Redesigning the active site of transaldolase TalB from escherichia coli: New variants with improved affinity towards nonphosphorylated substrates

ChemBioChem

Volumn 11, Issue 5, 2010, Pages 681-690

  Schneider, Sarah ^a   Gutiérrez, Mariana ^b   Sandalova, Tatyana ^c   Schneider, Gunter ^c   Clapés, Pere ^b   Sprenger, Georg A ^a   Samland, Anne K ^a  

^a UNIVERSITY OF STUTTGART   (Germany)

^b INSTITUTE OF ADVANCED CHEMISTRY OF CATALONIA IQAC CSIC   (Spain)

^c KAROLINSKA INSTITUTE   (Sweden)

Author keywords

Biocatalysis; Protein engineering; Saturation mutagenesis; Substrate specificity; Transaldolase

Indexed keywords

ARGININE; DIHYDROXYACETONE; FRUCTOSE; FRUCTOSE BISPHOSPHATE ALDOLASE; SERINE; TRANSALDOLASE;

ARTICLE; BINDING AFFINITY; BINDING SITE; CATALYSIS; ENZYME ACTIVITY; ENZYME STRUCTURE; ESCHERICHIA COLI; ISOMER; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

AMINO ACID SUBSTITUTION; BINDING SITES; BIOCATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DIHYDROXYACETONE; ESCHERICHIA COLI; FRUCTOSE; MUTAGENESIS, SITE-DIRECTED; PROTEIN ENGINEERING; SUBSTRATE SPECIFICITY; TRANSALDOLASE;

ESCHERICHIA COLI;

EID: 77949782018     PISSN: 14394227     EISSN: 14397633     Source Type: Journal    
DOI: 10.1002/cbic.200900720     Document Type: Article

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