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[[Image:1byb.png|left|200px]]
[[Image:1byb.png|left|200px]]


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{{STRUCTURE_1byb|  PDB=1byb  |  SCENE=  }}  
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===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}}


==About this Structure==
==About this Structure==
[[1byb]] is a 1 chain structure 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=1BYB OCA].  
[[1byb]] 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=1BYB OCA].  
 
==See Also==
*[[Alpha-Amylase|Alpha-Amylase]]


==Reference==
==Reference==
<ref group="xtra">PMID:8011643</ref><references group="xtra"/>
<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]]

Revision as of 06:47, 27 July 2012

File:1byb.png

Template:STRUCTURE 1byb

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

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

See Also

Reference

  1. 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
  2. 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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