Binding of non-catalytic ATP to human hexokinase I highlights the structural components for enzyme-membrane association control.
Rosano, C., Sabini, E., Rizzi, M., Deriu, D., Murshudov, G., Bianchi, M., Serafini, G., Magnani, M., Bolognesi, M.(1999) Structure 7: 1427-1437
- PubMed: 10574795 
- DOI: https://doi.org/10.1016/s0969-2126(00)80032-5
- Primary Citation of Related Structures:  
1QHA - PubMed Abstract: 
Hexokinase I sets the pace of glycolysis in the brain, catalyzing the ATP-dependent phosphorylation of glucose. The catalytic properties of hexokinase I are dependent on product inhibition as well as on the action of phosphate. In vivo, a large fraction of hexokinase I is bound to the mitochondrial outer membrane, where the enzyme adopts a tetrameric assembly. The mitochondrion-bound hexokinase I is believed to optimize the ATP/ADP exchange between glucose phosphorylation and the mitochondrial oxidative phosphorylation reactions.
Organizational Affiliation: 
Dipartimento di Fisica - INFM, Centro Biotecnologie Avanzate - IST, Universita' di Genova, Genova, 10. I-16132, Italy.