Activity and specificity of human aldolases.

Journal article

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.

Authors: Gamblin, S; Davies, G; Grimes, J; Jackson, R; Littlechild, J

• Publication status: Published
• Journal: Journal of molecular biology
• Volume: 219
• Issue: 4
• Pages: 573-576
• Publication date: 1991-06-01
• DOI: 10.1016/0022-2836(91)90650-u
• EISSN: 1089-8638
• ISSN: 0022-2836
• Language: English
• Keywords: Plasmodium; Sequence Alignment; Trypanosoma; Binding Sites; Substrate Specificity; Molecular Sequence Data; Protein Conformation; Fructose-Bisphosphate Aldolase; Animals; Isoenzymes; Humans; Fructosediphosphates; Amino Acid Sequence; Muscles; Structure-Activity Relationship; Models, Molecular