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Protein engineering vol.5 no.3 pp.197-211, 1992 the α / β hydrolase fold.
| Content Provider | CiteSeerX |
|---|---|
| Author | Ollis, David L. Cheah, Eong Cyglerl, Miroslaw Dijkstra, Bauke Frolow, Felix Franken, Sybille M. Joseph Schrag, L. Sussman, Joel L. Verschueren, Koen H. G. Goldmans, Adrian |
| Abstract | We have identified a new protein fold-the a/β hydrolase fold-that is common to several hydrolytic enzymes of widely differing phylogenetic origin and catalytic function. The core of each enzyme is similar: an a/β sheet, not barrel, of eight β-sheets connected by a-helices. These enzymes have diverged from a common ancestor so as to preserve the arrangement of the catalytic residues, not the binding site. They all have a catalytic triad, the elements of which are borne on loops which are the best-conserved structural features in the fold. Only the histidine in the nucleophile- histidine- acid catalytic triad is completely conserved, with the nucleophile and acid loops accommodating more than one type of amino acid. The unique topological and sequence arrangement of the triad residues produces a catalytic triad which is, in a sense, a mirror-image of the serine protease catalytic triad. There are now four groups of enzymes which contain catalytic triads and which are related by convergent evolution towards a stable, useful active site: the eukaryotic serine proteases, the cysteine proteases, subtilisins and the a/β hydrolase fold enzymes. Key words: catalytic triad/evolution/hydrolases/protein |
| File Format | |
| Access Restriction | Open |
| Subject Keyword | Hydrolase Fold Catalytic Triad Protein Engineering Vol New Protein Fold-the Amino Acid Acid Loop Sequence Arrangement Hydrolase Fold Enzyme Eukaryotic Serine Protease Catalytic Residue Hydrolase Fold-that Convergent Evolution Catalytic Triad Evolution Serine Protease Catalytic Triad Nucleophile Histidine Acid Catalytic Triad Cysteine Protease Several Hydrolytic Enzyme Phylogenetic Origin Common Ancestor Best-conserved Structural Feature Useful Active Site Binding Site Catalytic Function |
| Content Type | Text |
