1jf5
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(New page: 200px<br /><applet load="1jf5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jf5, resolution 3.20Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 16:03, 20 November 2007
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CRYSTAL STRUCTURE OF THERMOACTINOMYCES VULGARIS R-47 ALPHA-AMYLASE 2 MUTANT F286A
Overview
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.
About this Structure
1JF5 is a Single protein structure of sequence from Thermoactinomyces vulgaris with CA as ligand. Active as Neopullulanase, with EC number 3.2.1.135 Full crystallographic information is available from OCA.
Reference
Role of Phe286 in the recognition mechanism of cyclomaltooligosaccharides (cyclodextrins) by Thermoactinomyces vulgaris R-47 alpha-amylase 2 (TVAII). X-ray structures of the mutant TVAIIs, F286A and F286Y, and kinetic analyses of the Phe286-replaced mutant TVAIIs., Ohtaki A, Kondo S, Shimura Y, Tonozuka T, Sakano Y, Kamitori S, Carbohydr Res. 2001 Sep 7;334(4):309-13. PMID:11527532
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