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Volumn 132, Issue 33, 2010, Pages 11753-11758

Structurally informed site-directed mutagenesis of a stereochemically promiscuous aldolase to afford stereochemically complementary biocatalysts

Author keywords

[No Author keywords available]

Indexed keywords

ALDOL REACTIONS; ALDOLASES; CARBON-CARBON BOND FORMATION; DIASTEREOCONTROL; HYPERTHERMOPHILES; NATURAL SUBSTRATES; PYRUVATES; SITE DIRECTED MUTAGENESIS; STRUCTURAL INFORMATION; SULFOLOBUS SOLFATARICUS;

EID: 77955830263     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja104412a     Document Type: Article
Times cited : (40)

References (41)
  • 19
    • 77955788323 scopus 로고    scopus 로고
    • For a discussion of alternative directed evolution strategies based on combinatorial active-site saturation tests and iterative saturation mutagenesis that could have been used to evolve the stereoselectivity of this aldolase, see
    • For a discussion of alternative directed evolution strategies based on combinatorial active-site saturation tests and iterative saturation mutagenesis that could have been used to evolve the stereoselectivity of this aldolase, see
  • 27
    • 77955805642 scopus 로고    scopus 로고
    • This observation led to the discovery of a novel promiscuous metabolic pathway in S. solfataricus that was shown to metabolize d -glucose and d -galactose using the same series of enzymes in a pathway that may be indicative of the primitive state of the organism; See
    • This observation led to the discovery of a novel promiscuous metabolic pathway in S. solfataricus that was shown to metabolize d -glucose and d -galactose using the same series of enzymes in a pathway that may be indicative of the primitive state of the organism; See
  • 28
    • 77955834470 scopus 로고    scopus 로고
    • Ref 18
    • Ref 18.
  • 31
    • 77955788933 scopus 로고    scopus 로고
    • For reports of other aldolases that catalyze non-stereoselective aldol reactions, see
    • For reports of other aldolases that catalyze non-stereoselective aldol reactions, see
  • 36
    • 12744261280 scopus 로고    scopus 로고
    • This aldolase also catalyzes the highly stereoselective aldol reaction of pyruvate with l -glyceraldehyde acetonide to afford L-KDGal-5,6-acetonide in >95% de, see
    • This aldolase also catalyzes the highly stereoselective aldol reaction of pyruvate with l -glyceraldehyde acetonide to afford L-KDGal-5,6-acetonide in >95% de, see Lamble, H. J., Danson, M. J., Hough, D. W., and Bull, S. D. Chem. Commun. 2005, 124-126
    • (2005) Chem. Commun. , pp. 124-126
    • Lamble, H.J.1    Danson, M.J.2    Hough, D.W.3    Bull, S.D.4
  • 38
    • 77955797150 scopus 로고    scopus 로고
    • X-ray crystallographic analysis of D-2-deoxyribose-5-phosphate aldolase bound to d -2-deoxyribose-5-phosphate reveals a similar hydrogen bonding network between the hydroxyl residues of its bound sugar and conserved active site water molecules that play a critical role in catalysis and stereocontrol, see ref 15
    • X-ray crystallographic analysis of D-2-deoxyribose-5-phosphate aldolase bound to d -2-deoxyribose-5-phosphate reveals a similar hydrogen bonding network between the hydroxyl residues of its bound sugar and conserved active site water molecules that play a critical role in catalysis and stereocontrol, see ref 15.
  • 39
    • 77955819695 scopus 로고    scopus 로고
    • Berry and Nelson used our X-ray crystal structures of KDG-aldolase bound to D-KDG and D-KDGal to target the structurally analogous Thr-167 residue of N -acetylneuraminic acid lyase for mutation, which was shown to play a key role in determining the stereoselectivity of its aldol reactions for the preparation of diastereoisomeric sialic acid analogues, see refs 12 and 24
    • Berry and Nelson used our X-ray crystal structures of KDG-aldolase bound to D-KDG and D-KDGal to target the structurally analogous Thr-167 residue of N -acetylneuraminic acid lyase for mutation, which was shown to play a key role in determining the stereoselectivity of its aldol reactions for the preparation of diastereoisomeric sialic acid analogues, see refs 12 and 24.
  • 40
    • 77955823510 scopus 로고    scopus 로고
    • All aldolase catalyzed reactions were carried out using a large excess of pyruvate 1 that resulted in complete consumption of d -glyceraldehyde 2, thus, ensuring that any mixtures of D-KDGlu 3 and D-KDGal 4 were formed under kinetic control
    • All aldolase catalyzed reactions were carried out using a large excess of pyruvate 1 that resulted in complete consumption of d -glyceraldehyde 2, thus, ensuring that any mixtures of D-KDGlu 3 and D-KDGal 4 were formed under kinetic control.
  • 41
    • 77955805990 scopus 로고    scopus 로고
    • Spectroscopic data for D-KDGlu 3 and D-KDGal 4 were identical to those reported previously, see refs 18 and 25, and references contained therein
    • Spectroscopic data for D-KDGlu 3 and D-KDGal 4 were identical to those reported previously, see refs 18 and 25, and references contained therein.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.