메뉴 건너뛰기




Volumn 85, Issue 6, 2010, Pages 1839-1847

Characterization of an L-arabinose isomerase from Bacillus subtilis

Author keywords

Bacillus subtilis; Characterization; Homology modeling; L arabinose isomerase; Substrate specificity

Indexed keywords

AMINO ACID RESIDUES; BACILLUS SUBTILIS; CATALYTIC EFFICIENCIES; D-GALACTOSE; DNA SEQUENCE ANALYSIS; E. COLI; HOMOLOGY MODELING; HOMOLOGY MODELS; ISOMERASES; L-ARABINOSE; L-ARABINOSE ISOMERASE; MOLECULAR DYNAMICS SIMULATIONS; NATURAL SUBSTRATES; NICKEL-NITRILOTRIACETIC ACID CHROMATOGRAPHY; NUCLEOTIDE SEQUENCES; OPEN READING FRAME; PURIFIED ENZYME; SUBSTRATE SPECIFICITY; SUBTILIS; X RAY CRYSTAL STRUCTURES;

EID: 76849098687     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-009-2210-6     Document Type: Article
Times cited : (36)

References (26)
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 10.1016/0003-2697(76)90527-3 1:CAS:528:DyaE28XksVehtrY%3D
    • MM Bradford 1976 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 10.1016/0003-2697(76)90527-3 1:CAS:528: DyaE28XksVehtrY%3D
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 84986512474 scopus 로고
    • CHARMm: A program for macromolecular energy, minimization, and dynamics calculations
    • 10.1002/jcc.540040211 1:CAS:528:DyaL3sXit1aiu7w%3D
    • B Brooks RE Bruccoleri BD Olafson DJ States S Swaminathan M Karplus 1983 CHARMm: a program for macromolecular energy, minimization, and dynamics calculations J Comput Chem 4 187 217 10.1002/jcc.540040211 1:CAS:528: DyaL3sXit1aiu7w%3D
    • (1983) J Comput Chem , vol.4 , pp. 187-217
    • Brooks, B.1    Bruccoleri, R.E.2    Olafson, B.D.3    States, D.J.4    Swaminathan, S.5    Karplus, M.6
  • 4
    • 17044420476 scopus 로고    scopus 로고
    • A new efficient and practical synthesis of 2-deoxy-L-ribose
    • 10.1016/j.tet.2005.03.001 1:CAS:528:DC%2BD2MXjtFKmtLg%3D
    • B Cho JH Kim HB Jeon KS Kim 2005 A new efficient and practical synthesis of 2-deoxy-L-ribose Tetrahedron 61 4341 4346 10.1016/j.tet.2005.03.001 1:CAS:528:DC%2BD2MXjtFKmtLg%3D
    • (2005) Tetrahedron , vol.61 , pp. 4341-4346
    • Cho, B.1    Kim, J.H.2    Jeon, H.B.3    Kim, K.S.4
  • 5
    • 36348972810 scopus 로고    scopus 로고
    • Characterization of an L-arabinose isomerase from the Lactobacillus plantarum NC8 strain showing pronounced stability at acidic pH
    • DOI 10.1111/j.1574-6968.2007.00961.x
    • H Chouayekh W Bejar M Rhimi K Jelleli M Mseddi S Bejar 2007 Characterization of an l-arabinose isomerase from the Lactobacillus plantarum NC8 strain showing pronounced stability at acidic pH FEMS Microbiol Lett 277 260 267 10.1111/j.1574-6968.2007.00961.x 1:CAS:528:DC%2BD2sXhsVersLzI (Pubitemid 350145580)
    • (2007) FEMS Microbiology Letters , vol.277 , Issue.2 , pp. 260-267
    • Chouayekh, H.1    Bejar, W.2    Rhimi, M.3    Jelleli, K.4    Mseddi, M.5    Bejar, S.6
  • 6
    • 0346814641 scopus 로고
    • A new spectrophotometric method for the detection and determination of keto sugars and trioses
    • 1:CAS:528:DyaG38XhtFOgug%3D%3D
    • Z Dische E Borenfreund 1951 A new spectrophotometric method for the detection and determination of keto sugars and trioses J Biol Chem 192 583 587 1:CAS:528:DyaG38XhtFOgug%3D%3D
    • (1951) J Biol Chem , vol.192 , pp. 583-587
    • Dische, Z.1    Borenfreund, E.2
  • 7
    • 0036202220 scopus 로고    scopus 로고
    • Bioproduction strategies for rare hexose sugars
    • DOI 10.1007/s00114-002-0297-z
    • K Izumori 2002 Bioproduction strategies for rare hexose sugars Naturwissenschaften 89 120 124 10.1007/s00114-002-0297-z 1:CAS:528: DC%2BD38XhslKjt7s%3D (Pubitemid 34264058)
    • (2002) Naturwissenschaften , vol.89 , Issue.3 , pp. 120-124
    • Izumori, K.1
  • 8
    • 3142713057 scopus 로고    scopus 로고
    • Enzymatic conversion of D-galactose to D-tagatose: Heterologous expression and characterisation of a thermostable L-arabinose isomerase from Thermoanaerobacter mathranii
    • DOI 10.1007/s00253-004-1578-6
    • F Jorgensen OC Hansen P Stougaard 2004 Enzymatic conversion of D-galactose to D-tagatose: heterologous expression and characterisation of a thermostable L-arabinose isomerase from Thermoanaerobacter mathranii Appl Microbiol Biotechnol 64 816 822 10.1007/s00253-004-1578-6 1:CAS:528: DC%2BD2cXktlyrsr4%3D (Pubitemid 38918145)
    • (2004) Applied Microbiology and Biotechnology , vol.64 , Issue.6 , pp. 816-822
    • Jorgensen, F.1    Hansen, O.C.2    Stougaard, P.3
  • 9
    • 26444526645 scopus 로고    scopus 로고
    • Purification and characterization of an L-arabinose isomerase from an isolated strain of Geobacillus thermodenitrificans producing D-tagatose
    • DOI 10.1016/j.jbiotec.2005.06.004, PII S0168165605002920
    • HJ Kim DK Oh 2005 Purification and characterization of an L-arabinose isomerase from an isolated strain of Geobacillus thermodenitrificans producing D-tagatose J Biotechnol 120 162 173 10.1016/j.jbiotec.2005.06.004 1:CAS:528:DC%2BD2MXhtFSisLrL (Pubitemid 41429278)
    • (2005) Journal of Biotechnology , vol.120 , Issue.2 , pp. 162-173
    • Kim, H.-J.1    Oh, D.-K.2
  • 10
    • 0037129833 scopus 로고    scopus 로고
    • Cloning, expression and characterization of L-arabinose isomerase from Thermotoga neapolitana: Bioconversion of D-galactose to D-tagatose using the enzyme
    • 1:CAS:528:DC%2BD38XksF2jsrY%3D
    • BC Kim YH Lee HS Lee DW Lee EA Choe YR Pyun 2002 Cloning, expression and characterization of L-arabinose isomerase from Thermotoga neapolitana: bioconversion of D-galactose to D-tagatose using the enzyme FEMS Microbiol Lett 212 121 126 1:CAS:528:DC%2BD38XksF2jsrY%3D
    • (2002) FEMS Microbiol Lett , vol.212 , pp. 121-126
    • Kim, B.C.1    Lee, Y.H.2    Lee, H.S.3    Lee, D.W.4    Choe, E.A.5    Pyun, Y.R.6
  • 11
    • 33745454160 scopus 로고    scopus 로고
    • Characterization of a mutated Geobacillus stearothermophilus L-arabinose isomerase that increases the production rate of D-tagatose
    • DOI 10.1111/j.1365-2672.2006.02975.x
    • HJ Kim JH Kim HJ Oh DK Oh 2006 Characterization of a mutated Geobacillus stearothermophilus L-arabinose isomerase that increases the production rate of D-tagatose J Appl Microbiol 101 213 221 10.1111/j.1365-2672.2006.02975.x 1:CAS:528:DC%2BD28XotFKgtb4%3D (Pubitemid 43952021)
    • (2006) Journal of Applied Microbiology , vol.101 , Issue.1 , pp. 213-221
    • Kim, H.-J.1    Kim, J.-H.2    Oh, H.-J.3    Oh, D.-K.4
  • 13
    • 1642416740 scopus 로고    scopus 로고
    • Characterization of a Thermostable L-Arabinose (D-Galactose) Isomerase from the Hyperthermophilic Eubacterium Thermotoga maritima
    • DOI 10.1128/AEM.70.3.1397-1404.2004
    • DW Lee HJ Jang EA Choe BC Kim SJ Lee SB Kim YH Hong YR Pyun 2004 Characterization of a thermostable L-arabinose (D-galactose) isomerase from the hyperthermophilic eubacterium Thermotoga maritima Appl Environ Microbiol 70 1397 1404 10.1128/AEM.70.3.1397-1404.2004 1:CAS:528:DC%2BD2cXisVKjuro%3D (Pubitemid 38365119)
    • (2004) Applied and Environmental Microbiology , vol.70 , Issue.3 , pp. 1397-1404
    • Lee, D.-W.1    Jang, H.-J.2    Choe, E.-A.3    Kim, B.-C.4    Lee, S.-J.5    Kim, S.-B.6    Hong, Y.-H.7    Pyun, Y.-R.8
  • 14
    • 11444258321 scopus 로고    scopus 로고
    • Distinct metal dependence for catalytic and structural functions in the l-arabinose isomerases from the mesophilic Bacillus halodurans and the thermophilic Geobacillus stearothermophilus
    • DOI 10.1016/j.abb.2004.11.004, PII S0003986104006496
    • DW Lee EA Choe SB Kim SH Eom YH Hong SJ Lee HS Lee DY Lee YR Pyun 2005 Distinct metal dependence for catalytic and structural functions in the L-arabinose isomerases from the mesophilic Bacillus halodurans and the thermophilic Geobacillus stearothermophilus Arch Biochem Biophys 434 333 343 10.1016/j.abb.2004.11.004 1:CAS:528:DC%2BD2MXhvFyktw%3D%3D (Pubitemid 40082042)
    • (2005) Archives of Biochemistry and Biophysics , vol.434 , Issue.2 , pp. 333-343
    • Lee, D.-W.1    Choe, E.-A.2    Kim, S.-B.3    Eom, S.-H.4    Hong, Y.-H.5    Lee, S.-J.6    Lee, H.-S.7    Lee, D.-Y.8    Pyun, Y.-R.9
  • 15
    • 13844271823 scopus 로고    scopus 로고
    • A thermodynamic study of mesophilic, thermophilic, and hyperthermophilic L-arabinose isomerases: The effects of divalent metal ions on protein stability at elevated temperatures
    • DOI 10.1016/j.febslet.2005.01.027
    • DW Lee YH Hong EA Choe SJ Lee SB Kim HS Lee JW Oh HH Shin YR Pyun 2005 A thermodynamic study of mesophilic, thermophilic, and hyperthermophilic L-arabinose isomerases: the effects of divalent metal ions on protein stability at elevated temperatures FEBS Lett 579 1261 1266 10.1016/j.febslet.2005.01.027 1:CAS:528:DC%2BD2MXhtlOntLs%3D (Pubitemid 40248697)
    • (2005) FEBS Letters , vol.579 , Issue.5 , pp. 1261-1266
    • Lee, D.-W.1    Hong, Y.-H.2    Choe, E.-A.3    Lee, S.-J.4    Kim, S.-B.5    Lee, H.-S.6    Oh, J.-W.7    Shin, H.-H.8    Pyun, Y.-R.9
  • 16
    • 29144453887 scopus 로고    scopus 로고
    • Characterization of a thermoacidophilic L-arabinose isomerase from Alicyclobacillus acidocaldarius: Role of Lys-269 in pH optimum
    • DOI 10.1128/AEM.71.12.7888-7896.2005
    • SJ Lee DW Lee EA Choe YH Hong SB Kim BC Kim YR Pyun 2005 Characterization of a thermoacidophilic L-arabinose isomerase from Alicyclobacillus acidocaldarius: role of Lys-269 in pH optimum Appl Environ Microbiol 71 7888 7896 10.1128/AEM.71.12.7888-7896.2005 1:CAS:528:DC%2BD2MXhtlehtLjO (Pubitemid 41803907)
    • (2005) Applied and Environmental Microbiology , vol.71 , Issue.12 , pp. 7888-7896
    • Lee, S.-J.1    Lee, D.-W.2    Choe, E.-A.3    Hong, Y.-H.4    Kim, S.-B.5    Kim, B.-C.6    Pyun, Y.-R.7
  • 17
    • 33745287171 scopus 로고    scopus 로고
    • Crystal Structure of Escherichia coli L-Arabinose Isomerase (ECAI), The Putative Target of Biological Tagatose Production
    • DOI 10.1016/j.jmb.2006.04.040, PII S0022283606005146
    • BA Manjasetty MR Chance 2006 Crystal structure of Escherichia coli L-arabinose isomerase (ECAI), the putative target of biological tagatose production J Mol Biol 360 297 309 10.1016/j.jmb.2006.04.040 1:CAS:528: DC%2BD28Xmt1yrs7Y%3D (Pubitemid 43927823)
    • (2006) Journal of Molecular Biology , vol.360 , Issue.2 , pp. 297-309
    • Manjasetty, B.A.1    Chance, M.R.2
  • 18
    • 0014429922 scopus 로고
    • Purification and properties of an L-arabinose isomerase from Escherichia coli
    • 1:CAS:528:DyaF1cXksV2gtb8%3D
    • JW Patrick N Lee 1968 Purification and properties of an L-arabinose isomerase from Escherichia coli J Biol Chem 243 4312 4318 1:CAS:528: DyaF1cXksV2gtb8%3D
    • (1968) J Biol Chem , vol.243 , pp. 4312-4318
    • Patrick, J.W.1    Lee, N.2
  • 19
    • 55649100728 scopus 로고    scopus 로고
    • Cloning and characterization of a novel L-arabinose isomerase from Bacillus licheniformis
    • 10.1007/s00253-008-1652-6 1:CAS:528:DC%2BD1cXhtlaqsbnN
    • P Prabhu M Tiwari M Jeya P Gunasekaran IW Kim JK Lee 2008 Cloning and characterization of a novel L-arabinose isomerase from Bacillus licheniformis Appl Microbiol Biotechnol 81 283 290 10.1007/s00253-008-1652-6 1:CAS:528:DC%2BD1cXhtlaqsbnN
    • (2008) Appl Microbiol Biotechnol , vol.81 , pp. 283-290
    • Prabhu, P.1    Tiwari, M.2    Jeya, M.3    Gunasekaran, P.4    Kim, I.W.5    Lee, J.K.6
  • 20
    • 33644629689 scopus 로고    scopus 로고
    • Cloning, purification and biochemical characterization of metallic-ions independent and thermoactive l-arabinose isomerase from the Bacillus stearothermophilus US100 strain
    • 1:CAS:528:DC%2BD28XitVarsLw%3D
    • M Rhimi S Bejar 2006 Cloning, purification and biochemical characterization of metallic-ions independent and thermoactive l-arabinose isomerase from the Bacillus stearothermophilus US100 strain Biochim Biophys Acta 1760 191 199 1:CAS:528:DC%2BD28XitVarsLw%3D
    • (2006) Biochim Biophys Acta , vol.1760 , pp. 191-199
    • Rhimi, M.1    Bejar, S.2
  • 21
    • 0347874223 scopus 로고    scopus 로고
    • Bioconversion of D-galactose into D-tagatose by expression of L-arabinose isomerase
    • 10.1042/BA19990065 1:CAS:528:DC%2BD3cXhs1Sntb4%3D
    • HJ Roh P Kim YC Park JH Choi 2000 Bioconversion of D-galactose into D-tagatose by expression of L-arabinose isomerase Biotechnol Appl Biochem 31 Pt 1 1 4 10.1042/BA19990065 1:CAS:528:DC%2BD3cXhs1Sntb4%3D
    • (2000) Biotechnol Appl Biochem , vol.31 , Issue.PART 1 , pp. 1-4
    • Roh, H.J.1    Kim, P.2    Park, Y.C.3    Choi, J.H.4
  • 22
    • 0031576360 scopus 로고    scopus 로고
    • Structure and mechanism of L-Fucose Isomerase from Escherichia coli
    • DOI 10.1006/jmbi.1997.1280
    • JE Seemann GE Schulz 1997 Structure and mechanism of L-fucose isomerase from Escherichia coli J Mol Biol 273 256 268 10.1006/jmbi.1997.1280 1:CAS:528:DyaK2sXmvFymtb4%3D (Pubitemid 27460228)
    • (1997) Journal of Molecular Biology , vol.273 , Issue.1 , pp. 256-268
    • Seemann, J.E.1    Schulz, G.E.2
  • 23
    • 0041781898 scopus 로고    scopus 로고
    • Detailed analysis of grid-based molecular docking: A case study of CDOCKER-A CHARMm-based MD docking algorithm
    • 10.1002/jcc.10306 1:CAS:528:DC%2BD3sXntFent70%3D
    • G Wu DH Robertson CL Brooks 3rd M Vieth 2003 Detailed analysis of grid-based molecular docking: a case study of CDOCKER-A CHARMm-based MD docking algorithm J Comput Chem 24 1549 1562 10.1002/jcc.10306 1:CAS:528: DC%2BD3sXntFent70%3D
    • (2003) J Comput Chem , vol.24 , pp. 1549-1562
    • Wu, G.1    Robertson, D.H.2    Brooks III, C.L.3    Vieth, M.4
  • 24
    • 0037299866 scopus 로고    scopus 로고
    • Properties of L-arabinose isomerase from Escherichia coli as biocatalyst for tagatose production
    • DOI 10.1023/A:1022575601492
    • S Yoon P Kim DK Oh 2003 Properties of L-arabinose isomerase from Escherichia coli as biocatalyst for tagatose production World J Microbiol Biotechnol 19 47 51 10.1023/A:1022575601492 1:CAS:528:DC%2BD3sXhsFKkurY%3D (Pubitemid 36357487)
    • (2003) World Journal of Microbiology and Biotechnology , vol.19 , Issue.1 , pp. 47-51
    • Yoon, S.-H.1    Kim, P.2    Oh, D.-K.3
  • 25
    • 23044433521 scopus 로고    scopus 로고
    • A highly efficient synthesis of unnatural L-sugars from D-ribose
    • DOI 10.1016/j.tetlet.2005.06.117, PII S0040403905014012
    • M Yun HR Moon HO Kim WJ Choi YC Kim CS Park LS Jeong 2005 A highly efficient synthesis of unnatural l-sugars from d-ribose Tetrahedron Lett 46 5903 5905 10.1016/j.tetlet.2005.06.117 1:CAS:528:DC%2BD2MXntVCnsro%3D (Pubitemid 41073439)
    • (2005) Tetrahedron Letters , vol.46 , Issue.35 , pp. 5903-5905
    • Yun, M.1    Hyung, R.M.2    Hea, O.K.3    Won, J.C.4    Kim, Y.-C.5    Park, C.-S.6    Lak, S.J.7
  • 26
    • 4544321006 scopus 로고    scopus 로고
    • Production of natural and rare pentoses using microorganisms and their enzymes
    • A Zakaria 2001 Production of natural and rare pentoses using microorganisms and their enzymes Electron J Biotechnol 4 103 111
    • (2001) Electron J Biotechnol , vol.4 , pp. 103-111
    • Zakaria, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.