Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

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.


Journal article


J Mol Biol

Publication Date





573 - 576


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