Complexes of Thermoactinomyces vulgaris R-47 α-amylase 1 and pullulan model oligossacharides provide new insight into the mechanism for recognizing substrates with α-(1,6) glycosidic linkages-Reference-Cited by-同舟云学术

Complexes of Thermoactinomyces vulgaris R-47 α-amylase 1 and pullulan model oligossacharides provide new insight into the mechanism for recognizing substrates with α-(1,6) glycosidic linkages

Published:2005-11-10 Issue:23 Volume:272 Page:6145-6153
ISSN:1742-464X
Container-title:FEBS Journal
language:en
Short-container-title:

Author:

Abe Akemi,Yoshida Hiromi,Tonozuka Takashi,Sakano Yoshiyuki,Kamitori Shigehiro

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1742-4658.2005.05013.x/fullpdf

Reference32 articles.

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2. Comparison of primary structures and substrate specificities of two pullulan-hydrolyzing α-amylases, TVA I and TVA II, from Thermoactinomyces vulgaris R-47;Tonozuka;Biochem Biophys Acta,1995

3. Conversion of neopullulanase-α-amylase from Thermoactinomyces vulgaris R-47 into an amylopullulanase-type enzyme;Ibuka;J Biochem,1998

4. Crystal structures of Thermoactinomyces vulgaris R-47 α-amylase 1 (TVA I) at 1.6 Å resolution and α-amylase 2 (TVA II) at 2.3 Å resolution;Kamitori;J Mol Biol,2002

5. Complex structures of Thermoactinomyces vulgaris R-47 α-amylase 1 with malto-oligosaccharides demonstrate the role of domain N acting as a starch-binding domain;Abe;J Mol Biol,2004

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