메뉴 건너뛰기




Volumn , Issue , 2007, Pages 599-606

Hydantoinases

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84892304294     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/1-4020-5377-0_34     Document Type: Chapter
Times cited : (3)

References (26)
  • 1
    • 0033960556 scopus 로고    scopus 로고
    • Optimum ratio of D-carbamoylase to D-hydantionase for maximizing D-p-hydroxyphenylglycine productivity
    • Chao, Y.P., Chiang, C.J. and Chen, P.T. (2000). Optimum ratio of D-carbamoylase to D-hydantionase for maximizing D-p-hydroxyphenylglycine productivity. Biotechnol. Lett. 22, 99-103.
    • (2000) Biotechnol. Lett. , vol.22 , pp. 99-103
    • Chao, Y.P.1    Chiang, C.J.2    Chen, P.T.3
  • 2
    • 0033806695 scopus 로고    scopus 로고
    • Overproduction of D-hydantoinase and carbamoylase in a soluble form in Escherichia coli
    • Chao, Y.P., Chiang, C.J., Lo, T.E. and Fu, H. (2000). Overproduction of D-hydantoinase and carbamoylase in a soluble form in Escherichia coli. Appl. Microbiol. Biotechnol. 54, 348-353.
    • (2000) Appl. Microbiol. Biotechnol. , vol.54 , pp. 348-353
    • Chao, Y.P.1    Chiang, C.J.2    Lo, T.E.3    Fu, H.4
  • 3
    • 0033230902 scopus 로고    scopus 로고
    • One-step production of D-p- hydroxyphenylglycine by recombinant Escherichia coli strains
    • Chao, Y.P., Fu, H., Lo, T.E., Chen, P.T. and Wang, J.J. (1999). One-step production of D-p- hydroxyphenylglycine by recombinant Escherichia coli strains. Biotechnol. Prog. 15, 1039-1045.
    • (1999) Biotechnol. Prog. , vol.15 , pp. 1039-1045
    • Chao, Y.P.1    Fu, H.2    Lo, T.E.3    Chen, P.T.4    Wang, J.J.5
  • 4
    • 0037199453 scopus 로고    scopus 로고
    • Crystal structure of D-hydnatoinase from Bacillus stearothermophilus: Insight into the stereochemistry of enantioselectivity
    • Cheon, Y.H., Kim, H.S., Han, K.H., Abendroth, J., Niefind, K., Schomburg, D., Wang, J. and Kim, Y. (2002). Crystal structure of D-hydnatoinase from Bacillus stearothermophilus: insight into the stereochemistry of enantioselectivity. Biochem. 41, 9410-9417.
    • (2002) Biochem. , vol.41 , pp. 9410-9417
    • Cheon, Y.H.1    Kim, H.S.2    Han, K.H.3    Abendroth, J.4    Niefind, K.5    Schomburg, D.6    Wang, J.7    Kim, Y.8
  • 5
    • 2942586825 scopus 로고    scopus 로고
    • Manipulation of the active site loops of D-hydnatoinase, a (β/α) 8-barrel protein, for modulation of the substrate specificity
    • Cheron, Y.H., Park, H.S., Kim, H.S., Kim, Y. and Kim, H.S. (2004). Manipulation of the active site loops of D-hydnatoinase, a (β/α) 8-barrel protein, for modulation of the substrate specificity. Biochem. 43, 7413-7420.
    • (2004) Biochem. , vol.43 , pp. 7413-7420
    • Cheron, Y.H.1    Park, H.S.2    Kim, H.S.3    Kim, Y.4    Kim, H.S.5
  • 6
    • 18144390619 scopus 로고    scopus 로고
    • Chitin-binding domain based immobilization of D-hydantoinase
    • Chern, J.T. and Chao, Y.P. (2005). Chitin-binding domain based immobilization of D-hydantoinase. J. Biotechnol. 117, 267-275.
    • (2005) J. Biotechnol. , vol.117 , pp. 267-275
    • Chern, J.T.1    Chao, Y.P.2
  • 7
    • 33745957439 scopus 로고    scopus 로고
    • A simple and effective method to prepare immobilized enzymes using reconstituted oil bodies
    • Chiang, C.J, Chen, H.C., Kuo, H.F., Chao, Y.P. and Tzen, J.T. C. (2006). A simple and effective method to prepare immobilized enzymes using reconstituted oil bodies. Enzyme Microbial. Tech. 39, 1152-1158.
    • (2006) Enzyme Microbial. Tech. , vol.39 , pp. 1152-1158
    • Chiang, C.J.1    Chen, H.C.2    Kuo, H.F.3    Chao, Y.P.4    Tzen, J.T.5
  • 8
    • 0000685462 scopus 로고
    • The partial purification and properties of animal and plant hydantionase
    • Eadie, G.S., Bernheim, F. and Bernheim, M.L.C. (1949). The partial purification and properties of animal and plant hydantionase. J. Biol. Chem. 181, 449-458.
    • (1949) J. Biol. Chem. , vol.181 , pp. 449-458
    • Eadie, G.S.C.1    Bernheim, F.2    Bernheim, M.L.C.3
  • 9
    • 0034938591 scopus 로고    scopus 로고
    • Oil bodies and their associated proteins, oleosin and caleosin
    • Frandsen, G.I., Mundy, J. and Tzen, J.T.C. (2001). Oil bodies and their associated proteins, oleosin and caleosin. Physiol. Plant. 112, 301-307.
    • (2001) Physiol. Plant. , vol.112 , pp. 301-307
    • Frandsen, G.I.1    Mundy, J.2    Tzen, J.T.C.3
  • 10
    • 0013487813 scopus 로고
    • On the metabolism of hydantoins and hydantoic acid
    • Gaebler, O.H. and Keltch, A.K. (1926). On the metabolism of hydantoins and hydantoic acid. J. Biol. Chem. 70, 763-777.
    • (1926) J. Biol. Chem. , vol.70 , pp. 763-777
    • Gaebler, O.H.1    Keltch, A.K.2
  • 11
    • 0034127684 scopus 로고    scopus 로고
    • Expression and characterization of the chitin-binding domain of chintinase A1 from Bacillus circulans WL-12
    • Hashimoto, M., Ikegami, T., Seino, S., Ohuchi, N., Fukada, H., Sugiyama, J., Shirakawa, M. and Watanabe, T. (2000). Expression and characterization of the chitin-binding domain of chintinase A1 from Bacillus circulans WL-12. J. Bacteriol. 182, 3045-3054.
    • (2000) J. Bacteriol. , vol.182 , pp. 3045-3054
    • Hashimoto, M.1    Ikegami, T.2    Seino, S.3    Ohuchi, N.4    Fukada, H.5    Sugiyama, J.6    Shirakawa, M.7    Watanabe, T.8
  • 12
    • 0038010117 scopus 로고    scopus 로고
    • Purification of industrial hydantoinase in one chromatographic step without any tag
    • Huang, C.Y., Chao, Y.P. and Yang, Y.S. (2003). Purification of industrial hydantoinase in one chromatographic step without any tag. Protein Expr. Purif. 30, 134-139.
    • (2003) Protein Expr. Purif. , vol.30 , pp. 134-139
    • Huang, C.Y.1    Chao, Y.P.2    Yang, Y.S.3
  • 13
    • 0032519719 scopus 로고    scopus 로고
    • Identification of the structural similarity in the functionally related amidohydrolase acting on the cyclic amide ring
    • Kim, G.J. and Kim, H.S. (1998). Identification of the structural similarity in the functionally related amidohydrolase acting on the cyclic amide ring. Biochem. J. 330, 295-302.
    • (1998) Biochem. J. , vol.330 , pp. 295-302
    • Kim, G.J.1    Kim, H.S.2
  • 14
    • 0034114092 scopus 로고    scopus 로고
    • Construction and evaluation of a novel bifunctional N-carbamylase-D- hydantoinase fusion enzyme
    • Kim, G.J. Lee, D.E. and Kim, H.S. (2000). Construction and evaluation of a novel bifunctional N-carbamylase-D-hydantoinase fusion enzyme. Appl. Environ. Microbiol. 66, 2133-2138.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 2133-2138
    • Kim, G.J.1    Lee, D.E.2    Kim, H.S.3
  • 15
    • 0034059496 scopus 로고    scopus 로고
    • Inverting enantioselectivity by directed evolution of hydnatoinase for improved production of L-methionine
    • May, O., Nguyen, P.T. and Arnold, F.H. (2000). Inverting enantioselectivity by directed evolution of hydnatoinase for improved production of L-methionine. Nat. Biotechnol. 18, 317-320.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 317-320
    • May, O.1    Nguyen, P.T.2    Arnold, F.H.3
  • 17
    • 0019781513 scopus 로고
    • Microbial transformation of racemic hydantoins to D-amino acids, Biotechnol
    • Olivieri, R., Fascetti, E., Angellini, L. and Degen, L. (1981). Microbial transformation of racemic hydantoins to D-amino acids, Biotechnol. Bioeng. 23, 2173-2183.
    • (1981) Bioeng. , vol.23 , pp. 2173-2183
    • Olivieri, R.1    Fascetti, E.2    Angellini, L.3    Degen, L.4
  • 18
    • 0036669691 scopus 로고    scopus 로고
    • Industrial microbial enzymes: Their discovery by screening and use in large-scale production of useful chemicals in Japan
    • Owgawa, J. and Shimizu, S. (2002). Industrial microbial enzymes: their discovery by screening and use in large-scale production of useful chemicals in Japan. Curr. Opin. Biotechnol. 13, 367-75.
    • (2002) Curr. Opin. Biotechnol. , vol.13 , pp. 367-375
    • Owgawa, J.1    Shimizu, S.2
  • 19
    • 0033974090 scopus 로고    scopus 로고
    • Purification of recombinant hydantoinase and L-N-carbamoylase from Arthrobacter surescens expressed in Escherichia coli: Comparison of wild-type and genetically modified proteins
    • Pietzsch, M., Wiese, A. Ragnitz, K, Wilms, B., Altenbuchner, J., Mattes, R. and Syldatk, C. (2000). Purification of recombinant hydantoinase and L-N-carbamoylase from Arthrobacter surescens expressed in Escherichia coli: comparison of wild-type and genetically modified proteins. J. Chromatogr. B Biomed. Sci. Appl. 737, 179-186.
    • (2000) J. Chromatogr. B Biomed. Sci. Appl. , vol.737 , pp. 179-186
    • Pietzsch, M.1    Wiese, A.2    Ragnitz, K.3    Wilms, B.4    Altenbuchner, J.5    Mattes, R.6    Syldatk, C.7
  • 20
    • 0035912842 scopus 로고    scopus 로고
    • Molecular structure of dihydroorotase: A paradigm for catalysis through the use of a binuclear metal center
    • Thoden, J.B., Phillips, G.N. jr., Neal, T.M., Raushel, F.M. and Holden, H.M. (2001). Molecular structure of dihydroorotase: a paradigm for catalysis through the use of a binuclear metal center. Biochem. 40, 6989-6997.
    • (2001) Biochem. , vol.40 , pp. 6989-6997
    • Thoden, J.B.1    Phillips Jr., G.N.2    Neal, T.M.3    Raushel, F.M.4    Holden, H.M.5
  • 21
    • 0017122896 scopus 로고
    • Degradation of purines and pyrimidines by micro-organisms
    • Vogels, G.D. and Van der Drift, C. (1976). Degradation of purines and pyrimidines by micro-organisms. Bacteriol. Rev. 40, 403-68.
    • (1976) Bacteriol. Rev. , vol.40 , pp. 403-468
    • Vogels, G.D.1    Van Der Drift, C.2
  • 22
    • 33644858250 scopus 로고    scopus 로고
    • Immobilization of cells with surface-displayed chitin-binding domain
    • Wang, J.Y. and Chao, Y.P. (2006). Immobilization of cells with surface-displayed chitin-binding domain. Appl. Environ. Microbiol. 72, 927-931.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 927-931
    • Wang, J.Y.1    Chao, Y.P.2
  • 23
    • 0035831306 scopus 로고    scopus 로고
    • Development of an Escherichia coli whole cell biocatalyst for the production of L-amino acids
    • Wilms, B., Wiese, A., Syldatk, C., Mattes, R. and Altenbuchner, J. (2001). Development of an Escherichia coli whole cell biocatalyst for the production of L-amino acids. J. Biotechnol. 86, 19-30.
    • (2001) J. Biotechnol. , vol.86 , pp. 19-30
    • Wilms, B.1    Wiese, A.2    Syldatk, C.3    Mattes, R.4    Altenbuchner, J.5
  • 24
    • 0038492663 scopus 로고    scopus 로고
    • Crystal structure of D-hydantoinase from Burkholderia pickettii at a resolution of 2.7 angstroms: Insight into the molecular basis of enzyme thermostability
    • Xu, Z., Liu, Y., Yang, Y., Jiang, W., Arnold, E. and Ding, J. (2003). Crystal structure of D-hydantoinase from Burkholderia pickettii at a resolution of 2.7 angstroms: insight into the molecular basis of enzyme thermostability. J. Bacteriol. 185, 4038-4049.
    • (2003) J. Bacteriol. , vol.185 , pp. 4038-4049
    • Xu, Z.1    Liu, Y.2    Yang, Y.3    Jiang, W.4    Arnold, E.5    Ding, J.6
  • 25
    • 0001150167 scopus 로고
    • Distribution of hydantoin hydrolyzing activity in micro-organisms
    • Yamada, Y., Takahashi, S., Kii, Y. and Kumagai, H. (1978). Distribution of hydantoin hydrolyzing activity in micro-organisms. J. Ferment. Technol. 56, 484-491.
    • (1978) J. Ferment. Technol. , vol.56 , pp. 484-491
    • Yamada, Y.1    Takahashi, S.2    Kii, Y.3    Kumagai, H.4
  • 26
    • 13844263054 scopus 로고
    • Enzymatic production of L-tryptophan from D,L-5-indolylmethylhydantoin by mutants of Flavobacterium species T-523
    • Yokozeki, K., Sano, K., Eguchi, C., Yamada, K. and Mitsugi, K. (1987). Enzymatic production of L-tryptophan from D,L-5-indolylmethylhydantoin by mutants of Flavobacterium species T-523. Agri. Biol. Chem. 51, 819-825.
    • (1987) Agri. Biol. Chem. , vol.51 , pp. 819-825
    • Yokozeki, K.1    Sano, K.2    Eguchi, C.3    Yamada, K.4    Mitsugi, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.