Structural Insights into the Recovery of Aldolase Activity in N-Acetylneuraminic Acid Lyase by Replacement of the Catalytically Active Lysine with γ-Thialysine by Using a Chemical Mutagenesis Strategy

ChemBioChem

Volumn 14, Issue 4, 2013, Pages 474-481

  Timms, Nicole ^a   Windle, Claire L ^a   Polyakova, Anna ^a   Ault, James R ^a   Trinh, Chi H ^a   Pearson, Arwen R ^a   Nelson, Adam ^a   Berry, Alan ^a  

^a UNIVERSITY OF LEEDS   (United Kingdom)

Author keywords

Aldolases; Enzyme catalysis; N acetylneuraminic acid lyase; Thialysine; Unnatural amino acids

Indexed keywords

CYSTEINE; DEHYDROALANINE; ENZYME VARIANT; FRUCTOSE BISPHOSPHATE ALDOLASE; GAMMA THIALYSINE; LYASE; LYSINE; N ACETYLNEURAMINATE LYASE; PYRUVIC ACID; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; BACTERIAL GENE; CATALYSIS; CHEMICAL MUTAGENESIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ELECTROSPRAY MASS SPECTROMETRY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME MODIFICATION; ENZYME STRUCTURE; NANA GENE; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN PURIFICATION; SITE DIRECTED MUTAGENESIS; STAPHYLOCOCCUS AUREUS; STATIC ELECTRICITY; WILD TYPE;

CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; CYSTEINE; FRUCTOSE-BISPHOSPHATE ALDOLASE; KINETICS; LYSINE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; OXO-ACID-LYASES; STAPHYLOCOCCUS AUREUS;

EID: 84874387072     PISSN: 14394227     EISSN: 14397633     Source Type: Journal    
DOI: 10.1002/cbic.201200714     Document Type: Article

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