1izj

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[[Image:1izj.jpg|left|200px]]
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{{STRUCTURE_1izj| PDB=1izj | SCENE= }}
{{STRUCTURE_1izj| PDB=1izj | SCENE= }}
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'''Thermoactinomyces vulgaris R-47 alpha-amylase 1 mutant enzyme f313a'''
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===Thermoactinomyces vulgaris R-47 alpha-amylase 1 mutant enzyme f313a===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12860426 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12860426}}
==About this Structure==
==About this Structure==
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[[Category: Tonozuka, T.]]
[[Category: Tonozuka, T.]]
[[Category: Alpha-beta barrele]]
[[Category: Alpha-beta barrele]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 14:16:17 2008''

Revision as of 11:16, 1 July 2008

Image:1izj.png

Template:STRUCTURE 1izj

Thermoactinomyces vulgaris R-47 alpha-amylase 1 mutant enzyme f313a

Template:ABSTRACT PUBMED 12860426

About this Structure

1IZJ is a Single protein structure of sequence from Thermoactinomyces vulgaris. 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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