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Volumn 12, Issue 3, 1996, Pages 247-250

Hydrolysis of di-substituted hydantoins, by an enzyme preparation from lentil (Lens esculenta) seeds, for the synthesis of α,α-dialkylated amino acids with linear and cyclic substituents

Author keywords

Di substituted amino acids; Di substituted hydantoins; Lens esculenta

Indexed keywords

LENS CULINARIS;

EID: 17544370696     PISSN: 09593993     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF00360922     Document Type: Article
Times cited : (7)

References (28)
  • 2
    • 84981834366 scopus 로고
    • Herstellung von α-Aminosäureestern durch Alkoholyse der Methylesler
    • Brenner, M. & Huber, W. 1953 Herstellung von α-Aminosäureestern durch Alkoholyse der Methylesler. Helvetica Chimica Acta 36, 1109-1115.
    • (1953) Helvetica Chimica Acta , vol.36 , pp. 1109-1115
    • Brenner, M.1    Huber, W.2
  • 3
    • 0016811750 scopus 로고
    • Substrate and steric specificity of hydropyrimidine hydrase
    • Cecere, F., Galli, G. & Morisi, F. 1975 Substrate and steric specificity of hydropyrimidine hydrase. FEBS Letters 57, 192-194.
    • (1975) FEBS Letters , vol.57 , pp. 192-194
    • Cecere, F.1    Galli, G.2    Morisi, F.3
  • 4
    • 0028816066 scopus 로고
    • β-Turn conformations in crystal structures of model peptides containing α,α-di-n-propylglycine and α,α-di-n-butylglycine
    • Crisma, M., Valle, G., Toniolo, C., Prasad, S., Balaji Rao, R. & Balaram, P. 1995 β-Turn conformations in crystal structures of model peptides containing α,α-di-n-propylglycine and α,α-di-n-butylglycine. Biopolymers 35, 1-9.
    • (1995) Biopolymers , vol.35 , pp. 1-9
    • Crisma, M.1    Valle, G.2    Toniolo, C.3    Prasad, S.4    Balaji Rao, R.5    Balaram, P.6
  • 5
    • 0000685462 scopus 로고
    • The partial purification and properties of animal and plant hydantoinases
    • Eadie, G.S., Bernheim, F. & Bernheim, M.L.C. 1949 The partial purification and properties of animal and plant hydantoinases. Journal of Biological Chemistry 181, 449-458.
    • (1949) Journal of Biological Chemistry , vol.181 , pp. 449-458
    • Eadie, G.S.1    Bernheim, F.2    Bernheim, M.L.C.3
  • 7
    • 33947442725 scopus 로고
    • Identification of carbonyl compounds through conversion into hydantoins
    • Henze, H.R. & Speer, R.J. 1942 Identification of carbonyl compounds through conversion into hydantoins. Journal of the American Chemical Society 64, 522-523.
    • (1942) Journal of the American Chemical Society , vol.64 , pp. 522-523
    • Henze, H.R.1    Speer, R.J.2
  • 8
    • 0025336463 scopus 로고
    • Emerging approaches in the molecular design of receptor-selective peptide ligands: Conformational, topological and dynamic considerations
    • Hruby, V.J., Al-Obeidi, F & Kazmierski, W.M. 1990 Emerging approaches in the molecular design of receptor-selective peptide ligands: conformational, topological and dynamic considerations. Biochemical Journal 268, 249-262
    • (1990) Biochemical Journal , vol.268 , pp. 249-262
    • Hruby, V.J.1    Al-Obeidi, F.2    Kazmierski, W.M.3
  • 9
    • 0000831186 scopus 로고
    • Microbial conversion of DL-5-substituted hydantoins to the corresponding L-amino acids by Pseudomonas sp. strain NS671
    • Ishikawa, T., Watabe, K., Mukohara, Y., Kobayashi, S. & Nakamura, H. 1993 Microbial conversion of DL-5-substituted hydantoins to the corresponding L-amino acids by Pseudomonas sp. strain NS671. Bioscience, Biotechnology and Biochemistry 57, 982-986.
    • (1993) Bioscience, Biotechnology and Biochemistry , vol.57 , pp. 982-986
    • Ishikawa, T.1    Watabe, K.2    Mukohara, Y.3    Kobayashi, S.4    Nakamura, H.5
  • 11
    • 0000714772 scopus 로고
    • Enzymes in organic synthesis
    • Jones, J.B. 1986 Enzymes in organic synthesis. Tetrahedron 42, 3351-3403
    • (1986) Tetrahedron , vol.42 , pp. 3351-3403
    • Jones, J.B.1
  • 12
    • 0028073648 scopus 로고
    • Nonstandard amino acids in conformational design of peptides. Helical structure in crystals of 5-10 residue peptides containing dipropylglycine and dibutylglycine
    • Karle, I.L., Balaji Rao, R., Prasad, S., Kaul, R. & Balram, P. 1994 Nonstandard amino acids in conformational design of peptides. Helical structure in crystals of 5-10 residue peptides containing dipropylglycine and dibutylglycine. Journal of the American Chemical Society 116, 10355-10361.
    • (1994) Journal of the American Chemical Society , vol.116 , pp. 10355-10361
    • Karle, I.L.1    Balaji Rao, R.2    Prasad, S.3    Kaul, R.4    Balram, P.5
  • 13
    • 0000403752 scopus 로고
    • Modular design of synthetic protein mimics. Crystal structure of two seven-residue helical peptide segments linked by ε-aminocaproic acid
    • Karle, I.L., Flippen-Anderson, J.L., Sukumar, M., Uma, K. & Balram, P. 1991 Modular design of synthetic protein mimics. Crystal structure of two seven-residue helical peptide segments linked by ε-aminocaproic acid. Journal of the American Chemical Society 113, 3952-3956.
    • (1991) Journal of the American Chemical Society , vol.113 , pp. 3952-3956
    • Karle, I.L.1    Flippen-Anderson, J.L.2    Sukumar, M.3    Uma, K.4    Balram, P.5
  • 14
    • 0024094367 scopus 로고
    • Stereo-and substrate-specificity of a D-hydantoinase and a D-N-carbamyl-amino acid amidohydrolase of Arthrobacter crystallopoietes AM2
    • Möller, A., Syldatk, C., Schulze, M. & Wagner, F. 1988 Stereo-and substrate-specificity of a D-hydantoinase and a D-N-carbamyl-amino acid amidohydrolase of Arthrobacter crystallopoietes AM2. Enzyme and Microbial Technology 10, 618-625.
    • (1988) Enzyme and Microbial Technology , vol.10 , pp. 618-625
    • Möller, A.1    Syldatk, C.2    Schulze, M.3    Wagner, F.4
  • 18
    • 0028835439 scopus 로고
    • Contrasting solution conformations of peptides containing α,α-dialkylated residues with linear and cyclic side chains
    • Prasad, S., Balaji Rao, R. α Balram, P. 1995 Contrasting solution conformations of peptides containing α,α-dialkylated residues with linear and cyclic side chains. Biopolymers 35, 11-20.
    • (1995) Biopolymers , vol.35 , pp. 11-20
    • Prasad, S.1    Balaji Rao, R.2    Balram, P.3
  • 20
    • 0014164006 scopus 로고
    • Verbesserte synthese von tert.- Butyloxy-carbonyl-aminosäuren durch pH-stat-reaktion
    • Schnabel, E 1967 Verbesserte synthese von tert.- Butyloxy-carbonyl-aminosäuren durch pH-stat-reaktion. Liebigs Annalen der Chemie 702, 188-196.
    • (1967) Liebigs Annalen Der Chemie , vol.702 , pp. 188-196
    • Schnabel, E.1
  • 21
    • 77957009485 scopus 로고
    • Modification of proteins with cyanate
    • Stark, G.R. 1967 Modification of proteins with cyanate. Methods in Enzymology 11, 590-594.
    • (1967) Methods in Enzymology , vol.11 , pp. 590-594
    • Stark, G.R.1
  • 22
    • 0023121777 scopus 로고
    • Substrate- And stereospecificity, induction and metallodependence of a microbial hydantoinase
    • Syldatk, C., Cotoras, D., Dombach, G., Gro, C., Kallwa, H. & Wagner, F. 1987 Substrate- and stereospecificity, induction and metallodependence of a microbial hydantoinase. Biotechnology Letters 9, 25-30.
    • (1987) Biotechnology Letters , vol.9 , pp. 25-30
    • Syldatk, C.1    Cotoras, D.2    Dombach, G.3    Gro, C.4    Kallwa, H.5    Wagner, F.6
  • 23
    • 0002426626 scopus 로고
    • Production of optically pure D- And L-α-amino acids by bioconversion of D,L-5-monosubstituted hydantom derivatives
    • Syldatk, C., Läufer, A., Müller, R. & Höke, H. 1990 Production of optically pure D- and L-α-amino acids by bioconversion of D,L-5-monosubstituted hydantom derivatives. Advances in Biochemical Engineering/Biotechnology 41, 29-75.
    • (1990) Advances in Biochemical Engineering/Biotechnology , vol.41 , pp. 29-75
    • Syldatk, C.1    Läufer, A.2    Müller, R.3    Höke, H.4
  • 26
    • 0000053191 scopus 로고
    • The purification and properties of hydropyrimidine hydrase
    • Wallach, D.P. & Grisolla, S. 1957 The purification and properties of hydropyrimidine hydrase. Journal of Biological Chemistry 226, 277-288.
    • (1957) Journal of Biological Chemistry , vol.226 , pp. 277-288
    • Wallach, D.P.1    Grisolla, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.