메뉴 건너뛰기




Volumn 75, Issue 15, 2009, Pages 5161-5166

Isolation and characterization of a novel lysine racemase from a soil metagenomic library

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTATION; D-LYSINE; ISOLATION AND CHARACTERIZATION; L-LYSINE; METAGENOME; METAGENOMIC LIBRARIES; NUCLEOTIDE SEQUENCES; RACEMASE; REVERSE REACTIONS; SPECIFIC ACTIVITY;

EID: 67651249844     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.00074-09     Document Type: Article
Times cited : (28)

References (47)
  • 1
    • 77956938344 scopus 로고
    • Amino acid racemases and epimerases
    • P. D. Boyer ed, Academic Press, New York, NY
    • Adams, E. 1972. Amino acid racemases and epimerases, p. 479-507. In P. D. Boyer (ed.), The enzymes, vol. VI. Academic Press, New York, NY.
    • (1972) The enzymes , vol.6 , pp. 479-507
    • Adams, E.1
  • 2
    • 2642618726 scopus 로고
    • Amino acid utilization in bacterial growth. II. A study of threonine-isoleucine relationships in mutants of Escherichia coli
    • Amos, H., and G. N. Cohen. 1954. Amino acid utilization in bacterial growth. II. A study of threonine-isoleucine relationships in mutants of Escherichia coli. Biochem. J. 57:338-343.
    • (1954) Biochem. J , vol.57 , pp. 338-343
    • Amos, H.1    Cohen, G.N.2
  • 3
    • 0242363179 scopus 로고    scopus 로고
    • Capture of an intermediate in the catalytic cycle of L-aspartate-β-semialdehyde dehydrogenase
    • Blanco, J., R. A. Moore, and R. E. Viola. 2003. Capture of an intermediate in the catalytic cycle of L-aspartate-β-semialdehyde dehydrogenase. Proc. Natl. Acad. Sci. USA 100:12613-12617.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12613-12617
    • Blanco, J.1    Moore, R.A.2    Viola, R.E.3
  • 5
    • 0015951164 scopus 로고    scopus 로고
    • Chang, Y. F., and E. Adams. 1974. D-Lysine catabolic pathway in Pseudomonas putida: interrelations with L-lysine catabolism. J. Bacteriol. 117:753-764.
    • Chang, Y. F., and E. Adams. 1974. D-Lysine catabolic pathway in Pseudomonas putida: interrelations with L-lysine catabolism. J. Bacteriol. 117:753-764.
  • 6
    • 0017738062 scopus 로고
    • Factors influencing growth on L-lysine by Pseudomonas. Regulation of terminal enzymes in the δ-aminovalerate pathway and growth stimulation by α-ketoglutarate
    • Chang, Y. F., and E. Adams. 1977. Factors influencing growth on L-lysine by Pseudomonas. Regulation of terminal enzymes in the δ-aminovalerate pathway and growth stimulation by α-ketoglutarate. J. Biol. Chem. 252:7987-7991.
    • (1977) J. Biol. Chem , vol.252 , pp. 7987-7991
    • Chang, Y.F.1    Adams, E.2
  • 7
    • 0017729836 scopus 로고
    • Glutarate semialdehyde dehydrogenase of Pseudomonas. Purification, properties, and relation to L-lysine catabolism
    • Chang, Y. F., and E. Adams. 1977. Glutarate semialdehyde dehydrogenase of Pseudomonas. Purification, properties, and relation to L-lysine catabolism. J. Biol. Chem. 252:7979-7986.
    • (1977) J. Biol. Chem , vol.252 , pp. 7979-7986
    • Chang, Y.F.1    Adams, E.2
  • 8
    • 0030738222 scopus 로고    scopus 로고
    • Characterization of an ATP-dependent DNA ligase encoded by Haemophilus influenzae
    • Cheng, C., and S. Shuman. 1997. Characterization of an ATP-dependent DNA ligase encoded by Haemophilus influenzae. Nucleic Acids Res. 25:1369-1374.
    • (1997) Nucleic Acids Res , vol.25 , pp. 1369-1374
    • Cheng, C.1    Shuman, S.2
  • 9
    • 0028029573 scopus 로고
    • Bacterial glutamate racemase has high sequence similarity with myoglobins and forms an equimolar inactive complex with hemin
    • Choi, S. Y., N. Esaki, M. Ashiuchi, T. Yoshimura, and K. Soda. 1994. Bacterial glutamate racemase has high sequence similarity with myoglobins and forms an equimolar inactive complex with hemin. Proc. Natl. Acad. Sci. USA 91:10144-10147.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10144-10147
    • Choi, S.Y.1    Esaki, N.2    Ashiuchi, M.3    Yoshimura, T.4    Soda, K.5
  • 11
    • 0014671457 scopus 로고    scopus 로고
    • Corrigan, J. J. 1969. D-Amino acids in animals. Science 164:142-149.
    • Corrigan, J. J. 1969. D-Amino acids in animals. Science 164:142-149.
  • 12
    • 0017361672 scopus 로고
    • Catabolism of L-lysine by Pseudomonas aeruginosa
    • Fothergill, J. C., and J. R. Guest. 1977. Catabolism of L-lysine by Pseudomonas aeruginosa. J. Gen. Microbiol. 99:139-155.
    • (1977) J. Gen. Microbiol , vol.99 , pp. 139-155
    • Fothergill, J.C.1    Guest, J.R.2
  • 13
    • 0028363968 scopus 로고    scopus 로고
    • Gessert, S. F., J. H. Kim, F. E. Nargang, and R. L. Weiss. 1994. A polyprotein precursor of two mitochondrial enzymes in Neurospora crassa. Gene structure and precursor processing. J. Biol. Chem. 269:8189-8203.
    • Gessert, S. F., J. H. Kim, F. E. Nargang, and R. L. Weiss. 1994. A polyprotein precursor of two mitochondrial enzymes in Neurospora crassa. Gene structure and precursor processing. J. Biol. Chem. 269:8189-8203.
  • 14
    • 0013846341 scopus 로고
    • Coordination of enzyme synthesis in the arginine pathway of Escherichia coli K-12
    • Glansdorf, N., and G. Sand. 1965. Coordination of enzyme synthesis in the arginine pathway of Escherichia coli K-12. Biochim. Biophys. Acta 108:308-311.
    • (1965) Biochim. Biophys. Acta , vol.108 , pp. 308-311
    • Glansdorf, N.1    Sand, G.2
  • 15
    • 0000804170 scopus 로고
    • Glutamic acid racemase from Lactobacillus arabinosus
    • Glaser, L. 1960. Glutamic acid racemase from Lactobacillus arabinosus. J. Biol. Chem. 235:2095-2098.
    • (1960) J. Biol. Chem , vol.235 , pp. 2095-2098
    • Glaser, L.1
  • 16
    • 18744380665 scopus 로고    scopus 로고
    • Mechanism of nonhomologous end-joining in mycobacteria: A low-fidelity repair system driven by Ku, ligase D and ligase C
    • Gong, C., P. Bongiorno, A. Martins, N. C. Stephanou, H. Zhu, S. Shuman, and M. S. Glickman. 2005. Mechanism of nonhomologous end-joining in mycobacteria: a low-fidelity repair system driven by Ku, ligase D and ligase C. Nat. Struct. Mol. Biol. 12:304-312.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 304-312
    • Gong, C.1    Bongiorno, P.2    Martins, A.3    Stephanou, N.C.4    Zhu, H.5    Shuman, S.6    Glickman, M.S.7
  • 17
    • 0026455011 scopus 로고
    • Determination of free amino acid enantiomers in rat brain and serum by high-performance liquid chromatography after derivatization with N-tert-butyloxycarbonyl-L-cysteine and o-phthaldialdehyde
    • Hashimoto, A., T. Nishikawa, T. Oka, K. Takahashi, and T. Hayashi. 1992. Determination of free amino acid enantiomers in rat brain and serum by high-performance liquid chromatography after derivatization with N-tert-butyloxycarbonyl-L-cysteine and o-phthaldialdehyde. J. Chromatogr. 582:41-48.
    • (1992) J. Chromatogr , vol.582 , pp. 41-48
    • Hashimoto, A.1    Nishikawa, T.2    Oka, T.3    Takahashi, K.4    Hayashi, T.5
  • 18
    • 34047162578 scopus 로고    scopus 로고
    • Stereoselective synthesis of L-homophenylalanine using the carbamoylase method with in situ racemization via N-acylamino acid racemase
    • Hsu, S. K., H. H. Lo, W. D. Lin, I. C. Chen, C. H. Kao, and W. H. Hsu. 2007. Stereoselective synthesis of L-homophenylalanine using the carbamoylase method with in situ racemization via N-acylamino acid racemase. Process Biochem. 42:856-862.
    • (2007) Process Biochem , vol.42 , pp. 856-862
    • Hsu, S.K.1    Lo, H.H.2    Lin, W.D.3    Chen, I.C.4    Kao, C.H.5    Hsu, W.H.6
  • 19
    • 67651252266 scopus 로고
    • Distribution of lysine racemase in bacteria
    • Huang, H. T., and J. W. Davisson. 1958. Distribution of lysine racemase in bacteria. J. Bacteriol. 76:495-498.
    • (1958) J. Bacteriol , vol.76 , pp. 495-498
    • Huang, H.T.1    Davisson, J.W.2
  • 20
    • 28844495683 scopus 로고
    • Metabolism of L-lysine by bacterial enzymes. V. Glutaric semialdehyde dehydrogenase
    • Ichihara, A., and E. A. Ichihara. 1961. Metabolism of L-lysine by bacterial enzymes. V. Glutaric semialdehyde dehydrogenase. J. Biochem. 49:154-157.
    • (1961) J. Biochem , vol.49 , pp. 154-157
    • Ichihara, A.1    Ichihara, E.A.2
  • 21
    • 1642453835 scopus 로고    scopus 로고
    • Mechanistic and kinetic study of the ATP-dependent DNA ligase of Neisseria meningitidis
    • Magnet, S., and J. S. Blanchard. 2004. Mechanistic and kinetic study of the ATP-dependent DNA ligase of Neisseria meningitidis. Biochemistry 43:710-717.
    • (2004) Biochemistry , vol.43 , pp. 710-717
    • Magnet, S.1    Blanchard, J.S.2
  • 22
    • 34247892342 scopus 로고    scopus 로고
    • Role of DNA repair by nonhomologous-end joining in Bacillus subtilis spore resistance to extreme dryness, mono- and polychromatic UV, and ionizing radiation
    • Moeller, R., E. Stackebrandt, G. Reitz, T. Berger, P. Rettberg, A. J. Doherty, G. Horneck, and W. L. Nicholson. 2007. Role of DNA repair by nonhomologous-end joining in Bacillus subtilis spore resistance to extreme dryness, mono- and polychromatic UV, and ionizing radiation. J. Bacteriol. 189:3306-3311.
    • (2007) J. Bacteriol , vol.189 , pp. 3306-3311
    • Moeller, R.1    Stackebrandt, E.2    Reitz, G.3    Berger, T.4    Rettberg, P.5    Doherty, A.J.6    Horneck, G.7    Nicholson, W.L.8
  • 23
    • 0029976325 scopus 로고    scopus 로고
    • Cell cycle and genetic requirements of two pathways of nonhomologous end-joining repair of double-strand breaks in Saccharomyces cerevisiae
    • Moore, J. K., and J. E. Haber. 1996. Cell cycle and genetic requirements of two pathways of nonhomologous end-joining repair of double-strand breaks in Saccharomyces cerevisiae. Mol. Cell. Biol. 16:2164-2173.
    • (1996) Mol. Cell. Biol , vol.16 , pp. 2164-2173
    • Moore, J.K.1    Haber, J.E.2
  • 24
    • 28644434572 scopus 로고    scopus 로고
    • Crystal structure of putative N-acetyl-γ-glutamyl-phosphate reductase (AK071544) from rice (Oryza sativa)
    • Nonaka, T., A. Kita, J. Miura-Ohnuma, E. Katoh, N. Inagaki, T. Yamazaki, and K. Miki. 2005. Crystal structure of putative N-acetyl-γ-glutamyl-phosphate reductase (AK071544) from rice (Oryza sativa). Proteins 61:1137-1140.
    • (2005) Proteins , vol.61 , pp. 1137-1140
    • Nonaka, T.1    Kita, A.2    Miura-Ohnuma, J.3    Katoh, E.4    Inagaki, N.5    Yamazaki, T.6    Miki, K.7
  • 25
    • 1542404801 scopus 로고    scopus 로고
    • Enantiomeric separations of amino acids with inductively coupled plasma carbon emission detection
    • Peters, H. L., A. C. Davis, and B. T. Jones. 2004. Enantiomeric separations of amino acids with inductively coupled plasma carbon emission detection. Microchem. J. 76:85-89.
    • (2004) Microchem. J , vol.76 , pp. 85-89
    • Peters, H.L.1    Davis, A.C.2    Jones, B.T.3
  • 27
    • 27144458111 scopus 로고    scopus 로고
    • Multiple and interconnected pathways for L-lysine catabolism in Pseudomonas putida KT2440
    • Revelles, O., M. Espinosa-Urgel, T. Fuhrer, U. Sauer, and J. L. Ramos. 2005. Multiple and interconnected pathways for L-lysine catabolism in Pseudomonas putida KT2440. J. Bacteriol. 187:7500-7510.
    • (2005) J. Bacteriol , vol.187 , pp. 7500-7510
    • Revelles, O.1    Espinosa-Urgel, M.2    Fuhrer, T.3    Sauer, U.4    Ramos, J.L.5
  • 28
    • 0038147361 scopus 로고    scopus 로고
    • Distribution and characteristics of D-amino acid and D-aspartate oxidases in fish tissues
    • Sarower, M. G., T. Matsui, and H. Abe. 2003. Distribution and characteristics of D-amino acid and D-aspartate oxidases in fish tissues. J. Exp. Zool. A 295:151-159.
    • (2003) J. Exp. Zool. A , vol.295 , pp. 151-159
    • Sarower, M.G.1    Matsui, T.2    Abe, H.3
  • 29
    • 84961472980 scopus 로고
    • Pyridoxal enzymes acting on D-amino acids
    • Soda, K., and N. Esaki. 1994. Pyridoxal enzymes acting on D-amino acids. Pure Appl. Chem. 66:709-714.
    • (1994) Pure Appl. Chem , vol.66 , pp. 709-714
    • Soda, K.1    Esaki, N.2
  • 30
    • 0014176829 scopus 로고
    • Occurrence of arginine racemase in bacterial extract
    • Soda, K., T. Yorifuji, and K. Ogata. 1967. Occurrence of arginine racemase in bacterial extract. Biochim. Biophys. Acta 146:606-608.
    • (1967) Biochim. Biophys. Acta , vol.146 , pp. 606-608
    • Soda, K.1    Yorifuji, T.2    Ogata, K.3
  • 31
    • 0009426531 scopus 로고
    • Studies on the enzymic reduction of amino acids. II. Purification and properties of D-proline reductase and a proline racemase from Clostridium sticklandii
    • Stadtman, T. C., and P. Elliott. 1957. Studies on the enzymic reduction of amino acids. II. Purification and properties of D-proline reductase and a proline racemase from Clostridium sticklandii. J. Biol. Chem. 228:983-997.
    • (1957) J. Biol. Chem , vol.228 , pp. 983-997
    • Stadtman, T.C.1    Elliott, P.2
  • 32
    • 34447508310 scopus 로고    scopus 로고
    • Mycobacterial nonhomologous end joining mediates mutagenic repair of chromosomal double-strand DNA breaks
    • Stephanou, N. C., F. Gao, P. Bongiorno, S. Ehrt, D. Schnappinger, S. Shuman, and M. S. Glickman. 2007. Mycobacterial nonhomologous end joining mediates mutagenic repair of chromosomal double-strand DNA breaks. J. Bacteriol. 189:5237-5246.
    • (2007) J. Bacteriol , vol.189 , pp. 5237-5246
    • Stephanou, N.C.1    Gao, F.2    Bongiorno, P.3    Ehrt, S.4    Schnappinger, D.5    Shuman, S.6    Glickman, M.S.7
  • 34
    • 0028906783 scopus 로고    scopus 로고
    • Tokuyama, S., and K. Hatano. 1995. Cloning, DNA sequencing and heterologous expression of the gene for thermostable N-acylamino acid racemase from Amycolatopsis sp. TS-1-60 in Escherichia coli. Appl. Microbiol. Biotechnol. 42:884-889.
    • Tokuyama, S., and K. Hatano. 1995. Cloning, DNA sequencing and heterologous expression of the gene for thermostable N-acylamino acid racemase from Amycolatopsis sp. TS-1-60 in Escherichia coli. Appl. Microbiol. Biotechnol. 42:884-889.
  • 35
    • 0035087095 scopus 로고    scopus 로고
    • Functional characterization of alanine racemase from Schizosaccharomyces pombe: A eucaryotic counterpart to bacterial alanine racemase
    • Uo, T., T. Yoshimura, N. Tanaka, K. Takegawa, and N. Esaki. 2001. Functional characterization of alanine racemase from Schizosaccharomyces pombe: a eucaryotic counterpart to bacterial alanine racemase. J. Bacteriol. 183:2226-2233.
    • (2001) J. Bacteriol , vol.183 , pp. 2226-2233
    • Uo, T.1    Yoshimura, T.2    Tanaka, N.3    Takegawa, K.4    Esaki, N.5
  • 36
    • 0024561489 scopus 로고
    • Enzymes in the D-alanine branch of bacterial cell wall peptidoglycan assembly
    • Walsh, C. T. 1989. Enzymes in the D-alanine branch of bacterial cell wall peptidoglycan assembly. J. Biol. Chem. 264:2393-2396.
    • (1989) J. Biol. Chem , vol.264 , pp. 2393-2396
    • Walsh, C.T.1
  • 38
    • 4143121187 scopus 로고    scopus 로고
    • Structural basis for catalytic racemization and substrate specificity of an N-acylamino acid racemase homologue from Deinococcus radiodurans
    • Wang, W. C., W. C. Chiu, S. K. Hsu, C. L. Wu, C. Y. Chen, J. S. Liu, and W. H. Hsu. 2004. Structural basis for catalytic racemization and substrate specificity of an N-acylamino acid racemase homologue from Deinococcus radiodurans. J. Mol. Biol. 342:155-169.
    • (2004) J. Mol. Biol , vol.342 , pp. 155-169
    • Wang, W.C.1    Chiu, W.C.2    Hsu, S.K.3    Wu, C.L.4    Chen, C.Y.5    Liu, J.S.6    Hsu, W.H.7
  • 39
    • 0031827219 scopus 로고    scopus 로고
    • Occurrence of free D-aspartate and aspartate racemase in the blood shell Scapharca broughtonii
    • Watanabe, T., K. Shibata, Y. Kera, and R. Yamada. 1998. Occurrence of free D-aspartate and aspartate racemase in the blood shell Scapharca broughtonii. Amino Acids 14:353-360.
    • (1998) Amino Acids , vol.14 , pp. 353-360
    • Watanabe, T.1    Shibata, K.2    Kera, Y.3    Yamada, R.4
  • 42
    • 0007669244 scopus 로고    scopus 로고
    • Wood, W. A., and I. C. Gunsalus. 1951. D-Alanine formation; a racemase in Streptococcus faecalis. J. Biol. Chem. 190:403-416.
    • Wood, W. A., and I. C. Gunsalus. 1951. D-Alanine formation; a racemase in Streptococcus faecalis. J. Biol. Chem. 190:403-416.
  • 43
    • 63249132926 scopus 로고    scopus 로고
    • Wurges, K., K. Petrusevska, S. Serci, S. Wilhelm, C. Wandrey, A. Seidel-Morgenstern, M. P. Elsner, and S. Lutz. 2009. Enzyme-assisted physiochemical enantioseparation processes. Part I. Production and characterization of a recombinant amino acid racemase. J. Mol. Catal. B 58:10-16.
    • Wurges, K., K. Petrusevska, S. Serci, S. Wilhelm, C. Wandrey, A. Seidel-Morgenstern, M. P. Elsner, and S. Lutz. 2009. Enzyme-assisted physiochemical enantioseparation processes. Part I. Production and characterization of a recombinant amino acid racemase. J. Mol. Catal. B 58:10-16.
  • 44
    • 0014233708 scopus 로고
    • Adenosine triphosphate and pyrophosphate dependent phenylalanine racemase of Bacillus brevis Nagano
    • Yamada, M., and K. Kurahashi. 1968. Adenosine triphosphate and pyrophosphate dependent phenylalanine racemase of Bacillus brevis Nagano. J. Biochem. 63:59-69.
    • (1968) J. Biochem , vol.63 , pp. 59-69
    • Yamada, M.1    Kurahashi, K.2
  • 45
    • 0041876085 scopus 로고    scopus 로고
    • Amino acid racemases: Functions and mechanisms
    • Yoshimura, T., and N. Esak. 2003. Amino acid racemases: functions and mechanisms. J. Biosci. Bioeng. 96:103-109.
    • (2003) J. Biosci. Bioeng , vol.96 , pp. 103-109
    • Yoshimura, T.1    Esak, N.2
  • 47
    • 0001754823 scopus 로고    scopus 로고
    • Zenk, M. H., and H. Scherf. 1963. D-Tryptophan in höheren Pflanzen. Biochim. Biophys. Acta 71:737-738.
    • Zenk, M. H., and H. Scherf. 1963. D-Tryptophan in höheren Pflanzen. Biochim. Biophys. Acta 71:737-738.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.