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Volumn 63, Issue 12, 1999, Pages 2168-2173

Production of d-glutamate from l-glutamate with glutamate racemase and l-glutamate oxidase

Author keywords

D glutamate production; Glutamate racemase; L glutamate oxidase

Indexed keywords


EID: 0042784518     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.63.2168     Document Type: Article
Times cited : (8)

References (28)
  • 1
    • 0027482465 scopus 로고
    • Expression of glr (Murl, dga) gene encoding glutamate racemase in Escherichia coli
    • Yoshimura, T., Ashiuchi, M., Esaki, N., Kobatake, C., Choi, S. Y., and Soda, K., Expression of glr (murl, dga) gene encoding glutamate racemase in Escherichia coli0J. Biol. Chem., 268, 24242-24246 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 24242-24246
    • Yoshimura, T.1    Ashiuchi, M.2    Esaki, N.3    Kobatake, C.4    Choi, S.Y.5    Soda, K.6
  • 2
    • 0022376233 scopus 로고
    • Second lytic target of beta-lactam compounds that have a terminal D-amino acid residue
    • Tsuruoka, T., Tamura, A., Miyata, A., Takei, T., Inoue, S., and Matsuhasgi, ML, Second lytic target of beta-lactam compounds that have a terminal D-amino acid residue. Eur. J. Biochem., 151, 209-216 (1985).
    • (1985) Eur. J. Biochem. , vol.151 , pp. 209-216
    • Tsuruoka, T.1    Tamura, A.2    Miyata, A.3    Takei, T.4    Inoue, S.5    Matsuhasgi, M.L.6
  • 3
    • 0022918963 scopus 로고
    • Synthesis and biological activities of dynorphin A analogues with opioid antagonist properties
    • Gairin, J. E., Mazarguil, H., Alvinerie, P., Saint-Pierre, S., Meunier, J. C., and Cros, J., Synthesis and biological activities of dynorphin A analogues with opioid antagonist properties. J. Med. Chem., 29, 1913-1917 (1986).
    • (1986) J. Med. Chem. , vol.29 , pp. 1913-1917
    • Gairin, J.E.1    Mazarguil, H.2    Alvinerie, P.3    Saint-Pierre, S.4    Meunier, J.C.5    Cros, J.6
  • 4
    • 0008649778 scopus 로고
    • Synthesis of D-cysteine by a new pyridoxal enzyme
    • Soda, K., Synthesis of D-cysteine by a new pyridoxal enzyme. Trends in Biochem. Sci., 8, 152-153 (1983).
    • (1983) Trends in Biochem. Sci. , vol.8 , pp. 152-153
    • Soda, K.1
  • 5
    • 0030731779 scopus 로고    scopus 로고
    • Synthesis of optically active amino acids from a-keto acids with Escherichia coli cells expressing heterologous genes
    • Galkin, A., Kulakova L., Yoshimura, K., Soda, K., and Esaki, N., Synthesis of optically active amino acids from a-keto acids with Escherichia coli cells expressing heterologous genes. Applied. Environ. Microbiol., 63, 4651-4656 (1997).
    • (1997) Applied. Environ. Microbiol. , vol.63 , pp. 4651-4656
    • Galkin, A.1    Kulakova, L.2    Yoshimura, K.3    Soda, K.4    Esaki, N.5
  • 6
    • 0027903925 scopus 로고
    • The effect of amino acids and amino acid derivatives on cell proliferation
    • Szende, B., The effect of amino acids and amino acid derivatives on cell proliferation., Acta. Biomed. Ateneo. Parmense, 64, 139-145 (1993).
    • (1993) Acta. Biomed. Ateneo. Parmense , vol.64 , pp. 139-145
    • Szende, B.1
  • 7
    • 0026009655 scopus 로고
    • Biochemical and biological properties of methotrexate analogs containing D-glutamate and D-erythro, threo-4-fluoroglutamic acid
    • McGuire, J. J., Bolanowska, W. E., Coward, J. K., Sherwood, R. F., Russell, C. A., and Felschow, D. M., Biochemical and biological properties of methotrexate analogs containing D-glutamate and D-erythro, threo-4-fluoroglutamic acid. Biochem. Pharmacol., 42, 2400-2403 (1991).
    • (1991) Biochem. Pharmacol. , vol.42 , pp. 2400-2403
    • Mc Guire, J.J.1    Bolanowska, W.E.2    Coward, J.K.3    Sherwood, R.F.4    Russell, C.A.5    Felschow, D.M.6
  • 8
    • 0026102808 scopus 로고
    • Overproduction of glutamate racemase of Pediococcus pentosaceus in Escherichia coli clone cells and its purification
    • Choi, S. Y., Esaki, N., Yoshimura T., and Soda K., Overproduction of glutamate racemase of Pediococcus pentosaceus in Escherichia coli clone cells and its purification. Protein. Expr. Puri. 2, 90-93 (1991).
    • (1991) Protein. Expr. Puri. , vol.2 , pp. 90-93
    • Choi, S.Y.1    Esaki, N.2    Yoshimura, T.3    Soda, K.4
  • 9
    • 0026649716 scopus 로고
    • Reaction mechanism of glutamate racemase, a pyridoxal phosphate-in-dependent amino acid racemase
    • Choi, S. Y., Esaki, N., Yoshimura T., and Soda K., Reaction mechanism of glutamate racemase, a pyridoxal phosphate-in-dependent amino acid racemase. J. Biochem., 112, 139-142 (1992).
    • (1992) J. Biochem. , vol.112 , pp. 139-142
    • Choi, S.Y.1    Esaki, N.2    Yoshimura, T.3    Soda, K.4
  • 10
    • 0031778765 scopus 로고    scopus 로고
    • Properties of glutamate racemase from Bacillus subtilis IFO 3336 producing poly-y-glutamate
    • Ashiuchi, M., Tani, K., Soda, K., and Misono, H., Properties of glutamate racemase from Bacillus subtilis IFO 3336 producing poly-y-glutamate. J. Biochem., 123, 1156-1163 (1998).
    • (1998) J. Biochem. , vol.123 , pp. 1156-1163
    • Ashiuchi, M.1    Tani, K.2    Soda, K.3    Misono, H.4
  • 11
    • 0031859365 scopus 로고    scopus 로고
    • Characterization of the genes encoding D-amino acid transaminase and glutamate racemase, two D-glutamate biosynthetic enzymes of Bacillus sphaericus Atcc 10208
    • Fotheringham, I. G., Bledig, S. A., and Taylor, P. P., Characterization of the genes encoding D-amino acid transaminase and glutamate racemase, two D-glutamate biosynthetic enzymes of Bacillus sphaericus Atcc 10208. J. Bacteriol., 180, 4319-4323 (1998).
    • (1998) J. Bacteriol. , vol.180 , pp. 4319-4323
    • Fotheringham, I.G.1    Bledig, S.A.2    Taylor, P.P.3
  • 13
    • 0032791945 scopus 로고    scopus 로고
    • Isolation of the murl gene from Brevibacterium lactofermentum ATCC 13869 encoding D-glutamate racemase
    • Malathi, K. C., Wachi, M., and Nagai, K., Isolation of the murl gene from Brevibacterium lactofermentum ATCC 13869 encoding D-glutamate racemase. FEMS. Microbiol. Lett., 175, 193-196 (1999).
    • (1999) FEMS. Microbiol. Lett. , vol.175 , pp. 193-196
    • Malathi, K.C.1    Wachi, M.2    Nagai, K.3
  • 15
    • 85004388084 scopus 로고
    • Distribution of glutamate racemase in lactic acid bacteria and further characterization of the enzyme from
    • Nakajima, N., Tanizawa, K., Tanaka, H., and Soda, K., Distribution of glutamate racemase in lactic acid bacteria and further characterization of the enzyme from Pediococcus pentosaceus. Agric. Biol. Chem., 52, 3099-3104 (1988).
    • (1988) Pediococcus Pentosaceus. Agric. Biol. Chem. , vol.52 , pp. 3099-3104
    • Nakajima, N.1    Tanizawa, K.2    Tanaka, H.3    Soda, K.4
  • 16
    • 0028899510 scopus 로고
    • UDP-iV-acetyl-muramyl-L-alanine functions as an activator in the regulation of the Escherichia coli glutamate racemase activity
    • Ho, H.-T., Falk, P. J., Ervin, K. M., Krishnan, B. S., Discotto, L. F., Dougherty, T. J., and Pucci, M. J., UDP-iV-acetyl-muramyl-L-alanine functions as an activator in the regulation of the Escherichia coli glutamate racemase activity. Biochemistry., 34, 2464-2470 (1995).
    • (1995) Biochemistry. , vol.34 , pp. 2464-2470
    • Ho, H.-T.1    Falk, P.J.2    Ervin, K.M.3    Krishnan, B.S.4    Discotto, L.F.5    Dougherty, T.J.6    Pucci, M.J.7
  • 17
    • 0027263160 scopus 로고
    • Purification, cloning and cofactor independence of glutamate racemase from
    • Gallo, K. A. and Knowles, J. R., Purification, cloning and cofactor independence of glutamate racemase from Lactobacillus. Biochemistry., 32, 3981-3990 (1993).
    • (1993) Lactobacillus. Biochemistry. , vol.32 , pp. 3981-3990
    • Gallo, K.A.1    Knowles, J.R.2
  • 18
    • 84954958929 scopus 로고
    • Purification and properties of a new enzyme, L-glutamate oxidase from Streptomyces sp. X-119-6 grown on wheat bran
    • Kusakabe, H., Midorikawa, Y., Fujishima, T., Kuninaka, A., and Yoshino, H., Purification and properties of a new enzyme, L-glutamate oxidase from Streptomyces sp. X-119-6 grown on wheat bran. Agric. Biol. Chem., 47, 1323-1328, (1983).
    • (1983) Agric. Biol. Chem. , vol.47 , pp. 1323-1328
    • Kusakabe, H.1    Midorikawa, Y.2    Fujishima, T.3    Kuninaka, A.4    Yoshino, H.5
  • 19
  • 20
    • 0015136268 scopus 로고
    • Microchemical determination of organic nitrogen with Nessler reagent
    • Morrison, G. R., Microchemical determination of organic nitrogen with Nessler reagent. Anal. Biochem., 43, 527-532 (1971).
    • (1971) Anal. Biochem. , vol.43 , pp. 527-532
    • Morrison, G.R.1
  • 21
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254 (1976).
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 22
    • 0043165984 scopus 로고
    • A spectrophotometric microdetermination of keto acids with 3-methyl-2-benzothiazolone hydrazone
    • Soda, K., A spectrophotometric microdetermination of keto acids with 3-methyl-2-benzothiazolone hydrazone. J. General Microbiol., 131, 3339-3345 (1985).
    • (1985) J. General Microbiol. , vol.131 , pp. 3339-3345
    • Soda, K.1
  • 23
    • 85007849920 scopus 로고
    • Cloning, purification, and properties of a cofactor-independent glutamate racemase from Lactobacillus brevis ATCC 8287
    • Yagasaki, M., Iwata, K., Ishino, S., Azuma, M., and Ozaki, A., Cloning, purification, and properties of a cofactor-independent glutamate racemase from Lactobacillus brevis ATCC 8287. Biosci. Biotechnol. Biochem., 59, 610-614 (1995).
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 610-614
    • Yagasaki, M.1    Iwata, K.2    Ishino, S.3    Azuma, M.4    Ozaki, A.5
  • 24
    • 85007719495 scopus 로고
    • Optimal conditions for the enzymatic production of D-amino acids from the corresponding 5-substituted hydantoims
    • Yokozeki, K., Nakamori, S., Yamanaka, S., Eguchi, C., Mitsugi, K., and Yoshinaga, F., Optimal conditions for the enzymatic production of D-amino acids from the corresponding 5-substituted hydantoims. Agric. Biol. Chem., 51, 715-719 (1987).
    • (1987) Agric. Biol. Chem. , vol.51 , pp. 715-719
    • Yokozeki, K.1    Nakamori, S.2    Yamanaka, S.3    Eguchi, C.4    Mitsugi, K.5    Yoshinaga, F.6
  • 28
    • 0028837317 scopus 로고
    • Enzymatic production of D-glutamate from L-glutamate by a glutamate racemase
    • Yagasaki, M., Azuma, M., Ishino, S., and Ozaki, A., Enzymatic production of D-glutamate from L-glutamate by a glutamate racemase. J. Ferment. Bioeng., 79, 70-72 (1995).
    • (1995) J. Ferment. Bioeng. , vol.79 , pp. 70-72
    • Yagasaki, M.1    Azuma, M.2    Ishino, S.3    Ozaki, A.4


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