Activity and specificity of human aldolases.
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Gamblin SJ, Davies GJ, Grimes JM, Jackson RM, Littlechild JA, Watson HC
Activity and specificity of human aldolases.
J Mol Biol. 1991 Jun 20;219(4):573-6.
- PubMed ID
- 2056525 [ View in PubMed]
- Abstract
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.