Triosephosphate isomerase: A highly evolved biocatalyst

Cellular and Molecular Life Sciences

Volumn 67, Issue 23, 2010, Pages 3961-3982

  Wierenga, R K ^a   Kapetaniou, E G ^a   Venkatesan, R ^a  

^a UNIVERSITY OF OULU   (Finland)

Author keywords

Active site strain; Biocatalysis; Enolising chemistry; Evolution; Protein dynamics; Proton shuttling

Indexed keywords

ASPARAGINE; GLUTAMINE; GLYCERALDEHYDE 3 PHOSPHATE; HISTIDINE; LYSINE; TRIOSEPHOSPHATE ISOMERASE;

ALLOSTERISM; BIOCATALYST; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; GLYCOLYSIS; ISOMERIZATION; LIGAND BINDING; NONHUMAN; REVIEW; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; CATALYSIS; CATALYTIC DOMAIN; DIHYDROXYACETONE PHOSPHATE; EVOLUTION, MOLECULAR; GLYCERALDEHYDE 3-PHOSPHATE; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; PROTEIN CONFORMATION; PROTEIN FOLDING; SEQUENCE ALIGNMENT; TRIOSE-PHOSPHATE ISOMERASE;

EID: 78651330006     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-010-0473-9     Document Type: Review

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