1,4 glycosidic bonds: Difference between revisions

From The School of Biomedical Sciences Wiki
Jump to navigation Jump to search
Description of 1,4-glycosidic bonds
 
Nnjm2 (talk | contribs)
Lack of links. Poorly formatted references. All corrected.
Line 1: Line 1:
A 1,4-glycosidic bond is a covalent bond between the -OH group on carbon 1 of one sugar and the -OH group on carbon 4 of another sugar. This is a condensation reaction as a molecule of water is released. It can be broken by consuming a molecule of water in a hydrolysis reaction.1 The bond can either be in the α or β form depending on the position of the hydroxyl group on the carbon 1 involved in the bond. The α-1,4-glycosidic bond has the hydroxyl group pointing down. The β-1,4-glycosidic bond has the hydroxyl group pointing up.2
A 1,4-glycosidic bond is a covalent bond between the -OH group on [[carbon|carbon]] 1 of one sugar and the -OH group on carbon 4 of another [[sugar|sugar]]. This is a [[condensation reaction|condensation reaction]] as a [[molecule|molecule]] of [[water|water]] is released. It can be broken by consuming a molecule of water in a [[hydrolysis reaction|hydrolysis reaction]] <ref>Bruce, A., Johnson, A., Lewis, J., Raff, M., Roberts, K. and Walter, P. (2008). Molecular Biology of the Cell. 5th ed. New York: Garland Science. 56-57.</ref>.&nbsp;The bond can either be in the α or β form depending on the position of the [[hydroxyl group|hydroxyl group]] on the carbon 1 involved in the bond. The α-1,4-glycosidic bond has the hydroxyl group pointing down. The β-1,4-glycosidic bond has the hydroxyl group pointing up <ref>Bruce, A., Johnson, A., Lewis, J., Raff, M., Roberts, K. and Walter, P. (2008). Molecular Biology of the Cell. 5th ed. New York: Garland Science. 113.</ref>.&nbsp;1,4-glycosidic bonds can be found in both [[amylase|amylase]] and [[amylopectin|amylopectin]] in [[glycogen|glycogen]]. These linkages create branching in the [[polysaccharide|polysaccharide]]. Amylopectin and amylase are both readily hydrolysed by the [[α-amylase|α-amylase]] enzyme&nbsp;<ref>Berg JM, Tymoczko JL, Stryer L. (2002). Biochemistry. 5th ed. New York: W H Freeman. Section 11.2.2.</ref>.
1,4-glycosidic bonds can be found in both amylase and amylopectin in glycogen. These linkages create branching in the polysaccharide. Amylopectin and amylase are both readily hydrolysed by the α-amylase enzyme.3


References
=== References ===


1-Bruce, A., Johnson, A., Lewis, J., Raff, M., Roberts, K. and Walter, P. (2008). Molecular Biology of the Cell. 5th ed. New York: Garland Science. 56-57.
<references /><br>
 
2-Bruce, A., Johnson, A., Lewis, J., Raff, M., Roberts, K. and Walter, P. (2008). Molecular Biology of the Cell. 5th ed. New York: Garland Science. 113.
 
3-Berg JM, Tymoczko JL, Stryer L. (2002). Biochemistry. 5th ed. New York: W H Freeman. Section 11.2.2.

Revision as of 02:53, 24 November 2014

A 1,4-glycosidic bond is a covalent bond between the -OH group on carbon 1 of one sugar and the -OH group on carbon 4 of another sugar. This is a condensation reaction as a molecule of water is released. It can be broken by consuming a molecule of water in a hydrolysis reaction [1]. The bond can either be in the α or β form depending on the position of the hydroxyl group on the carbon 1 involved in the bond. The α-1,4-glycosidic bond has the hydroxyl group pointing down. The β-1,4-glycosidic bond has the hydroxyl group pointing up [2]. 1,4-glycosidic bonds can be found in both amylase and amylopectin in glycogen. These linkages create branching in the polysaccharide. Amylopectin and amylase are both readily hydrolysed by the α-amylase enzyme [3].

References

  1. Bruce, A., Johnson, A., Lewis, J., Raff, M., Roberts, K. and Walter, P. (2008). Molecular Biology of the Cell. 5th ed. New York: Garland Science. 56-57.
  2. Bruce, A., Johnson, A., Lewis, J., Raff, M., Roberts, K. and Walter, P. (2008). Molecular Biology of the Cell. 5th ed. New York: Garland Science. 113.
  3. Berg JM, Tymoczko JL, Stryer L. (2002). Biochemistry. 5th ed. New York: W H Freeman. Section 11.2.2.