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- W2082452555 abstract "Protein crystallography has determined the three-dimensional structures of 10 of the 13 enzymes of the glycolytic pathway. Diagrams and details of these enzyme structures are given in the paper. Most of the enzyme domains are variations and extensions of a many (4- 9)-stranded, predominantly or totally parallel, β-sheet that is shielded from solvent by α-helices (i.e. α/β structures). There are strong structural similarities between the domains of some, but not all, of the enzymes. In particular the dinucleotide binding fold of lactate dehydrogenase and the β-barrel of triose phosphate isomerase are found in other domains. General rules governing the topology and packing of α-helices against a β-sheet provide a basis for the combinatorial prediction of the tertiary fold of glycolytic domains from their amino acid sequence and observed secondary structure. The prediction algorithm demonstrates that there are severe restrictions on the number of possible structures. However, these restrictions do not fully explain some of the remarkable structural similarities between different enzymes that probably result from evolution from a common ancestor." @default.
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- W2082452555 date "1981-06-26" @default.
- W2082452555 modified "2023-09-27" @default.
- W2082452555 title "Analysis and prediction of structural motifs in the glycolytic enzymes" @default.
- W2082452555 cites W1590165017 @default.
- W2082452555 doi "https://doi.org/10.1098/rstb.1981.0071" @default.
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