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Volumn 26, Issue 3, 2013, Pages 181-186
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Modular exchange of substrate-binding loops alters both substrate and cofactor specificity in a member of the aldo-keto reductase superfamily
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Author keywords
aldo keto reductase; enzyme catalysis; oxidoreductases; protein stability; substrate specificity
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Indexed keywords
ALDO-KETO REDUCTASE;
ENZYME CATALYSIS;
OXIDO-REDUCTASES;
PROTEIN STABILITY;
SUBSTRATE SPECIFICITY;
ENZYME ACTIVITY;
GRAFTING (CHEMICAL);
SUBSTRATES;
ALCOHOL DEHYDROGENASE;
ALCOHOL DEHYDROGENASE D;
ALDEHYDE REDUCTASE;
ALDO KETO REDUCTASE;
GLYCERALDEHYDE;
OXIDOREDUCTASE;
UNCLASSIFIED DRUG;
ARTICLE;
BINDING AFFINITY;
CHIMERA;
CONTROLLED STUDY;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
ENZYME KINETICS;
ENZYME MODIFICATION;
ENZYME SPECIFICITY;
ENZYME STABILITY;
ENZYME SUBSTRATE COMPLEX;
HUMAN;
MUTATION;
NONHUMAN;
NUCLEOTIDE SEQUENCE;
PRIORITY JOURNAL;
PYROCOCCUS FURIOSUS;
SPECIES DIFFERENCE;
TURNOVER TIME;
ALCOHOL DEHYDROGENASE;
ALDEHYDE REDUCTASE;
AMINO ACID SEQUENCE;
GLYCERALDEHYDE;
HUMANS;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
MUTATION;
PROTEIN CONFORMATION;
PROTEIN ENGINEERING;
PROTEIN STABILITY;
PYROCOCCUS FURIOSUS;
SUBSTRATE SPECIFICITY;
TEMPERATURE;
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EID: 84874223993
PISSN: 17410126
EISSN: 17410134
Source Type: Journal
DOI: 10.1093/protein/gzs095 Document Type: Article |
Times cited : (25)
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References (27)
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