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Volumn 84, Issue 3, 1997, Pages 181-184

Efficient preparation of optically active p-trimethylsilylphenylalanine by using cell-free extract of blastobacter sp. A17p-4

Author keywords

Blastobacter sp. A17p 4; Cell free extract; Heat treatment; N carbamoyl amino acid amidohydrolase; p trimethylsilylphenylalanine; Silicon containing amino acid

Indexed keywords

BACTERIA; CATALYSIS; COMPOSITION EFFECTS; ENZYME KINETICS; ENZYMES; EXTRACTION; HEAT TREATMENT; HYDROLYSIS; OPTICAL MATERIALS; PH EFFECTS; SILICON COMPOUNDS;

EID: 0030669428     PISSN: 0922338X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0922-338X(97)82051-X     Document Type: Article
Times cited : (13)

References (18)
  • 5
    • 0001039009 scopus 로고
    • α-Amino acid synthesis (Tetrahedron Symposia-in-print)
    • O'Donnell, M. J. (ed.): α-Amino acid synthesis (Tetrahedron Symposia-in-print). Tetrahedron, 44, 5253-5614 (1988).
    • (1988) Tetrahedron , vol.44 , pp. 5253-5614
    • O'Donnell, M.J.1
  • 6
    • 0029946286 scopus 로고    scopus 로고
    • Amino acids and their derivatives as stoichiometric auxiliaries in asymmetric synthesis
    • Studer, A.: Amino acids and their derivatives as stoichiometric auxiliaries in asymmetric synthesis. Synthesis, 1996, 793-815 (1996).
    • (1996) Synthesis , vol.1996 , pp. 793-815
    • Studer, A.1
  • 8
    • 0347238085 scopus 로고
    • Organosilicon biochemistry
    • July/August
    • Tanaka, A. and Kawamoto, T.: Organosilicon biochemistry. Chim. Oggi, July/August, 63-69 (1994).
    • (1994) Chim. Oggi , pp. 63-69
    • Tanaka, A.1    Kawamoto, T.2
  • 11
    • 84951602838 scopus 로고
    • Mechanism of asymmetric production of L-aromatic amino acids from the corresponding hydantoins by Flavobacterium sp
    • Yokozeki, K., Hirose, Y., and Kubota, K.: Mechanism of asymmetric production of L-aromatic amino acids from the corresponding hydantoins by Flavobacterium sp. Agric. Biol. Chem., 51, 737-746 (1987).
    • (1987) Agric. Biol. Chem. , vol.51 , pp. 737-746
    • Yokozeki, K.1    Hirose, Y.2    Kubota, K.3
  • 12
    • 0025449545 scopus 로고
    • Production of L-tryptophan from D,L-5-indolylmethylhydantoin by resting cells of a mutant of Arthrobacter species (DSM 3747)
    • Gross, C., Syldatk, C., Mackowiak, V., and Wagner, F.: Production of L-tryptophan from D,L-5-indolylmethylhydantoin by resting cells of a mutant of Arthrobacter species (DSM 3747). J. Biotechnol., 14, 363-376 (1990).
    • (1990) J. Biotechnol. , vol.14 , pp. 363-376
    • Gross, C.1    Syldatk, C.2    Mackowiak, V.3    Wagner, F.4
  • 13
    • 0343809770 scopus 로고
    • The catalytic racemization of optically active hydantoin derivatives and of related substances as the result of tautomeric change
    • Dakin, H. D.: The catalytic racemization of optically active hydantoin derivatives and of related substances as the result of tautomeric change. Am. Chem. J., 44, 48-60 (1910).
    • (1910) Am. Chem. J. , vol.44 , pp. 48-60
    • Dakin, H.D.1
  • 14
    • 0028533605 scopus 로고
    • Thermostable N-carbamoyl-D-amino acid amidohydrolase: Screening, purification and characterization
    • Ogawa, J., Chung, M. C.-M., Hida, S., Yamada, H., and Shimizu, S.: Thermostable N-carbamoyl-D-amino acid amidohydrolase: screening, purification and characterization. J. Biotechnol., 38, 11-19 (1994).
    • (1994) J. Biotechnol. , vol.38 , pp. 11-19
    • Ogawa, J.1    Chung, M.C.-M.2    Hida, S.3    Yamada, H.4    Shimizu, S.5
  • 15
    • 84954975176 scopus 로고
    • Synthesis of N-carbamyl-D-2-thienylglycine and D-2-thienylglycine by microbial hydantoinase
    • Shimizu, S., Shimada, H., Takahashi, S., Ohashi, T., Tani, Y., and Yamada, H.: Synthesis of N-carbamyl-D-2-thienylglycine and D-2-thienylglycine by microbial hydantoinase. Agric. Biol. Chem., 44, 2233-2234 (1980).
    • (1980) Agric. Biol. Chem. , vol.44 , pp. 2233-2234
    • Shimizu, S.1    Shimada, H.2    Takahashi, S.3    Ohashi, T.4    Tani, Y.5    Yamada, H.6
  • 16
    • 0028168717 scopus 로고
    • ß-Ureidopropionase with N-carbamoyl-α-L-amino acid amidohydrolase activity from an aerobic bacterium, Pseudomonas putida IFO 12996
    • Ogawa, J. and Shimizu, S.: ß-Ureidopropionase with N-carbamoyl-α-L-amino acid amidohydrolase activity from an aerobic bacterium, Pseudomonas putida IFO 12996. Eur. J. Biochem., 223, 625-630 (1994).
    • (1994) Eur. J. Biochem. , vol.223 , pp. 625-630
    • Ogawa, J.1    Shimizu, S.2
  • 17
    • 0028805827 scopus 로고
    • Purification and characterization of N-carbamoyl-L-amino acid amidohydrolase with broad substrate specificity from Alcaligenes xylosoxidans
    • Ogawa, J., Miyake, H., and Shimizu, S.: Purification and characterization of N-carbamoyl-L-amino acid amidohydrolase with broad substrate specificity from Alcaligenes xylosoxidans. Appl. Microbiol. Biotechnol., 43, 1039-1043 (1995).
    • (1995) Appl. Microbiol. Biotechnol. , vol.43 , pp. 1039-1043
    • Ogawa, J.1    Miyake, H.2    Shimizu, S.3
  • 18
    • 0030118058 scopus 로고    scopus 로고
    • N-Carbamyl-L-amino acid amidohydrolase of Pseudomonas sp. strain NS671: Purification and some properties of the enzyme expressed in Escherichia coli
    • Ishikawa, T., Watabe, K., Mukohara, Y., and Nakamura, H.: N-Carbamyl-L-amino acid amidohydrolase of Pseudomonas sp. strain NS671: purification and some properties of the enzyme expressed in Escherichia coli. Biosci. Biotech. Biochem., 60, 612-615 (1996).
    • (1996) Biosci. Biotech. Biochem. , vol.60 , pp. 612-615
    • Ishikawa, T.1    Watabe, K.2    Mukohara, Y.3    Nakamura, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.