D., Chan, N. L., and Hsu, W. H. (2005) Asymmetrical synthesis of L-homophenylalanine using engineered Escherichia coli aspartate aminotransferase. Biotechnol. Prog. 21, 411-415.
    • (2005) Biotechnol. Prog. , vol.21 , pp. 411-415
    • Lo, H.H.1    Hsu, S.K.2    Lin, W.D.3    Chan, N.L.4    Hsu, W.H.5
  • 4
    • 41549085495 scopus 로고    scopus 로고
    • A novel hydantoinase process using recombinant Escherichia coli cells with dihydropyrimidinase and L-N-carbamoylase activities as biocatalyst for the production of L-homophenylalanine
    • Kao, C. H., Lo, H. H., Hsu, S. K., and Hsu, W. H. (2008) A novel hydantoinase process using recombinant Escherichia coli cells with dihydropyrimidinase and L-N-carbamoylase activities as biocatalyst for the production of L-homophenylalanine. J. Biotechnol. 134, 231-239.
    • (2008) J. Biotechnol. , vol.134 , pp. 231-239
    • Kao, C.H.1    Lo, H.H.2    Hsu, S.K.3    Hsu, W.H.4
  • 5
    • 84876161680 scopus 로고    scopus 로고
    • Identification of homophenylalanine biosynthetic genes from the cyanobacterium Nostoc punctiforme PCC73102 and application to its microbial production by Escherichia coli
    • Koketsu, K., Mitsuhashi, S., and Tabata, K. (2013) Identification of homophenylalanine biosynthetic genes from the cyanobacterium Nostoc punctiforme PCC73102 and application to its microbial production by Escherichia coli. Appl. Environ. Microbiol. 79, 2201-2208.
    • (2013) Appl. Environ. Microbiol. , vol.79 , pp. 2201-2208
    • Koketsu, K.1    Mitsuhashi, S.2    Tabata, K.3
  • 6
    • 60849102424 scopus 로고    scopus 로고
    • Sustainable biocatalytic synthesis of L-homophenylalanine as pharmaceutical drug precursor
    • Ahmad, A. L., Oh, P. C., and Abd Shukor, S. R. (2009) Sustainable biocatalytic synthesis of L-homophenylalanine as pharmaceutical drug precursor. Biotechnol. Adv. 27, 286-296.
    • (2009) Biotechnol. Adv. , vol.27 , pp. 286-296
    • Ahmad, A.L.1    Oh, P.C.2    Abd Shukor, S.R.3
  • 7
    • 77950899704 scopus 로고    scopus 로고
    • Expanding metabolism for total biosynthesis of the nonnatural amino acid Lhomoalanine
    • Zhang, K., Li, H., Cho, K. M., and Liao, J. C. (2010) Expanding metabolism for total biosynthesis of the nonnatural amino acid Lhomoalanine. Proc. Natl. Acad. Sci. U.S.A. 107, 6234-6239.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 6234-6239
    • Zhang, K.1    Li, H.2    Cho, K.M.3    Liao, J.C.4
  • 8
    • 0021325176 scopus 로고
    • Isolation and characterization of a bacterium possessing L-phenylalanine dehydrogenase activity
    • Hummel, W., Weiss, N., and Kula, M.-R. (1984) Isolation and characterization of a bacterium possessing L-phenylalanine dehydrogenase activity. Arch. Microbiol. 137, 47-52.
    • (1984) Arch. Microbiol. , vol.137 , pp. 47-52
    • Hummel, W.1    Weiss, N.2    Kula, M.-R.3
  • 9
    • 0023664631 scopus 로고
    • Novel phenylalanine dehydrogenases from Sporosarcina ureae and Bacillus sphaericus. Purification and characterization
    • Asano, Y., Nakazawa, A., and Endo, K. (1987) 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
  • 10
    • 0028292390 scopus 로고
    • Cloning, sequencing, and expression of Rhodococcus L-phenylalanine dehydrogenase. Sequence comparisons to amino-acid dehydrogenases
    • Brunhuber, N. M., Banerjee, A., Jacobs, W. R., Jr., and Blanchard, J. S. (1994) Cloning, sequencing, and expression of Rhodococcus L-phenylalanine dehydrogenase. Sequence comparisons to amino-acid dehydrogenases. J. Biol. Chem. 269, 16203-16211.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16203-16211
    • Brunhuber, N.M.1    Banerjee, A.2    Jacobs Jr., W.R.3    Blanchard, J.S.4
  • 11
    • 0024285821 scopus 로고
    • Gene cloning and sequence determination of leucine dehydrogenase from Bacillus stearothermophilus and structural comparison with other NAD(P)+-dependent dehydrogenases
    • Nagata, S., Tanizawa, K., Esaki, N., Sakamoto, Y., Ohshima, T., Tanaka, H., and Soda, K. (1988) Gene cloning and sequence determination of leucine dehydrogenase from Bacillus stearothermophilus and structural comparison with other NAD(P)+-dependent dehydrogenases. Biochemistry 27, 9056-9062.
    • (1988) Biochemistry , vol.27 , pp. 9056-9062
    • Nagata, S.1    Tanizawa, K.2    Esaki, N.3    Sakamoto, Y.4    Ohshima, T.5    Tanaka, H.6    Soda, K.7
  • 12
    • 84863594395 scopus 로고    scopus 로고
    • Control of glutamate homeostasis in Bacillus subtilis: A complex interplay between ammonium assimilation, glutamate biosynthesis and degradation
    • Gunka, K., and Commichau, F. M. (2012) Control of glutamate homeostasis in Bacillus subtilis: A complex interplay between ammonium assimilation, glutamate biosynthesis and degradation. Mol. Microbiol. 85, 213-224.
    • (2012) Mol. Microbiol. , vol.85 , pp. 213-224
    • Gunka, K.1    Commichau, F.M.2
  • 13
    • 0024688380 scopus 로고
    • Purification and properties of L-alanine dehydrogenase of the phototrophic bacterium Rhodobacter capsulatus E1F1
    • Caballero, F. J., Cardenas, J., and Castillo, F. (1989) Purification and properties of L-alanine dehydrogenase of the phototrophic bacterium Rhodobacter capsulatus E1F1. J. Bacteriol. 171, 3205-3210.
    • (1989) J. Bacteriol. , vol.171 , pp. 3205-3210
    • Caballero, F.J.1    Cardenas, J.2    Castillo, F.3
  • 14
    • 0028129875 scopus 로고
    • Why does Escherichia coli have two primary pathways for synthesis of glutamate?
    • Helling, R. B. (1994) Why does Escherichia coli have two primary pathways for synthesis of glutamate? J. Bacteriol. 176, 4664-4668.
    • (1994) J Bacteriol. , vol.176 , pp. 4664-4668
    • Helling, R.B.1
  • 17
    • 33845964503 scopus 로고    scopus 로고
    • Efficient regeneration of NADPH using an engineered phosphite dehydrogenase
    • Johannes, T. W., Woodyer, R. D., and Zhao, H. (2007) Efficient regeneration of NADPH using an engineered phosphite dehydrogenase. Biotechnol. Bioeng. 96, 18-26.
    • (2007) Biotechnol. Bioeng. , vol.96 , pp. 18-26
    • Johannes, T.W.1    Woodyer, R.D.2    Zhao, H.3
  • 18
    • 0026857665 scopus 로고
    • NADPH regeneration by glucose dehydrogenase from Gluconobacter scleroides for L-leucovorin synthesis
    • Eguchi, T., Kuge, Y., Inoue, K., Yoshikawa, N., Mochida, K., and Uwajima, T. (1992) NADPH regeneration by glucose dehydrogenase from Gluconobacter scleroides for L-leucovorin synthesis. Biosci. Biotechnol. Biochem. 56, 701-703.
    • (1992) Biosci. Biotechnol. Biochem. , vol.56 , pp. 701-703
    • Eguchi, T.1    Kuge, Y.2    Inoue, K.3    Yoshikawa, N.4    Mochida, K.5    Uwajima, T.6
  • 19
    • 84856021987 scopus 로고    scopus 로고
    • Combinatorial reshaping of the Candida antarctica lipase A substrate pocket for enantioselectivity using an extremely condensed library
    • Sandstrom, A. G., Wikmark, Y., Engstrom, K., Nyhlen, J., and Backvall, J. E. (2012) Combinatorial reshaping of the Candida antarctica lipase A substrate pocket for enantioselectivity using an extremely condensed library. Proc. Natl. Acad. Sci. U.S.A. 109, 78-83.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 78-83
    • Sandstrom, A.G.1    Wikmark, Y.2    Engstrom, K.3    Nyhlen, J.4    Backvall, J.E.5
  • 20
    • 0027769953 scopus 로고
    • Conformational flexibility in glutamate dehydrogenase. Role of water in substrate recognition and catalysis
    • Stillman, T. J., Baker, P. J., Britton, K. L., and Rice, D. W. (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
  • 21
    • 0029111444 scopus 로고
    • The use of natural and unnatural amino acid substrates to define the substrate specificity differences of Escherichia coli aspartate and tyrosine aminotransferases
    • Onuffer, J. J., Ton, B. T., Klement, I., and Kirsch, J. F. (1995) The use of natural and unnatural amino acid substrates to define the substrate specificity differences of Escherichia coli aspartate and tyrosine aminotransferases. Protein Sci. 4, 1743-1749.
    • (1995) Protein Sci. , vol.4 , pp. 1743-1749
    • Onuffer, J.J.1    Ton, B.T.2    Klement, I.3    Kirsch, J.F.4
  • 22
    • 0031731648 scopus 로고    scopus 로고
    • Novel biosynthetic approaches to the production of unnatural amino acids using transaminases
    • Taylor, P. P., Pantaleone, D. P., Senkpeil, R. F., and Fotheringham, I. G. (1998) Novel biosynthetic approaches to the production of unnatural amino acids using transaminases. Trends Biotechnol. 16, 412-418.
    • (1998) Trends Biotechnol. , vol.16 , pp. 412-418
    • Taylor, P.P.1    Pantaleone, D.P.2    Senkpeil, R.F.3    Fotheringham, I.G.4
  • 23
    • 0026101712 scopus 로고
    • Thermostable phenylalanine dehydrogenase of Thermoactinomyces intermedius: Cloning, expression, and sequencing of its gene
    • Takada, H., Yoshimura, T., Ohshima, T., Esaki, N., and 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
  • 24
    • 79955611425 scopus 로고    scopus 로고
    • Driving forces enable high-titer anaerobic 1-butanol synthesis in Escherichia coli
    • Shen, C. R., Lan, E. I., Dekishima, Y., Baez, A., Cho, K. M., and Liao, J. C. (2011) Driving forces enable high-titer anaerobic 1-butanol synthesis in Escherichia coli. Appl. Environ. Microbiol. 77, 2905-2915.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 2905-2915
    • Shen, C.R.1    Lan, E.I.2    Dekishima, Y.3    Baez, A.4    Cho, K.M.5    Liao, J.C.6
  • 25
    • 79955164750 scopus 로고    scopus 로고
    • Engineered ketol-acid reductoisomerase and alcohol dehydrogenase enable anaerobic 2-methylpropan-1-ol production at theoretical yield in Escherichia coli
    • Bastian, S., Liu, X., Meyerowitz, J. T., Snow, C. D., Chen, M. M., and Arnold, F. H. (2011) Engineered ketol-acid reductoisomerase and alcohol dehydrogenase enable anaerobic 2-methylpropan-1-ol production at theoretical yield in Escherichia coli. Metab. Eng. 13, 345-352.
    • (2011) Metab. Eng. , vol.13 , pp. 345-352
    • Bastian, S.1    Liu, X.2    Meyerowitz, J.T.3    Snow, C.D.4    Chen, M.M.5    Arnold, F.H.6
  • 26
    • 0017397091 scopus 로고
    • Charges of nicotinamide adenine nucleotides and adenylate energy charge as regulatory parameters of the metabolism in Escherichia coli
    • Andersen, K. B., and von Meyenburg, K. (1977) Charges of nicotinamide adenine nucleotides and adenylate energy charge as regulatory parameters of the metabolism in Escherichia coli. J. Biol. Chem. 252, 4151-4156.
    • (1977) J. Biol. Chem. , vol.252 , pp. 4151-4156
    • Andersen, K.B.1    Von Meyenburg, K.2
  • 27
    • 0027755179 scopus 로고
    • Evolution of substrate diversity in the superfamily of amino acid dehydrogenases. Prospects for rational chiral synthesis
    • Britton, K. L., Baker, P. J., Engel, P. C., Rice, D. W., and Stillman, T. J. (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
  • 28
    • 0037167635 scopus 로고    scopus 로고
    • Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its discrimination between phenylalanine and tyrosine substrates
    • Seah, S. Y., Britton, K. L., Rice, D. W., Asano, Y., and Engel, P. C. (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.1    Britton, K.L.2    Rice, D.W.3    Asano, Y.4    Engel, P.C.5
  • 29
    • 0034622509 scopus 로고    scopus 로고
    • Rhodococcus L-phenylalanine dehydrogenase: Kinetics, mechanism, and structural basis for catalytic specificity
    • Brunhuber, N. M., Thoden, J. B., Blanchard, J. S., and Vanhooke, J. L. (2000) Rhodococcus L-phenylalanine dehydrogenase: kinetics, mechanism, and structural basis for catalytic specificity. Biochemistry 39, 9174-9187.
    • (2000) Biochemistry , vol.39 , pp. 9174-9187
    • Brunhuber, N.M.1    Thoden, J.B.2    Blanchard, J.S.3    Vanhooke, J.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.