1jf5: Difference between revisions

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[[Image:1jf5.gif|left|200px]]
{{Seed}}
[[Image:1jf5.png|left|200px]]


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{{STRUCTURE_1jf5|  PDB=1jf5  |  SCENE=  }}  
{{STRUCTURE_1jf5|  PDB=1jf5  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF THERMOACTINOMYCES VULGARIS R-47 ALPHA-AMYLASE 2 MUTANT F286A'''
===CRYSTAL STRUCTURE OF THERMOACTINOMYCES VULGARIS R-47 ALPHA-AMYLASE 2 MUTANT F286A===




==Overview==
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Phe286 located in the center of the active site of alpha-amylase 2 from Thermoactinomyces vulgaris R-47 (TVAII) plays an important role in the substrate recognition for cyclomaltooligosaccharides (cyclodextrins). The X-ray structures of mutant TVAIIs with the replacement of Phe286 by Ala (F286A) and Tyr (F286Y) were determined at 3.2 A resolution. Their structures have no significant differences from that of the wild-type enzyme. The kinetic analyses of Phe286-replaced variants showed that the variants with non-aromatic residues, Ala (F286A) and Leu (F286L), have lower enzymatic activities than those with aromatic residues, Tyr (F286Y) and Trp (F286W), and the replacement of Phe286 affects enzymatic activities for CDs more than those for starch.
The line below this paragraph, {{ABSTRACT_PUBMED_11527532}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 11527532 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11527532}}


==About this Structure==
==About this Structure==
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[[Category: Tonozuka, T.]]
[[Category: Tonozuka, T.]]
[[Category: Beta/alpha barrel]]
[[Category: Beta/alpha barrel]]
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