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Raghad zoubi
From Proteopedia
(Difference between revisions)
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| - | ==Ameylase== | + | '''Bold text'''==α Ameylase== |
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | ||
This is a default text for your page '''Raghad zoubi'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | This is a default text for your page '''Raghad zoubi'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
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== Introduction == | == Introduction == | ||
| - | The | + | The <scene name='60/609816/Alpha-amylase/1'>Alpha-amylase</scene> (EC 3.2.1.1 ) (CAS# 9014-71-5) (alternative names: 1,4-α-D-glucan glucanohydrolase; glycogenase) are calcium metalloenzymes, completely unable to function in the absence of calcium. By acting at random locations along the starch chain, α-amylase breaks down long-chain carbohydrates, ultimately yielding maltotriose and maltose from amylose, or maltose, glucose and "limit dextrin" from amylopectin. Because it can act anywhere on the substrate, α-amylase tends to be faster-acting than β-amylase. In animals, it is a major digestive enzyme, and its optimum pH is 6.7–7.0.[3] |
In human physiology, both the salivary and pancreatic amylases are α-amylases. | In human physiology, both the salivary and pancreatic amylases are α-amylases. | ||
Revision as of 13:46, 22 November 2014
Bold text==α Ameylase==
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
