1byc
From Proteopedia
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{{STRUCTURE_1byc| PDB=1byc | SCENE= }} | {{STRUCTURE_1byc| PDB=1byc | 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== | ||
| - | [[1byc]] 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=1BYC OCA]. | + | [[1byc]] 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=1BYC OCA]. |
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| + | ==See Also== | ||
| + | *[[Alpha-Amylase|Alpha-Amylase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <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 10:37, 26 July 2012
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
1byc 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
