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Volumn 46, Issue 24, 2007, Pages 4468-4470

Enhancing activity and controlling stereoselectivity in a designed PLP-dependent aldolase

Author keywords

Aldolases; Amino acids; Biocatalysis; Rational design; Stereoselectivity

Indexed keywords

AMINO ACIDS; ENZYMES; MUTAGENESIS; PHOSPHATES;

EID: 34250782571     PISSN: 14337851     EISSN: None     Source Type: Journal    
DOI: 10.1002/anie.200700710     Document Type: Article
Times cited : (38)

References (25)
  • 3
    • 0035471134 scopus 로고    scopus 로고
    • For recent reviews, see
    • For recent reviews, see: T. M. Penning, J. M. Jez, Chem. Rev. 2001, 101, 3027;
    • (2001) Chem. Rev , vol.101 , pp. 3027
    • Penning, T.M.1    Jez, J.M.2
  • 5
    • 34250872269 scopus 로고    scopus 로고
    • Angew. Chem. Int. Ed. 2007, 46, 3212.
    • (2007) Chem. Int. Ed , vol.46 , pp. 3212
    • Angew1
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    • 33750445263 scopus 로고    scopus 로고
    • Angew. Chem. Int. Ed. 2006, 45, 6824.
    • (2006) Chem. Int. Ed , vol.45 , pp. 6824
    • Angew1
  • 9
    • 34250765405 scopus 로고    scopus 로고
    • As seen for the Tyr265Ala variant, introduction of lysine at position 265 decreases the racemase activity of the enzyme by more than three orders of magnitude. Neither D- nor L-alanine was found to be a substrate for the Tyr265Lys mutant.
    • As seen for the Tyr265Ala variant, introduction of lysine at position 265 decreases the racemase activity of the enzyme by more than three orders of magnitude. Neither D- nor L-alanine was found to be a substrate for the Tyr265Lys mutant.
  • 11
    • 33845516860 scopus 로고    scopus 로고
    • For diastereoselective D-phenylserine synthases, see: J. Steinreiber, K. Fesko, C. Reisinger, M. Schürmann, F. van Assema, M. Wolberg, D. Mink, H. Griengl, Tetrahedron 2007, 63, 918.
    • For diastereoselective D-phenylserine synthases, see: J. Steinreiber, K. Fesko, C. Reisinger, M. Schürmann, F. van Assema, M. Wolberg, D. Mink, H. Griengl, Tetrahedron 2007, 63, 918.
  • 13
    • 4444276636 scopus 로고    scopus 로고
    • (2R,3S)-β-Phenylserine was purchased as a racemic mixture of D- and L-threo-β-phenylserine isomers. In the presence of the aldolases, only the D-isomer is converted to product (reference [3]). The erythro isomer, (2R,3R)- β-phenylserine, was synthesized from cinnamic acid in five steps following an asymmetric dihydroxylation strategy: H. C. Kolb, M. S. Van-Nieuwenhze, K. B. Sharpless, Chem. Rev. 1994, 94, 2483;
    • (2R,3S)-β-Phenylserine was purchased as a racemic mixture of D- and L-threo-β-phenylserine isomers. In the presence of the aldolases, only the D-isomer is converted to product (reference [3]). The erythro isomer, (2R,3R)- β-phenylserine, was synthesized from cinnamic acid in five steps following an asymmetric dihydroxylation strategy: H. C. Kolb, M. S. Van-Nieuwenhze, K. B. Sharpless, Chem. Rev. 1994, 94, 2483;
  • 23
  • 25
    • 34250770286 scopus 로고    scopus 로고
    • The models of the enzyme complexes are based on earlier hybrid docking and ab initio calculations performed with aldimines of all four α-methyl-β-phenylserine diastereomers at the Tyr265Ala active site (reference [4, The (2R,3S, and (2R,3R)-β- phenylserine derivatives were superimposed on their α-methyl counterparts, and the additional point mutations (Tyr265Lys, Met134Phe, and Ile352Trp) were introduced with the MacPymol software Delano Scientific LLC, 2006, manually choosing the rotamers that exhibit no steric clashes
    • The models of the enzyme complexes are based on earlier hybrid docking and ab initio calculations performed with aldimines of all four α-methyl-β-phenylserine diastereomers at the Tyr265Ala active site (reference [4]). The (2R,3S)- and (2R,3R)-β- phenylserine derivatives were superimposed on their α-methyl counterparts, and the additional point mutations (Tyr265Lys, Met134Phe, and Ile352Trp) were introduced with the MacPymol software (Delano Scientific LLC, 2006), manually choosing the rotamers that exhibit no steric clashes.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.