Title |
Sugar recognition by human galactokinase
|
---|---|
Published in |
BMC Molecular and Cell Biology, November 2003
|
DOI | 10.1186/1471-2091-4-16 |
Pubmed ID | |
Authors |
David J Timson, Richard J Reece |
Abstract |
Galactokinase catalyses the first committed step of galactose catabolism in which the sugar is phosphorylated at the expense of MgATP. Recent structural studies suggest that the enzyme makes several contacts with galactose--five side chain and two main chain hydrogen bonds. Furthermore, it has been suggested that inhibition of galactokinase may help sufferers of the genetic disease classical galactosemia which is caused by defects in another enzyme of the pathway galactose-1-phosphate uridyl transferase. Galactokinases from different sources have a range of substrate specificities and a diversity of kinetic mechanisms. Therefore only studies on the human enzyme are likely to be of value in the design of therapeutically useful inhibitors. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
United States | 1 | 3% |
Unknown | 30 | 97% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Bachelor | 7 | 23% |
Student > Ph. D. Student | 4 | 13% |
Student > Master | 4 | 13% |
Professor | 2 | 6% |
Researcher | 2 | 6% |
Other | 2 | 6% |
Unknown | 10 | 32% |
Readers by discipline | Count | As % |
---|---|---|
Agricultural and Biological Sciences | 8 | 26% |
Biochemistry, Genetics and Molecular Biology | 6 | 19% |
Chemistry | 3 | 10% |
Medicine and Dentistry | 3 | 10% |
Unknown | 11 | 35% |