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Volumn 17, Issue 5, 2007, Pages 721-727

Synthesis of L-threo-3,4-dihydroxyphenylserine (L-threo-DOPS) with thermostabilized low-specific L-threonine aldolase from Streptomyces coelicolor A3(2)

Author keywords

In vitro mutagenesis; L threo DOPS; L threonine aldolase; Thermostability

Indexed keywords

FRUCTOSE BISPHOSPHATE ALDOLASE; GLYCINE; PROTOCATECHUALDEHYDE; THREO 3,4 DIHYDROXYPHENYLSERINE; THREONINE ALDOLASE; UNCLASSIFIED DRUG;

EID: 34250186111     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (30)

References (18)
  • 1
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantitites of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantitites of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 2
    • 33748705981 scopus 로고    scopus 로고
    • Substitutions for Cys-472 and His-509 at the activity site of β-galactosidase from Lactococcus lactis ssp. lactis 7962 cause large decreases in enzyme activity
    • Chung, H. Y., E. J. Yang, and H. C. Chang. 2006. Substitutions for Cys-472 and His-509 at the activity site of β-galactosidase from Lactococcus lactis ssp. lactis 7962 cause large decreases in enzyme activity. J. Microbiol. Biotechnol. 16: 1325-1329.
    • (2006) J. Microbiol. Biotechnol , vol.16 , pp. 1325-1329
    • Chung, H.Y.1    Yang, E.J.2    Chang, H.C.3
  • 3
    • 0035709383 scopus 로고    scopus 로고
    • Biocatalytic synthesis of hydroxylated natural products using aldolases and related enzymes
    • Fessner, W. D. and V. Helaine. 2001. Biocatalytic synthesis of hydroxylated natural products using aldolases and related enzymes. Curr Opin. Biotechnol. 12: 574-586.
    • (2001) Curr Opin. Biotechnol , vol.12 , pp. 574-586
    • Fessner, W.D.1    Helaine, V.2
  • 4
    • 1942469509 scopus 로고    scopus 로고
    • Development of an efficient, scalable, aldolase-catalyzed process for enantioselective synthesis of statin intermediates
    • Greenberg, W. A., A. Varvak, S. R. Hanson, K. Wong, H. J. Huang, P. Chen, and M. J. Burk. 2004. Development of an efficient, scalable, aldolase-catalyzed process for enantioselective synthesis of statin intermediates. PNAS 101: 5788-5793.
    • (2004) PNAS , vol.101 , pp. 5788-5793
    • Greenberg, W.A.1    Varvak, A.2    Hanson, S.R.3    Wong, K.4    Huang, H.J.5    Chen, P.6    Burk, M.J.7
  • 5
    • 37049075862 scopus 로고
    • Stereospecific lysis of a range of β-hydroxy-α-amino acids catalyzed by a novel aldolase from S. amakusaensis
    • Herbert, R. B., B. Wilkinson, G. J. Ellames, and E. K. Kunec. 1993. Stereospecific lysis of a range of β-hydroxy-α-amino acids catalyzed by a novel aldolase from S. amakusaensis. J. Chem. Soc. Chem. Commun. 205-206.
    • (1993) J. Chem. Soc. Chem. Commun , pp. 205-206
    • Herbert, R.B.1    Wilkinson, B.2    Ellames, G.J.3    Kunec, E.K.4
  • 6
    • 0030931107 scopus 로고    scopus 로고
    • Isolation and characterization of D-threonine aldolase, a pyridoxal-5′-phosphate-dependent enzyme from Arthrobacter sp. DK-38
    • Kataoka, M., M. Ikemi, T. Morikawa, T. Miyoshi, K. Nishi, M. Wada, H. Yamada, and S. Shimizu. 1997. Isolation and characterization of D-threonine aldolase, a pyridoxal-5′-phosphate-dependent enzyme from Arthrobacter sp. DK-38. Eur J. Biochem. 248: 385-393.
    • (1997) Eur J. Biochem , vol.248 , pp. 385-393
    • Kataoka, M.1    Ikemi, M.2    Morikawa, T.3    Miyoshi, T.4    Nishi, K.5    Wada, M.6    Yamada, H.7    Shimizu, S.8
  • 7
    • 0032125729 scopus 로고    scopus 로고
    • Gene cloning, biochemical characterization and physiological role of a thermostable low-specificity L-threonine aldolase from Escherichia coli
    • Liu, J. Q., T. Dairi, N. Itoh, M. Kataoka, S. Shimizu, and H. Yamada. 1998. Gene cloning, biochemical characterization and physiological role of a thermostable low-specificity L-threonine aldolase from Escherichia coli. Eur. J. Biochem. 255: 220-226.
    • (1998) Eur. J. Biochem , vol.255 , pp. 220-226
    • Liu, J.Q.1    Dairi, T.2    Itoh, N.3    Kataoka, M.4    Shimizu, S.5    Yamada, H.6
  • 8
    • 7144257171 scopus 로고    scopus 로고
    • Low-specific L-threonine aldolase of Pseudomonas sp. NCIMB 10558: Purification, characterization and its application to β-hydroxy-α-amino acid synthesis
    • Liu, J. Q., S. Ito, T. Dairi, N. Itoh, S. Shimizu, and H. Yamada. 1998. Low-specific L-threonine aldolase of Pseudomonas sp. NCIMB 10558: Purification, characterization and its application to β-hydroxy-α-amino acid synthesis. Appl. Microbiol. Biotechnol. 49: 702-708.
    • (1998) Appl. Microbiol. Biotechnol , vol.49 , pp. 702-708
    • Liu, J.Q.1    Ito, S.2    Dairi, T.3    Itoh, N.4    Shimizu, S.5    Yamada, H.6
  • 10
    • 0033912395 scopus 로고    scopus 로고
    • Gene cloning and overexpression of low-specific D-threonine aldolase from Alcaligenes xylosoxidans and its application for production of a key intermediate for Parkinsonism drug
    • Liu, J. Q., M. Odani, T. Yasuoka, T. Dairi, N. Itoh, M. Kataoka, S. Shimizu, and H. Yamada. 2000. Gene cloning and overexpression of low-specific D-threonine aldolase from Alcaligenes xylosoxidans and its application for production of a key intermediate for Parkinsonism drug. Appl. Microbiol. Biotechnol. 54: 44-51.
    • (2000) Appl. Microbiol. Biotechnol , vol.54 , pp. 44-51
    • Liu, J.Q.1    Odani, M.2    Yasuoka, T.3    Dairi, T.4    Itoh, N.5    Kataoka, M.6    Shimizu, S.7    Yamada, H.8
  • 11
    • 0017911968 scopus 로고
    • Measurements of molecular weights by gel electrophoresis
    • Nielsen, T. B. and J. A. Reynolds. 1978. Measurements of molecular weights by gel electrophoresis. Methods Enzymol. 48: 3-10.
    • (1978) Methods Enzymol , vol.48 , pp. 3-10
    • Nielsen, T.B.1    Reynolds, J.A.2
  • 12
    • 34250158647 scopus 로고    scopus 로고
    • Ohashi, N, S. Nagata, K. Ishizumi, and K. Maeshima. 1984. Process for producing threo-3(3,4-dihydroxyphenyl)serine. European patent 0084928
    • Ohashi, N., S. Nagata, K. Ishizumi, and K. Maeshima. 1984. Process for producing threo-3(3,4-dihydroxyphenyl)serine. European patent 0084928.
  • 14
    • 0037436563 scopus 로고    scopus 로고
    • Dispelling the myths - biocatalysis in industrial synthesis
    • Schoemaker, H. E., D. Mink, and M. G. Wubbolts. 2003. Dispelling the myths - biocatalysis in industrial synthesis. Science 14: 1694-1697.
    • (2003) Science , vol.14 , pp. 1694-1697
    • Schoemaker, H.E.1    Mink, D.2    Wubbolts, M.G.3
  • 15
    • 33746930529 scopus 로고    scopus 로고
    • Increased refolding yield of disulfide bond bridged fab-toxin homodimers by the insertion of CH3 domains
    • Song, J. W., J. S. Won, Y. C. Lee, and M. Y. Choe. 2006. Increased refolding yield of disulfide bond bridged fab-toxin homodimers by the insertion of CH3 domains. J. Microbiol. Biotechnol. 16: 1104-1110.
    • (2006) J. Microbiol. Biotechnol , vol.16 , pp. 1104-1110
    • Song, J.W.1    Won, J.S.2    Lee, Y.C.3    Choe, M.Y.4
  • 16
    • 0036900263 scopus 로고    scopus 로고
    • The production of fine chemicals by biotransformation
    • Straathof, A. J., S. Panke, and A. Schmid. 2002. The production of fine chemicals by biotransformation. Curr. Opin. Biotechnol. 13: 548-556.
    • (2002) Curr. Opin. Biotechnol , vol.13 , pp. 548-556
    • Straathof, A.J.1    Panke, S.2    Schmid, A.3
  • 17
    • 0032500091 scopus 로고    scopus 로고
    • Pyridoxal-mediated enzyme system for aldol and retro-aldol reactions
    • Tanaka, F., M. Oda, and I. Fujii. 1998. Pyridoxal-mediated enzyme system for aldol and retro-aldol reactions. Tetrahedr. Lett. 39: 5057-5060.
    • (1998) Tetrahedr. Lett , vol.39 , pp. 5057-5060
    • Tanaka, F.1    Oda, M.2    Fujii, I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.