메뉴 건너뛰기




Volumn 51, Issue 5, 1999, Pages 586-591

A new route to L-threo-3-[4-(methylthio)phenylserine], a key intermediate for the synthesis of antibiotics: Recombinant low-specificity D- threonine aldolase-catalyzed stereospecific resolution

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTIC AGENT; BACTERIAL ENZYME; FLORFENICOL; FRUCTOSE BISPHOSPHATE ALDOLASE; PHENYLSERINE; PRODRUG; THIAMPHENICOL; THREONINE;

EID: 0033065569     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002530051436     Document Type: Article
Times cited : (37)

References (22)
  • 2
    • 0031263239 scopus 로고    scopus 로고
    • Antimicrobial therapy of bovine respiratory disease
    • Apley M (1997) Antimicrobial therapy of bovine respiratory disease. Vet Clin North Am Food Animal Pract 13: 562-565
    • (1997) Vet Clin North Am Food Animal Pract , vol.13 , pp. 562-565
    • Apley, M.1
  • 3
    • 0023160460 scopus 로고
    • High-performance liquid chromatographic determination of enantiomeric amino acids and amino alcohols after derivatization with o-phthaldialdehyde and various chiral mercaptans
    • Buck RH, Krummen K (1987) High-performance liquid chromatographic determination of enantiomeric amino acids and amino alcohols after derivatization with o-phthaldialdehyde and various chiral mercaptans. J Chromatogr 387: 255-265
    • (1987) J Chromatogr , vol.387 , pp. 255-265
    • Buck, R.H.1    Krummen, K.2
  • 5
    • 0023685171 scopus 로고
    • New strategy for racemization of 2-amino-1,3-propanediols, key intermediates for the synthesis of antibiotic drugs
    • Giordano C, Caviccholi S, Levi S, Villia M (1988) New strategy for racemization of 2-amino-1,3-propanediols, key intermediates for the synthesis of antibiotic drugs. Tetrahedron Lett 29: 5561-5564
    • (1988) Tetrahedron Lett , vol.29 , pp. 5561-5564
    • Giordano, C.1    Caviccholi, S.2    Levi, S.3    Villia, M.4
  • 6
    • 0026345845 scopus 로고
    • Direct conversion of (1S, 2S-2-amino-1-[(4-methylthio)phenyl]-1,3-propanediol into its enantiomer for efficient synthesis of thiamphenicol and florfenicol
    • Giordano C, Caviccholi S, Levi S, Villia M (1991) Direct conversion of (1S, 2S)-2-amino-1-[(4-methylthio)phenyl]-1,3-propanediol into its enantiomer for efficient synthesis of thiamphenicol and florfenicol. J Org Chem 56: 6114-6118
    • (1991) J Org Chem , vol.56 , pp. 6114-6118
    • Giordano, C.1    Caviccholi, S.2    Levi, S.3    Villia, M.4
  • 7
    • 37049075862 scopus 로고
    • Stereospecific lysis of a range of β-hydroxy-α-amino acids catalysed by a novel aldolase from Streptomyces amakusaensis
    • Herbert RB, Wilkinson B, Ellames GJ, Kunec EK (1993) Stereospecific lysis of a range of β-hydroxy-α-amino acids catalysed by a novel aldolase from Streptomyces 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
  • 8
    • 0032338508 scopus 로고    scopus 로고
    • Synthesis of 4-sulfur-substituted (2S,3R)-3-phenylserines by enzymatic resolution. Enantiopure precursors for thiamphenicol and florfenicol
    • Kaptein B, Dooren TJGM, Boesten WHJ, Sonke T, Duchateau ALL, Broxterman QB, Kamphuis J (1998) Synthesis of 4-sulfur-substituted (2S,3R)-3-phenylserines by enzymatic resolution. Enantiopure precursors for thiamphenicol and florfenicol. Org Proc Res Dev 2: 10-17
    • (1998) Org Proc Res Dev , vol.2 , pp. 10-17
    • Kaptein, B.1    Tjgm, D.2    Boesten, W.H.J.3    Sonke, T.4    Duchateau, A.L.L.5    Broxterman, Q.B.6    Kamphuis, J.7
  • 9
    • 0030872722 scopus 로고    scopus 로고
    • Purification and characterization of L-allo-threonine aldolase of Aeromonas jandaei
    • Kataoka M, Wada M, Nishi K, Yamada H, Shimizu S (1997a) Purification and characterization of L-allo-threonine aldolase of Aeromonas jandaei. FEMS Microbiol Lett 151: 245-248
    • (1997) FEMS Microbiol Lett , vol.151 , pp. 245-248
    • Kataoka, M.1    Wada, M.2    Nishi, K.3    Yamada, H.4    Shimizu, S.5
  • 10
    • 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, Ikemi, Morikawa T, Miyoshi T, Nishi K, Wada M, Yamada H, Shimizu S (1997b) 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.T.2    Miyoshi, T.3    Nishi, K.4    Wada, M.5    Yamada, H.6    Shimizu, S.7
  • 11
    • 0015497816 scopus 로고
    • Threonine aldolase from Candida humicola: Purification, crystallization and properties
    • Kumagai H, Nagatae T, Yoshida H, Yamada H (1972) Threonine aldolase from Candida humicola: purification, crystallization and properties. Biochim Biophys Acta 258: 779-790
    • (1972) Biochim Biophys Acta , vol.258 , pp. 779-790
    • Kumagai, H.1    Nagatae, T.2    Yoshida, H.3    Yamada, H.4
  • 12
    • 0032489407 scopus 로고    scopus 로고
    • Diastereoselective synthesis of γ-hydroxy-β-amino alcohols and (2S, 3S)-β-hydroxyleucine from chiral D-(N,N-dibenzylamino)serine (TBDMS) aldehyde
    • Laib T, Chastanet J, Zhu J (1998) Diastereoselective synthesis of γ-hydroxy-β-amino alcohols and (2S, 3S)-β-hydroxyleucine from chiral D-(N,N-dibenzylamino)serine (TBDMS) aldehyde. J Org Chem 63: 1709-1713
    • (1998) J Org Chem , vol.63 , pp. 1709-1713
    • Laib, T.1    Chastanet, J.2    Zhu, J.3
  • 13
    • 0031009927 scopus 로고    scopus 로고
    • L-allo-Threonine aldolase from Aeromonas jandaei DK-39: Gene cloning, nucleotide sequencing, and idetification of the pyridoxal-5′-phosphate-binding lysine residue by site-directed mutagenesis
    • Liu JQ, Dairi T, Kataoka M, Shimizu S, Yamada H (1997a) L-allo-Threonine aldolase from Aeromonas jandaei DK-39: gene cloning, nucleotide sequencing, and idetification of the pyridoxal-5′-phosphate-binding lysine residue by site-directed mutagenesis. J Bacteriol 179: 3555-3560
    • (1997) J Bacteriol , vol.179 , pp. 3555-3560
    • Liu, J.Q.1    Dairi, T.2    Kataoka, M.3    Shimizu, S.4    Yamada, H.5
  • 14
    • 0030980668 scopus 로고    scopus 로고
    • GLY1 gene of Saccharomyces cerevisiae encodes a low-specificity L-threonine aldolase that catalyzes cleavage of L-allo-Threonine and L-threonine to glycine: Expression of the gene in Escherichia coli and purification and characterization of the enzyme
    • Liu JQ, Nakata S, Dairi T, Misono H, Shimizu S, Yamada H (1997b) GLY1 gene of Saccharomyces cerevisiae encodes a low-specificity L-threonine aldolase that catalyzes cleavage of L-allo-threonine and L-threonine to glycine: expression of the gene in Escherichia coli and purification and characterization of the enzyme. Eur J Biochem 245: 289-293
    • (1997) Eur J Biochem , vol.245 , pp. 289-293
    • Liu, J.Q.1    Nakata, S.2    Dairi, T.3    Misono, H.4    Shimizu, S.5    Yamada, H.6
  • 15
    • 0032479296 scopus 로고    scopus 로고
    • A novel metal-activated pyridoxal enzyme with a unique primary structure, low-specificity D-threonine aldolase from Arthrobacter sp. strain DK-38: Molecular cloning and cofactor characterization
    • Liu JQ, Dairi T, Itoh N, Kataoka M, Shimizu S, Yamada H (1998a) A novel metal-activated pyridoxal enzyme with a unique primary structure, low-specificity D-threonine aldolase from Arthrobacter sp. strain DK-38: molecular cloning and cofactor characterization. J Biol Chem 273: 16678-16685
    • (1998) J Biol Chem , vol.273 , pp. 16678-16685
    • Liu, J.Q.1    Dairi, T.2    Itoh, N.3    Kataoka, M.4    Shimizu, S.5    Yamada, H.6
  • 16
    • 0032125729 scopus 로고    scopus 로고
    • Gene cloning, biochemical characterization and physiological role of a thermostable low-specificity L-threonine aldolase from Escherichia coli
    • Liu JQ, Dairi T, Itoh N, Kataoka M, Shimizu S, Yamada H (1998b) Gene cloning, biochemical characterization and physiological role of a thermostable low-specificity L-threonine aldolase from Escherichia coli. Eur J Biochem 254: 220-226
    • (1998) Eur J Biochem , vol.254 , pp. 220-226
    • Liu, J.Q.1    Dairi, T.2    Itoh, N.3    Kataoka, M.4    Shimizu, S.5    Yamada, H.6
  • 17
    • 7144257171 scopus 로고    scopus 로고
    • Low-specificity l-threonine aldolase of Pseudomonas sp. NCIMB 10558: Purification, characterization and its application to β-hydroxy-α-amino acids syntheses
    • Liu JQ, Dairi T, Itoh N, Kataoka M, Shimizu S, Yamada H (1998c) Low-specificity L-threonine aldolase of Pseudomonas sp. NCIMB 10558: purification, characterization and its application to β-hydroxy-α-amino acids syntheses. Appl Microbiol Biotechnol 49: 702-708
    • (1998) Appl Microbiol Biotechnol , vol.49 , pp. 702-708
    • Liu, J.Q.1    Dairi, T.2    Itoh, N.3    Kataoka, M.4    Shimizu, S.5    Yamada, H.6
  • 18
    • 0030200671 scopus 로고    scopus 로고
    • The metabolism of L-DOPA and L-threo-3,4-dihydroxyphenylserine and their effects on monoamines in the human brain: Analysis of the intraventricular fluid from parkinsonian patients
    • Maruyama W, Naoi M, Narabayashi H (1996) The metabolism of L-DOPA and L-threo-3,4-dihydroxyphenylserine and their effects on monoamines in the human brain: analysis of the intraventricular fluid from parkinsonian patients. J Neuro sci 139: 141-148
    • (1996) J Neuro Sci , vol.139 , pp. 141-148
    • Maruyama, W.1    Naoi, M.2    Narabayashi, H.3
  • 20
    • 0021881054 scopus 로고
    • Serine hydroxymethyltransferase from Escherichia coli: Purification and properties
    • Schirch V, Hopkins S, Villar E, Angelaccio S (1985) Serine hydroxymethyltransferase from Escherichia coli: purification and properties. J Bacteriol 163: 1-7
    • (1985) J Bacteriol , vol.163 , pp. 1-7
    • Schirch, V.1    Hopkins, S.2    Villar, E.3    Angelaccio, S.4
  • 22
    • 0001115196 scopus 로고
    • Formation of threonine aldolase by bacteria and yeasts
    • Yamada H, Kumagai H, Nagate T, Yoshida H (1971) Formation of threonine aldolase by bacteria and yeasts. Agric Biol Chem 35: 1340-1345
    • (1971) Agric Biol Chem , vol.35 , pp. 1340-1345
    • Yamada, H.1    Kumagai, H.2    Nagate, T.3    Yoshida, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.