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Activity and specificity of human aldolases.
- Source :
-
Journal of molecular biology [J Mol Biol] 1991 Jun 20; Vol. 219 (4), pp. 573-6. - Publication Year :
- 1991
-
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.
- Subjects :
- Amino Acid Sequence
Animals
Binding Sites
Fructose-Bisphosphate Aldolase metabolism
Fructosediphosphates metabolism
Humans
Isoenzymes metabolism
Models, Molecular
Molecular Sequence Data
Muscles enzymology
Plasmodium enzymology
Protein Conformation
Sequence Alignment
Structure-Activity Relationship
Substrate Specificity
Trypanosoma enzymology
Fructose-Bisphosphate Aldolase chemistry
Isoenzymes chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0022-2836
- Volume :
- 219
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Journal of molecular biology
- Publication Type :
- Academic Journal
- Accession number :
- 2056525
- Full Text :
- https://doi.org/10.1016/0022-2836(91)90650-u