Using site-saturation mutagenesis to explore mechanism and substrate specificity in thiamin diphosphate-dependent enzymes

FEBS Journal

Volumn 280, Issue 24, 2013, Pages 6395-6411

  Andrews, Forest H ^a   McLeish, Michael J ^a  

^a INDIANA UNIVERSITY   (United States)

Author keywords

2 oxoglutarate decarboxylase; benzoylformate; carboligation; decarboxylase; directed evolution; enantiospecificity; MenD; pyruvate; ThDP; transketolase

Indexed keywords

2 OXOGLUTARATE DECARBOXYLASE; 2 OXOGLUTARIC ACID; 2 OXOVALERATE; 2 SUCCINYL 5 ENOLPYRUVYL 6 HYDROXY 3 CYCLOHEXENE 1 CARBOXYLATE SYNTHASE; 2 SUCCINYL 6 HYDROXY 2,4 CYCLOHEXADIENE 1 CARBOXYLATE; 3 METHOXYBENZALDEHYDE; ALANINE; ASPARTIC ACID; BENZALDEHYDE DERIVATIVE; BENZOYLFORMATE DECARBOXYLASE; BETA HYDROXYPYRUVATE; CARBON; CARBON DIOXIDE; CARBOXYLIC ACID DERIVATIVE; CARBOXYLYASE; COCARBOXYLASE; HISTIDINE; ISOLEUCINE; LEUCINE; OXOGLUTARATE DEHYDROGENASE; PYRUVATE DECARBOXYLASE; PYRUVIC ACID DERIVATIVE; RIBOSE 5 PHOSPHATE; SERINE; SUCCINYL COENZYME A; SYNTHETASE; THREONINE; TRANSKETOLASE; UNCLASSIFIED DRUG; VALERIC ACID DERIVATIVE;

AMINO ACID SUBSTITUTION; CARBON SOURCE; CATALYSIS; CITRIC ACID CYCLE; CLOSTRIDIUM ACETOBUTYLICUM; CRYSTAL STRUCTURE; DECARBOXYLATION; ENANTIOSELECTIVITY; ENZYME ACTIVATION; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME MECHANISM; ENZYME PHOSPHORYLATION; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; HYDROPHOBICITY; MUTAGENESIS; NONHUMAN; NUCLEOPHILICITY; PRIORITY JOURNAL; PROTEIN CLEAVAGE; PROTEIN FUNCTION; REVIEW; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES PASTORIANUS; SITE SATURATION MUTAGENESIS; STEREOCHEMISTRY; STRUCTURE ANALYSIS; THERMOSTABILITY;

2-OXOGLUTARATE DECARBOXYLASE; BENZOYLFORMATE; CARBOLIGATION; DECARBOXYLASE; DIRECTED EVOLUTION; ENANTIOSPECIFICITY; MEND; PYRUVATE; THDP; TRANSKETOLASE;

ANIMALS; CARBOXY-LYASES; CATALYSIS; HUMANS; MUTAGENESIS, SITE-DIRECTED; MUTATION; STEREOISOMERISM; THIAMINE PYROPHOSPHATE;

EID: 84889631836     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12459     Document Type: Review

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