1byd

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[[Image:1byd.png|left|200px]]
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{{STRUCTURE_1byd| PDB=1byd | SCENE= }}
{{STRUCTURE_1byd| PDB=1byd | SCENE= }}
===CRYSTAL STRUCTURES OF SOYBEAN BETA-AMYLASE REACTED WITH BETA-MALTOSE AND MALTAL: ACTIVE SITE COMPONENTS AND THEIR APPARENT ROLE IN CATALYSIS===
===CRYSTAL STRUCTURES OF SOYBEAN BETA-AMYLASE REACTED WITH BETA-MALTOSE AND MALTAL: ACTIVE SITE COMPONENTS AND THEIR APPARENT ROLE IN CATALYSIS===
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{{ABSTRACT_PUBMED_8011643}}
{{ABSTRACT_PUBMED_8011643}}
==About this Structure==
==About this Structure==
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1BYD is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BYD OCA].
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[[1byd]] is a 1 chain structure of [[Alpha-Amylase]] with sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BYD OCA].
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==See Also==
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*[[Alpha-Amylase|Alpha-Amylase]]
==Reference==
==Reference==
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<ref group="xtra">PMID:8011643</ref><references group="xtra"/>
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<ref group="xtra">PMID:008011643</ref><ref group="xtra">PMID:015794648</ref><references group="xtra"/>
[[Category: Beta-amylase]]
[[Category: Beta-amylase]]
[[Category: Glycine max]]
[[Category: Glycine max]]
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[[Category: Mikami, B.]]
[[Category: Mikami, B.]]
[[Category: Sacchettini, J C.]]
[[Category: Sacchettini, J C.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 13:43:53 2009''
 

Revision as of 18:48, 26 July 2012

Template:STRUCTURE 1byd

Contents

CRYSTAL STRUCTURES OF SOYBEAN BETA-AMYLASE REACTED WITH BETA-MALTOSE AND MALTAL: ACTIVE SITE COMPONENTS AND THEIR APPARENT ROLE IN CATALYSIS

Template:ABSTRACT PUBMED 8011643

About this Structure

1byd is a 1 chain structure of Alpha-Amylase with sequence from Glycine max. Full crystallographic information is available from OCA.

See Also

Reference

  • Mikami B, Degano M, Hehre EJ, Sacchettini JC. Crystal structures of soybean beta-amylase reacted with beta-maltose and maltal: active site components and their apparent roles in catalysis. Biochemistry. 1994 Jun 28;33(25):7779-87. PMID:8011643
  • Kang YN, Tanabe A, Adachi M, Utsumi S, Mikami B. Structural analysis of threonine 342 mutants of soybean beta-amylase: role of a conformational change of the inner loop in the catalytic mechanism. Biochemistry. 2005 Apr 5;44(13):5106-16. PMID:15794648 doi:10.1021/bi0476580

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