1izj
From Proteopedia
(New page: 200px<br /><applet load="1izj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1izj, resolution 2.20Å" /> '''Thermoactinomyces vu...) |
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| - | [[Image:1izj.jpg|left|200px]]<br /><applet load="1izj" size=" | + | [[Image:1izj.jpg|left|200px]]<br /><applet load="1izj" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1izj, resolution 2.20Å" /> | caption="1izj, resolution 2.20Å" /> | ||
'''Thermoactinomyces vulgaris R-47 alpha-amylase 1 mutant enzyme f313a'''<br /> | '''Thermoactinomyces vulgaris R-47 alpha-amylase 1 mutant enzyme f313a'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Thermoactinomyces vulgaris R-47 produces two alpha-amylases, TVAI and | + | Thermoactinomyces vulgaris R-47 produces two alpha-amylases, TVAI and TVAII, differing in substrate specificity from each other. TVAI favors high-molecular-weight substrates like starch, and scarcely hydrolyzes cyclomaltooligosaccharides (cyclodextrins) with a small cavity. TVAII favors low-molecular-weight substrates like oligosaccharides, and can efficiently hydrolyze cyclodextrins with various sized cavities. To understand the relationship between the structure and substrate specificity of these enzymes, we precisely examined the roles of key residues for substrate recognition by X-ray structural and kinetic parameter analyses of mutant enzymes and successfully obtained mutants in which the substrate specificity of each enzyme is partially converted into that of another. |
==About this Structure== | ==About this Structure== | ||
| - | 1IZJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] Full crystallographic information is available from [http:// | + | 1IZJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IZJ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: alpha-beta barrele]] | [[Category: alpha-beta barrele]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:17:22 2008'' |
Revision as of 11:17, 21 February 2008
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Thermoactinomyces vulgaris R-47 alpha-amylase 1 mutant enzyme f313a
Overview
Thermoactinomyces vulgaris R-47 produces two alpha-amylases, TVAI and TVAII, differing in substrate specificity from each other. TVAI favors high-molecular-weight substrates like starch, and scarcely hydrolyzes cyclomaltooligosaccharides (cyclodextrins) with a small cavity. TVAII favors low-molecular-weight substrates like oligosaccharides, and can efficiently hydrolyze cyclodextrins with various sized cavities. To understand the relationship between the structure and substrate specificity of these enzymes, we precisely examined the roles of key residues for substrate recognition by X-ray structural and kinetic parameter analyses of mutant enzymes and successfully obtained mutants in which the substrate specificity of each enzyme is partially converted into that of another.
About this Structure
1IZJ is a Single protein structure of sequence from Thermoactinomyces vulgaris with as ligand. Active as Alpha-amylase, with EC number 3.2.1.1 Full crystallographic information is available from OCA.
Reference
Mutual conversion of substrate specificities of Thermoactinomyces vulgaris R-47 alpha-amylases TVAI and TVAII by site-directed mutagenesis., Ohtaki A, Iguchi A, Mizuno M, Tonozuka T, Sakano Y, Kamitori S, Carbohydr Res. 2003 Jul 22;338(15):1553-8. PMID:12860426
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