1wo2

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{{STRUCTURE_1wo2| PDB=1wo2 | SCENE= }}
{{STRUCTURE_1wo2| PDB=1wo2 | SCENE= }}
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'''Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaacharides under the effect of the chloride ion'''
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===Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaacharides under the effect of the chloride ion===
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==Overview==
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Pig pancreatic alpha-amylase (PPA), an enzyme belonging to the alpha-amylase family, is involved in the degradation of starch. Like some other members of this family, PPA requires chloride to reach maximum activity levels. To further explain the mechanism of chloride activation, a crystal of wild-type PPA soaked with maltopentaose using a chloride-free buffer was analyzed by X-ray crystallography. A conspicuous reorientation of the acid/base catalyst Glu233 residue was found to occur. The structural results, along with kinetic data, show that the acid/base catalyst is maintained in the active site, in an optimum position, pointing toward the scissile bond-atom, due to the presence of chloride ions. The present study therefore explains the mechanism of PPA activation by chloride ions.
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The line below this paragraph, {{ABSTRACT_PUBMED_15736930}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15736930 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15736930}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Molecular basis of the effects of chloride ion on the acid-base catalyst in the mechanism of pancreatic alpha-amylase., Qian M, Ajandouz el H, Payan F, Nahoum V, Biochemistry. 2005 Mar 8;44(9):3194-201. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15736930 15736930]
Molecular basis of the effects of chloride ion on the acid-base catalyst in the mechanism of pancreatic alpha-amylase., Qian M, Ajandouz el H, Payan F, Nahoum V, Biochemistry. 2005 Mar 8;44(9):3194-201. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15736930 15736930]
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Enzyme-catalyzed condensation reaction in a mammalian alpha-amylase. High-resolution structural analysis of an enzyme-inhibitor complex., Qian M, Nahoum V, Bonicel J, Bischoff H, Henrissat B, Payan F, Biochemistry. 2001 Jun 26;40(25):7700-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11412124 11412124]
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Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaccharides., Payan F, Qian M, J Protein Chem. 2003 Apr;22(3):275-84. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12962327 12962327]
[[Category: Alpha-amylase]]
[[Category: Alpha-amylase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Qian, M.]]
[[Category: Qian, M.]]
[[Category: Beta-alpha-barrel]]
[[Category: Beta-alpha-barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:55:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:43:00 2008''

Revision as of 18:43, 27 July 2008

Image:1wo2.png

Template:STRUCTURE 1wo2

Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaacharides under the effect of the chloride ion

Template:ABSTRACT PUBMED 15736930

About this Structure

1WO2 is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

Reference

Molecular basis of the effects of chloride ion on the acid-base catalyst in the mechanism of pancreatic alpha-amylase., Qian M, Ajandouz el H, Payan F, Nahoum V, Biochemistry. 2005 Mar 8;44(9):3194-201. PMID:15736930

Enzyme-catalyzed condensation reaction in a mammalian alpha-amylase. High-resolution structural analysis of an enzyme-inhibitor complex., Qian M, Nahoum V, Bonicel J, Bischoff H, Henrissat B, Payan F, Biochemistry. 2001 Jun 26;40(25):7700-9. PMID:11412124

Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaccharides., Payan F, Qian M, J Protein Chem. 2003 Apr;22(3):275-84. PMID:12962327

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