Amylase: Difference between revisions

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<StructureSection load='' size='350' side='right' scene='Sandbox_182/Alpha-amylase/1' caption='Amylase complex with Ca+2 (green) and Na+ (purple) ions (PDB code [[1hvx]])'>
<StructureSection load='' size='350' side='right' scene='Sandbox_182/Alpha-amylase/1' caption='Amylase complex with Ca+2 (green) and Na+ (purple) ions (PDB code [[1hvx]])'>
=Introduction=
=Introduction=
Discovered and isolated by [http://en.wikipedia.org/wiki/Anselme_Payen Anselme Payen] in 1833, amylase was the first enzyme to be discovered<ref name="book">Yamamoto T.1988. Handbook of Amylases and Related Enzymes: Their Sources, Isolation Methods, Properties and Applications. Osaka Japan: Pergamon Press</ref>. Amylases are hydrolases, acting on α-1,4-glycosidic bonds<ref name="Path">PMID:9541387</ref>. They can be further subdivided into α,β and γ amylases<ref name="book"/>.'''α-Amylase''' (AAM) is an enzyme that acts as a catalyst for the hydrolysis of α-linked polysaccharides into α-anomeric products<ref name="Main">PMID:11226887</ref>. The enzyme can be derived from a variety of sources, each with different characteristics. α-Amylase found within the human body serves as the enzyme active in pancreatic juice and saliva<ref name="Path"/>. α-Amylase is not only essential in human physiology but has a number of important biotechnological functions in various processing industries.  '''β/α amylase''' (BAAM) is a precursor protein which is cleaved to form the β-amylase and α-amylase after secretion.  '''β amylase''' (BAM) acts at the non-reducing chain ends and liberate only β-maltose<ref>PMID:6168260</ref>.<br />
Discovered and isolated by [http://en.wikipedia.org/wiki/Anselme_Payen Anselme Payen] in 1833, amylase was the first enzyme to be discovered<ref name="book">Yamamoto T.1988. Handbook of Amylases and Related Enzymes: Their Sources, Isolation Methods, Properties and Applications. Osaka Japan: Pergamon Press</ref>. Amylases are hydrolases, acting on α-1,4-glycosidic bonds<ref name="Path">PMID:9541387</ref>. They can be further subdivided into α,β and γ amylases<ref name="book"/>.'''α-Amylase''' (AAM) is an enzyme that acts as a catalyst for the hydrolysis of α-linked polysaccharides into α-anomeric products<ref name="Main">PMID:11226887</ref>. The enzyme can be derived from a variety of sources, each with different characteristics. α-Amylase found within the human body serves as the enzyme active in pancreatic juice and saliva<ref name="Path"/>. α-Amylase is not only essential in human physiology but has a number of important biotechnological functions in various processing industries.  '''β/α amylase''' (BAAM) is a precursor protein which is cleaved to form the β-amylase and α-amylase after secretion.  '''β amylase''' (BAM) acts at the non-reducing chain ends and liberate only β-maltose<ref>PMID:6168260</ref>.  '''γ amylase''' (GAM) acts at the non-reducing chain ends of amylose and amylopectin and liberates glucose. <br />
For α-amylase see [[Raghad zoubi]]<br />
For α-amylase see [[Raghad zoubi]]<br />
See also [[Amylase (Hebrew)]].
See also [[Amylase (Hebrew)]].

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Andrea Gorrell, Shane Riley, Randi Woodbeck, David Canner, Michal Harel, Alexander Berchansky, Jaime Prilusky, Joel L. Sussman, Ann Taylor