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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
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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
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28
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77955834470
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Ref 18
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Ref 18.
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77955788933
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For reports of other aldolases that catalyze non-stereoselective aldol reactions, see
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For reports of other aldolases that catalyze non-stereoselective aldol reactions, see
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36
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12744261280
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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
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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
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37
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38
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77955797150
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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.
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39
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77955819695
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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
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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.
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40
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77955823510
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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
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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.
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41
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77955805990
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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
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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.
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