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Volumn 20, Issue 39, 2014, Pages 12572-12583

Engineering the Donor Selectivity of D-Fructose-6-Phosphate Aldolase for Biocatalytic Asymmetric Cross-Aldol Additions of Glycolaldehyde

Author keywords

aldol reaction; carbohydrates; enzyme catalysis; enzyme models; protein engineering

Indexed keywords

CARBOHYDRATES; CONDENSATION REACTIONS; EFFICIENCY; ENZYMES; FRUCTOSE; KETONES; MUTAGENESIS;

EID: 84982307297     PISSN: 09476539     EISSN: 15213765     Source Type: Journal    
DOI: 10.1002/chem.201403281     Document Type: Article
Times cited : (38)

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    • The involvement of residue Y131 as an acid–base catalyst has not been definitely proven, however a variety of evidence points towards its essential role in FSA catalysis., Alternatively, residue D6 could also be proposed as a potential acid–base catalyst on the basis of its homology to the essential D17 residue of TalB. Similarly the participation of a water molecule in proton transfer to and from the substrate/intermediates has been proposed for FSA,, as well as other class I aldolases, such as, -fructose-1,6 bisphosphate aldolase from rabbit muscle (RAMA), 2-deoxy-, -ribose 5-phosphate aldolase from, E. coli, (DERA), or 2-dehydro-3-deoxy-phosphogluconate aldolase from, E. coli, (KDPG),, and transaldolases (e.g., transaldolase from, Thermoplasma acidophilum, (TacTAL) or transaldolase from, E. coli, (TalB)
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.