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Volumn 29, Issue 2, 2007, Pages 303-308

Subunit dissociation and stability alteration of D-hydantoinase deleted at the terminal amino acid residue

Author keywords

Hydantoinase; Purification; Stability alteration; Subunit dissociation; Terminal residue deletion

Indexed keywords

AMINO ACIDS; DISSOCIATION; ENZYME KINETICS; ESCHERICHIA COLI; PURIFICATION;

EID: 33846155635     PISSN: 01415492     EISSN: 15736776     Source Type: Journal    
DOI: 10.1007/s10529-006-9238-9     Document Type: Article
Times cited : (13)

References (22)
  • 1
    • 0035713489 scopus 로고    scopus 로고
    • Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids
    • Altenbuchner J, Siemann-Herzberg M, Syldatk C (2001) Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids. Curr Opin Biotechnol 12:559-563
    • (2001) Curr Opin Biotechnol , vol.12 , pp. 559-563
    • Altenbuchner, J.1    Siemann-Herzberg, M.2    Syldatk, C.3
  • 2
    • 0036299882 scopus 로고    scopus 로고
    • X-ray structure of a dihydropyrimidinase from Thermus sp. at 1.3 Å resolution
    • Abendroth J, Niefind K, Schomburg D (2002) X-ray structure of a dihydropyrimidinase from Thermus sp. at 1.3 Å resolution. J Mol Biol 320:143-156
    • (2002) J Mol Biol , vol.320 , pp. 143-156
    • Abendroth, J.1    Niefind, K.2    Schomburg, D.3
  • 3
    • 0033081891 scopus 로고    scopus 로고
    • A new proposal for urease mechanism based on the crystal structures of the native and inhibited enzyme from Bacillus pasteurii: Why urea hydrolysis costs two nickels
    • Benini S, Rypniewski WR, Wilson KS, Miletti S, Ciurli S, Mangani S (1999) A new proposal for urease mechanism based on the crystal structures of the native and inhibited enzyme from Bacillus pasteurii: why urea hydrolysis costs two nickels. Structure 7:205-216
    • (1999) Structure , vol.7 , pp. 205-216
    • Benini, S.1    Rypniewski, W.R.2    Wilson, K.S.3    Miletti, S.4    Ciurli, S.5    Mangani, S.6
  • 4
    • 0034000386 scopus 로고    scopus 로고
    • The complex of Bacillus pasteurii urease with acetohydroxamate anion from X-ray data at 1.55 Å resolution
    • Benini S, Rypniewski WR, Wilson KS, Miletti S, Ciurli S, Mangani S (2000) The complex of Bacillus pasteurii urease with acetohydroxamate anion from X-ray data at 1.55 Å resolution. J Biol Inorg Chem 5:110-118
    • (2000) J Biol Inorg Chem , vol.5 , pp. 110-118
    • Benini, S.1    Rypniewski, W.R.2    Wilson, K.S.3    Miletti, S.4    Ciurli, S.5    Mangani, S.6
  • 5
    • 0037199453 scopus 로고    scopus 로고
    • Crystal structure of D-hydantoinase from Bacillus stearothermophilus: Insight into the stereochemistry of enantioselectivity
    • Cheon YH, Kim HS, Han KH, Abendroth J, Niefind K, Schomburg D, Wang J, Kim Y (2002) Crystal structure of D-hydantoinase from Bacillus stearothermophilus: insight into the stereochemistry of enantioselectivity. Biochemistry 41:9410-9417
    • (2002) Biochemistry , 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
  • 6
    • 5344275196 scopus 로고    scopus 로고
    • Structural roles of the active site iron(III) ions in catechol 1,2-dioxygenases and differential secondary structure changes in isoenzymes A and B from Acinetobacter radioresistens S13
    • Nardoa G, Tilli S, Pessionea E, CavalettoaM, Giuntaa C, Briganti F (2004) Structural roles of the active site iron(III) ions in catechol 1,2-dioxygenases and differential secondary structure changes in isoenzymes A and B from Acinetobacter radioresistens S13. Arch Biochem Biophys 431:79-87
    • (2004) Arch Biochem Biophys , vol.431 , pp. 79-87
    • Nardoa, G.1    Tilli, S.2    Pessionea, E.3    Cavalettoa, M.4    Giuntaa, C.5    Briganti, F.6
  • 7
    • 0031977176 scopus 로고    scopus 로고
    • Efficient conversion of 5-substituted hydantoins to D-alpha-amino acids using recombinant Escherichia coli strains
    • Grifantini R, Galli G, Garpani G, Pratesi C, Frascotti G, Grandi G (1998) Efficient conversion of 5-substituted hydantoins to D-alpha-amino acids using recombinant Escherichia coli strains. Microbiology 144: 947-954
    • (1998) Microbiology , vol.144 , pp. 947-954
    • Grifantini, R.1    Galli, G.2    Garpani, G.3    Pratesi, C.4    Frascotti, G.5    Grandi, G.6
  • 8
    • 0032481264 scopus 로고    scopus 로고
    • C-terminal regions of D-hydantoinases are non-essential for catalysis, but affect the oligomeric structure
    • Kim GJ, Kim HS (1998) C-terminal regions of D-hydantoinases are non-essential for catalysis, but affect the oligomeric structure. Biochem Biophys Res Commun 243:96-100
    • (1998) Biochem Biophys Res Commun , vol.243 , pp. 96-100
    • Kim, G.J.1    Kim, H.S.2
  • 9
    • 0024094367 scopus 로고
    • Stereio- and substrate-specificity of a D-hydantoinase and a D-N- carbamoyl-amino acid amidohydrolase of Arthrobacter crystallopoietes AM2
    • Moller A, Syldatk C, Schulze M, Wagner F (1988) Stereio- and substrate-specificity of a D-hydantoinase and a D-N- carbamoyl-amino acid amidohydrolase of Arthrobacter crystallopoietes AM2. Enzyme Microb Technol 10:618-625
    • (1988) Enzyme Microb Technol , vol.10 , pp. 618-625
    • Moller, A.1    Syldatk, C.2    Schulze, M.3    Wagner, F.4
  • 10
    • 0036862421 scopus 로고    scopus 로고
    • Complete conversion of D, L-5-monosubstituted hydantoins with a low velocity of chemical racemization into D-amino acids using whole cells of recombinant Escherichia coli
    • Martinez-Rodriguez S, Las Heras-Vazquez FJ, Clemente-Jimenez JM, Mingorance-Cazorla L, Rodriguez-Vico F (2002) Complete conversion of D, L-5-monosubstituted hydantoins with a low velocity of chemical racemization into D-amino acids using whole cells of recombinant Escherichia coli. Biotechnol Prog 18:1201-1206
    • (2002) Biotechnol Prog , vol.18 , pp. 1201-1206
    • Martinez-Rodriguez, S.1    Las Heras-Vazquez, F.J.2    Clemente-Jimenez, J.M.3    Mingorance-Cazorla, L.4    Rodriguez-Vico, F.5
  • 11
    • 4644326682 scopus 로고    scopus 로고
    • Mutational analysis of the hydantoin hydrolysis pathway in Pseudomonas putida RU-KM3S
    • Matcher GF, Burton SG, Dorrington RA (2004) Mutational analysis of the hydantoin hydrolysis pathway in Pseudomonas putida RU-KM3S. Appl Microbiol Biotechnol 65:391-400
    • (2004) Appl Microbiol Biotechnol , vol.65 , pp. 391-400
    • Matcher, G.F.1    Burton, S.G.2    Dorrington, R.A.3
  • 12
    • 0036669691 scopus 로고    scopus 로고
    • Industrial microbial enzymes: Their discovery by screening and use in large-scale production of useful chemicals in Japan
    • Ogawa J, Shimizu S (2002) Industrial microbial enzymes: their discovery by screening and use in large-scale production of useful chemicals in Japan. Curr Opin Biotechnol 13:367-375
    • (2002) Curr Opin Biotechnol , vol.13 , pp. 367-375
    • Ogawa, J.1    Shimizu, S.2
  • 13
    • 0034233319 scopus 로고    scopus 로고
    • Production of D-amino acid using whole cells of recombinant Escherichia coli with separately and coexpressed D-hydantoinase and N-carbamoylase
    • Park JH, Kim GJ, Kim HS, (2000) Production of D-amino acid using whole cells of recombinant Escherichia coli with separately and coexpressed D-hydantoinase and N-carbamoylase. Biotechnol Prog 16:564-570
    • (2000) Biotechnol Prog , vol.16 , pp. 564-570
    • Park, J.H.1    Kim, G.J.2    Kim, H.S.3
  • 14
    • 27944483308 scopus 로고    scopus 로고
    • Gene sequence, soluble expression and homologous comparison of a D-hydantoinase from Pseudomonas putida YZ-26
    • Shi YW, Zhao LX, Niu LX, Feng X, Yuan JM (2005) Gene sequence, soluble expression and homologous comparison of a D-hydantoinase from Pseudomonas putida YZ-26. Chem Commun Chin Univ 21:552-557
    • (2005) Chem Commun Chin Univ , vol.21 , pp. 552-557
    • Shi, Y.W.1    Zhao, L.X.2    Niu, L.X.3    Feng, X.4    Yuan, J.M.5
  • 15
    • 33745683864 scopus 로고    scopus 로고
    • Purification, enzymatic properties of a recombinant D-hydantoinase and its dissociation by zinc ion
    • Shi YW, Niu LX, Feng X, Yuan JM (2006) Purification, enzymatic properties of a recombinant D-hydantoinase and its dissociation by zinc ion. World J Microbiol Biotechnol 22:350-357
    • (2006) World J Microbiol Biotechnol , vol.22 , pp. 350-357
    • Shi, Y.W.1    Niu, L.X.2    Feng, X.3    Yuan, J.M.4
  • 16
    • 0002426626 scopus 로고
    • Production of optically pure D- and L-amino acids by bioconversion of D, L-5-monosubstituted hydantoin derivatives
    • Syldatk C, Laufer A, Muller R, Hoke H (1990) Production of optically pure D- and L-amino acids by bioconversion of D, L-5-monosubstituted hydantoin derivatives. Adv Biochem Eng Biotechnol 41:31-75
    • (1990) Adv Biochem Eng Biotechnol , vol.41 , pp. 31-75
    • Syldatk, C.1    Laufer, A.2    Muller, R.3    Hoke, H.4
  • 18
    • 0035912842 scopus 로고    scopus 로고
    • Molecular structure of dihydroorotase: A paradigm for catalysis through the use of a binuclear metal center
    • Thoden JB, Phillips GNJ, Neal TM, Raushel FM, Holden HM (2001) Molecular structure of dihydroorotase: a paradigm for catalysis through the use of a binuclear metal center. Biochemistry 40:6989-6997
    • (2001) Biochemistry , vol.40 , pp. 6989-6997
    • Thoden, J.B.1    Phillips, G.N.J.2    Neal, T.M.3    Raushel, F.M.4    Holden, H.M.5
  • 19
    • 28944446279 scopus 로고    scopus 로고
    • Orientation and oligomerization specificity of the Bcr coiled-coil oligomerization domain
    • Taylor CM, Keating AE (2005) Orientation and oligomerization specificity of the Bcr coiled-coil oligomerization domain. Biochemistry 44:16246-16256
    • (2005) Biochemistry , vol.44 , pp. 16246-16256
    • Taylor, C.M.1    Keating, A.E.2
  • 20
    • 32944457963 scopus 로고    scopus 로고
    • Identification of inducible protein complexes in the phenol degrader Pseudomonas sp. strain phDV1 by blue native gel electrophoresis and mass spectrometry
    • Tsirogianni E, Aivaliotis M, Papasotiriou DG, Karas M, Tsiotis G. (2006) Identification of inducible protein complexes in the phenol degrader Pseudomonas sp. strain phDV1 by blue native gel electrophoresis and mass spectrometry. Amino Acids 30:63-72
    • (2006) Amino Acids , vol.30 , pp. 63-72
    • Tsirogianni, E.1    Aivaliotis, M.2    Papasotiriou, D.G.3    Karas, M.4    Tsiotis, G.5
  • 21
    • 0038492663 scopus 로고    scopus 로고
    • Crystal structure of D-hydantoinase from Burkholderia pickettii at a resolution of 2.7 Angstroms: Insights into the molecular basis of enzyme thermostability
    • Xu Z, Liu YQ, Yang YL, Jiang WH, Arnold E, Ding JP (2003) Crystal structure of D-hydantoinase from Burkholderia pickettii at a resolution of 2.7 Angstroms: insights 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.Q.2    Yang, Y.L.3    Jiang, W.H.4    Arnold, E.5    Ding, J.P.6
  • 22
    • 0000416214 scopus 로고    scopus 로고
    • Enzymatic production of L-amino acids from the corresponding 5′-substituted hydantoins by a newly isolated bacterium Bacillus brevis AJ-12299
    • Yamashiro A, Yokozeki K, Kano H, Kubota K (1998) Enzymatic production of L-amino acids from the corresponding 5′-substituted hydantoins by a newly isolated bacterium Bacillus brevis AJ-12299. Agric Biol Chem 52:2851-2856
    • (1998) Agric Biol Chem , vol.52 , pp. 2851-2856
    • Yamashiro, A.1    Yokozeki, K.2    Kano, H.3    Kubota, K.4


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