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1: J Mol Biol. 1991 Jun 20;219(4):573-6.Click here to read Links

Activity and specificity of human aldolases.

Gamblin SJ, Davies GJ, Grimes JM, Jackson RM, Littlechild JA, Watson HC.

Department of Biochemistry, School of Medical Sciences, University of Bristol, U.K.

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.

PMID: 2056525 [PubMed - indexed for MEDLINE]

Structures reported by this article