Glucokinase: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 2: | Line 2: | ||
</span><br> | </span><br> | ||
=== | === <span>Refer</span>ences <span style="background-color: initial; font-size: 17.5296px;"> </span> === | ||
<references /> | <references /> | ||
=== [[Image: | === <ref>RCSB Protein Data Bank. 1V4T: Crystal Structure of Human GLucokinase Structure Summary Page. 2011. [cited: 5/12/2016] Available from: http://www.rcsb.org/pdb/explore.do?structureId=1v4t</ref>[[Image:Structure of Glucokinase.jpg|thumb]] === | ||
Revision as of 09:40, 5 December 2016
Glucokinase is an enzyme that phosphorylates glucose to become glucose-6-phosphate. It is an isozyme of hexokinase (hexokinase IV) that is present in hepatocytes. Compared to the other forms of hexokinase, glucokinase has a low affinity for glucose. This means that when glucose levels in the body are low, glucose isn't phosphorylated to become glucose-6-phosphate, and it goes to other tissues that have a greater need for the glucose. Furthermore, glucokinase is not inhibited by the product glucose-6-phosphate. This allows the enzyme to continually phosphorylate glucose, even when the concentration of glucose-6-phosphate is very high[1].
References
- ↑ Lehninger, A. L. Nelson, D. L. Cox, M. M. (2000) Principles of Biochemistry, 6th edition, New York: Worth Publishers. Chapter 15, page 578.
- ↑ RCSB Protein Data Bank. 1V4T: Crystal Structure of Human GLucokinase Structure Summary Page. 2011. [cited: 5/12/2016] Available from: http://www.rcsb.org/pdb/explore.do?structureId=1v4t