Amylase: Difference between revisions
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{{STRUCTURE_1hvx| PDB=1hvx |SCENE='Sandbox_182/Alpha-amylase/1'>TextToBeDisplayed</scene>}} | {{STRUCTURE_1hvx| PDB=1hvx |SCENE='Sandbox_182/Alpha-amylase/1'>TextToBeDisplayed</scene>}} | ||
=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 is an enzyme that acts as a catalyst for the hydrolysis of alpha-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 salvia<ref name="Path"/>. α-Amylase is not only essential in human physiology but has a number of important biotechnological functions in various processing industries. | 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 alpha-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 salvia<ref name="Path"/>. α-Amylase is not only essential in human physiology but has a number of important biotechnological functions in various processing industries. Beta/alpha amylase (BAAM) is a precursor protein which is cleaved to form the beta-amylase and alpha-amylase after secretion. | ||
=Structure<ref name="Main"/>= | =Structure<ref name="Main"/>= | ||
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===3D structures of Alpha-amylase=== | ===3D structures of Alpha-amylase=== | ||
''Updated May 2012'' | |||
===Alpha-amylase=== | ===Alpha-amylase=== | ||
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[[1pif]] – pAAM – pig | [[1pif]] – pAAM – pig | ||
[[6taa]], [[2aaa]] - AoAAM | [[6taa]], [[2aaa]] - AoAAM<br /> | ||
[[4aee]] – AAM catalytic domain – ''Staphylothermus marinus''<br /> | |||
[[3ren]] – AAM – ''Clostridium perfringens'' | |||
''AAM binary complexes'' | ''AAM binary complexes'' | ||
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[[1lf9]] - TtGAM + acarbose<br /> | [[1lf9]] - TtGAM + acarbose<br /> | ||
===Beta/alpha-amylase=== | |||
[[2laa]], [[2lab]] – BAAM – ''Paenibacillus polymyxa'' - NMR | |||
===Maltohexaose-producing amylase=== | ===Maltohexaose-producing amylase=== | ||