1izj
From Proteopedia
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|PDB= 1izj |SIZE=350|CAPTION= <scene name='initialview01'>1izj</scene>, resolution 2.20Å | |PDB= 1izj |SIZE=350|CAPTION= <scene name='initialview01'>1izj</scene>, resolution 2.20Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
- | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1ji1|1JI1]], [[1izk|1IZK]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1izj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1izj OCA], [http://www.ebi.ac.uk/pdbsum/1izj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1izj RCSB]</span> | ||
}} | }} | ||
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[[Category: Sakano, Y.]] | [[Category: Sakano, Y.]] | ||
[[Category: Tonozuka, T.]] | [[Category: Tonozuka, T.]] | ||
- | [[Category: CA]] | ||
[[Category: alpha-beta barrele]] | [[Category: alpha-beta barrele]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:26:55 2008'' |
Revision as of 18:26, 30 March 2008
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, resolution 2.20Å | |||||||
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Ligands: | |||||||
Activity: | Alpha-amylase, with EC number 3.2.1.1 | ||||||
Related: | 1JI1, 1IZK
| ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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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