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Volumn 6, Issue 2, 2002, Pages 111-122

A thermostable L-aminoacylase from Thermococcus litoralis: Cloning, overexpression, characterization, and applications in biotransformations

Author keywords

Biotransformations; Carboxypeptidase; L Aminoacylase; Substrate specificity; Thermococcus litoralis; Thermostable

Indexed keywords

ESCHERICHIA COLI; PYROCOCCUS HORIKOSHII; SULFOLOBUS SOLFATARICUS; THERMOCOCCUS; THERMOCOCCUS LITORALIS;

EID: 0036545508     PISSN: 14310651     EISSN: 14334909     Source Type: Journal    
DOI: 10.1007/s007920100230     Document Type: Article
Times cited : (43)

References (40)
  • 1
    • 0023777735 scopus 로고
    • Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli
    • Amst
    • Amann E, Ochs B, Abel KJ (1988) Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli. Gene (Amst) 60:301-315
    • (1988) Gene , vol.60 , pp. 301-315
    • Amann, E.1    Ochs, B.2    Abel, K.J.3
  • 3
    • 0032530505 scopus 로고    scopus 로고
    • Biocatalysis to amino acid-based chiral pharmaceuticals: Examples and perspectives
    • Bommarius AS, Schwarm M, Drauz K (1998) Biocatalysis to amino acid-based chiral pharmaceuticals: examples and perspectives. J Mol Catal B Enzym 5:1-11
    • (1998) J Mol Catal B Enzym , vol.5 , pp. 1-11
    • Bommarius, A.S.1    Schwarm, M.2    Drauz, K.3
  • 4
    • 0344836063 scopus 로고    scopus 로고
    • Studies on kinetic parameters and stability of aminoacylase in non-conventional media
    • Boross L, Kosary J, Stefanovits-Banyai E, Sisak C, Szajani B (1998) Studies on kinetic parameters and stability of aminoacylase in non-conventional media. J Biotechnol 66:69-73
    • (1998) J Biotechnol , vol.66 , pp. 69-73
    • Boross, L.1    Kosary, J.2    Stefanovits-Banyai, E.3    Sisak, C.4    Szajani, B.5
  • 5
    • 0344654050 scopus 로고    scopus 로고
    • Industrial applications of immobilized biocatalysts and biomaterials
    • Chibata I (1996) Industrial applications of immobilized biocatalysts and biomaterials. Adv Mol Cell Biol 15A:151-160
    • (1996) Adv Mol Cell Biol , vol.15 A , pp. 151-160
    • Chibata, I.1
  • 6
    • 0026539476 scopus 로고
    • Purification and characterization of a thermostable carboxypeptidase from the extreme thermophilic archaebacterium Sulfolobus solfataricus
    • Colombo S, D'Auria S, Fusi P, Zecca L, Raia CA, Tortora P (1992) Purification and characterization of a thermostable carboxypeptidase from the extreme thermophilic archaebacterium Sulfolobus solfataricus. Eur J Biochem 206:349-357
    • (1992) Eur J Biochem , vol.206 , pp. 349-357
    • Colombo, S.1    D'Auria, S.2    Fusi, P.3    Zecca, L.4    Raia, C.A.5    Tortora, P.6
  • 7
    • 0029619829 scopus 로고
    • Molecular cloning, nucleotide sequence, and expression of a carboxypeptidase-encoding gene from the archaebacterium Sulfolobus solfataricus
    • Colombo S, Toietta G, Zecca L, Vanoni M, Tortora P (1995) Molecular cloning, nucleotide sequence, and expression of a carboxypeptidase-encoding gene from the archaebacterium Sulfolobus solfataricus. J Bacteriol 177:5561-5566
    • (1995) J Bacteriol , vol.177 , pp. 5561-5566
    • Colombo, S.1    Toietta, G.2    Zecca, L.3    Vanoni, M.4    Tortora, P.5
  • 8
    • 0028981745 scopus 로고
    • Use of the overexpressed Bacillus stearothermophilus aminoacylase for the resolution of D,L amino acids in conventional and non-conventional media
    • Dion M, Loussouarn F, Batisse N, Rabiller C, Sakanyan V (1995) Use of the overexpressed Bacillus stearothermophilus aminoacylase for the resolution of D,L amino acids in conventional and non-conventional media. Biotechnol Lett 17:905-910
    • (1995) Biotechnol Lett , vol.17 , pp. 905-910
    • Dion, M.1    Loussouarn, F.2    Batisse, N.3    Rabiller, C.4    Sakanyan, V.5
  • 9
    • 0019809411 scopus 로고
    • Modified colourimetric ninhydrin methods for peptidase assay
    • Doi E, Shibata D, Matoba T (1981) Modified colourimetric ninhydrin methods for peptidase assay. Anal Biochem 118:173-184
    • (1981) Anal Biochem , vol.118 , pp. 173-184
    • Doi, E.1    Shibata, D.2    Matoba, T.3
  • 10
    • 0039401912 scopus 로고    scopus 로고
    • Chiral amino acids: A versatile tool in the synthesis of pharmaceuticals and fine chemicals
    • Drauz K (1997) Chiral amino acids: a versatile tool in the synthesis of pharmaceuticals and fine chemicals. Chimia 51:310-314
    • (1997) Chimia , vol.51 , pp. 310-314
    • Drauz, K.1
  • 12
    • 0001495722 scopus 로고    scopus 로고
    • Biocatalysis in organic synthesis. Part 9. Highly enantioselective kinetic resolution of secondary alcohols catalyzed by acylase
    • Faraldos J, Arroyo E, Herradon B (1997) Biocatalysis in organic synthesis. Part 9. Highly enantioselective kinetic resolution of secondary alcohols catalyzed by acylase. Synlett 4:367-370
    • (1997) Synlett , vol.4 , pp. 367-370
    • Faraldos, J.1    Arroyo, E.2    Herradon, B.3
  • 13
    • 0024971021 scopus 로고
    • Stability and activity of a thermostable malic enzyme in denaturants and water-miscible organic solvents
    • Guagliardi A, Manco G, Rossi M, Bartolucci S (1989) Stability and activity of a thermostable malic enzyme in denaturants and water-miscible organic solvents. Eur J Biochem 183:25-30
    • (1989) Eur J Biochem , vol.183 , pp. 25-30
    • Guagliardi, A.1    Manco, G.2    Rossi, M.3    Bartolucci, S.4
  • 15
    • 0024375506 scopus 로고
    • Reactivities of sulfhydryl groups in native and metal-free aminoacylase I
    • Heese D, Rohm KH (1989) Reactivities of sulfhydryl groups in native and metal-free aminoacylase I. Biol Chem Hoppe-Seyler 370:607-612
    • (1989) Biol Chem Hoppe-Seyler , vol.370 , pp. 607-612
    • Heese, D.1    Rohm, K.H.2
  • 17
    • 0023883352 scopus 로고
    • Aminoacylase I from hog kidney: Anion effects and pH dependence of kinetic parameters
    • Henseling J, Rohm K-H (1988) Aminoacylase I from hog kidney: anion effects and pH dependence of kinetic parameters. Biochim Biophys Acta 959:370-377
    • (1988) Biochim Biophys Acta , vol.959 , pp. 370-377
    • Henseling, J.1    Rohm, K.-H.2
  • 18
    • 0036006278 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of an aminoacylase from the hyperthermophilic archaeon Thermococcus litoralis
    • in press
    • Hollingsworth EJ, Isupov MN, Littlechild JA (2002) Crystallization and preliminary X-ray diffraction analysis of an aminoacylase from the hyperthermophilic archaeon Thermococcus litoralis. Acta Crystallogr D 58 (in press)
    • (2002) Acta Crystallogr D , vol.58
    • Hollingsworth, E.J.1    Isupov, M.N.2    Littlechild, J.A.3
  • 19
    • 0344061526 scopus 로고    scopus 로고
    • Hyperthermophiles and their ossible potential in biotechnology
    • Huber H, Stetter KO (1998) Hyperthermophiles and their ossible potential in biotechnology. J Biotechnol 64:39-52
    • (1998) J Biotechnol , vol.64 , pp. 39-52
    • Huber, H.1    Stetter, K.O.2
  • 20
    • 0035140695 scopus 로고    scopus 로고
    • Novel bifunctional hyperthermostable carboxypeptidase/aminoacylase from Pyrococcus horikoshii OT3
    • Ishikawa K, Ishida H, Matsui I, Kawarabayashi Y, Kikuchi H (2001) Novel bifunctional hyperthermostable carboxypeptidase/aminoacylase from Pyrococcus horikoshii OT3. Appl Environ Microbiol 67:673-679
    • (2001) Appl Environ Microbiol , vol.67 , pp. 673-679
    • Ishikawa, K.1    Ishida, H.2    Matsui, I.3    Kawarabayashi, Y.4    Kikuchi, H.5
  • 21
    • 0028360865 scopus 로고
    • A thermophilic, lipolytic Bacillus sp., and continuous assay of its p-nitrophenyl-palmitate esterase activity
    • Janssen PH, Monk CR, Morgan HW (1994) A thermophilic, lipolytic Bacillus sp., and continuous assay of its p-nitrophenyl-palmitate esterase activity. FEMS Microbiol Lett 120:195-200
    • (1994) FEMS Microbiol Lett , vol.120 , pp. 195-200
    • Janssen, P.H.1    Monk, C.R.2    Morgan, H.W.3
  • 23
    • 0034237457 scopus 로고    scopus 로고
    • Characterization of a solvent resistant and thermostable aminopeptidase from the hyperthermophilic bacterium Aquifex aeolicus
    • Khan AR, Nirasawa S, Kaneko S, Shimonishi T, Hayashi K (2000) Characterization of a solvent resistant and thermostable aminopeptidase from the hyperthermophilic bacterium Aquifex aeolicus. Enzyme Microbiol Technol 27:83-88
    • (2000) Enzyme Microbiol Technol , vol.27 , pp. 83-88
    • Khan, A.R.1    Nirasawa, S.2    Kaneko, S.3    Shimonishi, T.4    Hayashi, K.5
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond) 227:680-685
    • (1970) Nature (Lond) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0021689684 scopus 로고
    • The complete nucleotide sequence of the Pseudomonas gene coding for carboxypeptidase G2
    • Amst
    • Minton NP, Atkinson T, Bruton CJ, Sherwood RF (1984) The complete nucleotide sequence of the Pseudomonas gene coding for carboxypeptidase G2. Gene (Amst) 31:31-38
    • (1984) Gene , vol.31 , pp. 31-38
    • Minton, N.P.1    Atkinson, T.2    Bruton, C.J.3    Sherwood, R.F.4
  • 26
    • 4243240870 scopus 로고    scopus 로고
    • Biocatalysis for synthesis of chiral pharmaceutical intermediates
    • Lederberg JL (ed) Academic Press, London
    • Patel RN (2000) Biocatalysis for synthesis of chiral pharmaceutical intermediates. In: Lederberg JL (ed) Encyclopedia of microbiology, vol 1. Academic Press, London, pp 430-444
    • (2000) Encyclopedia of Microbiology , vol.1 , pp. 430-444
    • Patel, R.N.1
  • 27
    • 0020669405 scopus 로고
    • Determination of total protein
    • Hirs CHW, Timasheff SN (eds) Academic Press, New York
    • Peterson GL (1983) Determination of total protein. In: Hirs CHW, Timasheff SN (eds) Methods in enzymology, vol 91. Academic Press, New York, pp 95-119
    • (1983) Methods in Enzymology , vol.91 , pp. 95-119
    • Peterson, G.L.1
  • 28
    • 0019776662 scopus 로고
    • Minimization of variation in the response to different proteins of the Coomassie blue G dye-binding assay for protein
    • Read SM, Northcote DH (1981) Minimization of variation in the response to different proteins of the Coomassie blue G dye-binding assay for protein. Anal Biochem 116:53-64
    • (1981) Anal Biochem , vol.116 , pp. 53-64
    • Read, S.M.1    Northcote, D.H.2
  • 31
    • 0032731656 scopus 로고    scopus 로고
    • Biocatalysis for industrial production of fine chemicals
    • Schulze B, Wubbolts MG (1999) Biocatalysis for industrial production of fine chemicals. Curr Opin Biotechnol 10:609-615
    • (1999) Curr Opin Biotechnol , vol.10 , pp. 609-615
    • Schulze, B.1    Wubbolts, M.G.2
  • 32
    • 0034303174 scopus 로고    scopus 로고
    • Cloning, expression and characterization of pyrrolidone carboxyl peptidase from the archaeon Thermococcus litoralis
    • Singleton MR, Taylor SJC, Parrat JS, Littlechild JA (2000) Cloning, expression and characterization of pyrrolidone carboxyl peptidase from the archaeon Thermococcus litoralis. Extremophiles 4:297-303
    • (2000) Extremophiles , vol.4 , pp. 297-303
    • Singleton, M.R.1    Taylor, S.J.C.2    Parrat, J.S.3    Littlechild, J.A.4
  • 33
    • 0028883459 scopus 로고
    • Secondary structure of holo- and apo-aminoacylase from prediction, circular dichroism, and FT-Raman spectroscopy
    • Tokyo
    • Tang Z-Y, Yu J-Y, He B, Wang Z-F, Zhou H-M (1995) Secondary structure of holo- and apo-aminoacylase from prediction, circular dichroism, and FT-Raman spectroscopy. J Biochem (Tokyo) 118:706-709
    • (1995) J Biochem , vol.118 , pp. 706-709
    • Tang, Z.-Y.1    Yu, J.-Y.2    He, B.3    Wang, Z.-F.4    Zhou, H.-M.5
  • 34
    • 0027968068 scopus 로고
    • Clustal W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994) Clustal W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22:4673-4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 35
    • 0034663707 scopus 로고    scopus 로고
    • Purification and characterisation of Ak.1 protease, a thermostable subtilisin with a disulphide bond in the substrate-binding cleft
    • Toogood HS, Smith CA, Baker EN, Daniel RM (2000) Purification and characterisation of Ak.1 protease, a thermostable subtilisin with a disulphide bond in the substrate-binding cleft. Biochem J 350:321-328
    • (2000) Biochem J , vol.350 , pp. 321-328
    • Toogood, H.S.1    Smith, C.A.2    Baker, E.N.3    Daniel, R.M.4
  • 37
    • 0026516871 scopus 로고
    • Kinetics of the course of inactivation of aminoacylase by 1,10-phenanthroline
    • Wang Z-X, Wu H-B, Wang X-C, Zhou H-M, Tsou C-L (1992) Kinetics of the course of inactivation of aminoacylase by 1,10-phenanthroline. Biochem J 281:285-290
    • (1992) Biochem J , vol.281 , pp. 285-290
    • Wang, Z.-X.1    Wu, H.-B.2    Wang, X.-C.3    Zhou, H.-M.4    Tsou, C.-L.5
  • 38
    • 0027380254 scopus 로고
    • A comparison of Zn(II) and Co(II) in the kinetics of inactivation of aminoacylase by 1,10-phenanthroline and reconstitution of the apoenzyme
    • Wu H-B, Tsou C-L (1993) A comparison of Zn(II) and Co(II) in the kinetics of inactivation of aminoacylase by 1,10-phenanthroline and reconstitution of the apoenzyme. Biochem J 296:435-441
    • (1993) Biochem J , vol.296 , pp. 435-441
    • Wu, H.-B.1    Tsou, C.-L.2
  • 39
    • 0030469028 scopus 로고    scopus 로고
    • Kinetics of inhibition of aminoacylase activity by dithiothreitol or 2-mercaptoethanol
    • Yang Y, Wang H-R, Zhou H-M (1996) Kinetics of inhibition of aminoacylase activity by dithiothreitol or 2-mercaptoethanol. Int J Pept Protein Res 48:532-538
    • (1996) Int J Pept Protein Res , vol.48 , pp. 532-538
    • Yang, Y.1    Wang, H.-R.2    Zhou, H.-M.3
  • 40
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Amst
    • Yanisch-Perron C, Vieira J, Messing J (1985) Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene (Amst) 33:103-119
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3


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