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The structure of the type I fructose 1,6-bisphosphate aldolase from human muscle has been extended from 3 A to 2 A resolution. The improvement in the resulting electron density map is such that the 20 or so C-terminal residues, known to be associated with activity and isozyme specificity, have been located. The side-chain of the Schiff's base-forming lysine 229 is located towards the centre of an eight-stranded beta-barrel type structure. The C-terminal "tail" extends from the rim of the beta-barrel towards lysine 229, thus forming part of the active site of the enzyme. This structural arrangement appears to explain the difference in activity and specificity of the three tissue-specific human aldolases and helps with our understanding of the type I aldolase reaction mechanism.

Type

Journal article

Journal

J Mol Biol

Publication Date

20/06/1991

Volume

219

Pages

573 - 576

Keywords

Amino Acid Sequence, Animals, Binding Sites, Fructose-Bisphosphate Aldolase, Fructosediphosphates, Humans, Isoenzymes, Models, Molecular, Molecular Sequence Data, Muscles, Plasmodium, Protein Conformation, Sequence Alignment, Structure-Activity Relationship, Substrate Specificity, Trypanosoma