Structure-based mutagenesis approaches toward expanding the substrate specificity of D-2-deoxyribose-5-phosphate aldolase.
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Sequential Aldol Condensation Catalyzed by Hyperthermophilic 2-Deoxy-D-Ribose-5-Phosphate AldolaseStructural insight for substrate tolerance to 2-deoxyribose-5-phosphate aldolase from the pathogen Streptococcus suisCreation of the first anomeric D/L-sugar kinase by means of directed evolutionIn vivo selection for the directed evolution of L-rhamnulose aldolase from L-rhamnulose-1-phosphate aldolase (RhaD).Overcoming inefficient cellobiose fermentation by cellobiose phosphorylase in the presence of xylose.Improving upon nature: active site remodeling produces highly efficient aldolase activity toward hydrophobic electrophilic substrates.Chemoenzymatic synthesis of building blocks for statin side chains.Redesigning Aldolase Stereoselectivity by Homologous Grafting.Extending enzyme molecular recognition with an expanded amino acid alphabet.Selection strategies for improved biocatalysts.Directed evolution of aldolases for exploitation in synthetic organic chemistryMutagenesis of the phosphate-binding pocket of KDPG aldolase enhances selectivity for hydrophobic substrates.Efficient production of a thermophilic 2-deoxyribose-5-phosphate aldolase in glucose-limited fed-batch cultivations of Escherichia coli by continuous lactose induction strategy.Characterization and application of a newly synthesized 2-deoxyribose-5-phosphate aldolase.Inter- and intramolecular aldol reactions promiscuously catalyzed by a proline-based tautomerase.Biosynthesis of 2-deoxysugars using whole-cell catalyst expressing 2-deoxy-D-ribose 5-phosphate aldolase.Microbial production of 4-hydroxybenzylidene acetone, the direct precursor of raspberry ketone.Linking coupled motions and entropic effects to the catalytic activity of 2-deoxyribose-5-phosphate aldolase (DERA)† †Electronic supplementary information (ESI) available: Further experimental and computational data. See DOI: 10.1039/c5sc03666f.Conformational Sampling of the Intrinsically Disordered C-Terminal Tail of DERA Is Important for Enzyme CatalysisEnzyme engineering toolbox – a ‘catalyst’ for change
P2860
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P2860
Structure-based mutagenesis approaches toward expanding the substrate specificity of D-2-deoxyribose-5-phosphate aldolase.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
Structure-based mutagenesis ap ...... xyribose-5-phosphate aldolase.
@en
type
label
Structure-based mutagenesis ap ...... xyribose-5-phosphate aldolase.
@en
prefLabel
Structure-based mutagenesis ap ...... xyribose-5-phosphate aldolase.
@en
P2093
P1476
Structure-based mutagenesis ap ...... xyribose-5-phosphate aldolase.
@en
P2093
Andreas Heine
Chi-Huey Wong
David P Clark
Grace DeSantis
Junjie Liu
P356
10.1016/S0968-0896(02)00429-7
P407
P577
2003-01-01T00:00:00Z