Mutual conversion of substrate specificities of Thermoactinomyces vulgaris R-47 alpha-amylases TVAI and TVAII by site-directed mutagenesis (Q27641684)

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Akihiro Iguchi

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Masahiro Mizuno

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Takashi Tonozuka

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Yoshiyuki Sakano

describes a project that uses

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publication date

22 July 2003

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published in

Carbohydrate Research

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volume

338

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issue

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page(s)

1553-8

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site-directed mutagenesis

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based on heuristic

inferred from title

cites work

Comparison of primary structures and substrate specificities of two pullulan-hydrolyzing alpha-amylases, TVA I and TVA II, from Thermoactinomyces vulgaris R-47.

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Conversion of neopullulanase-alpha-amylase from Thermoactinomyces vulgaris R-47 into an amylopullulanse-type enzyme.

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A convenient enzymatic synthesis of 4(2)-alpha-isomaltosylisomaltose using Thermoactinomyces vulgaris R-47 alpha-amylase II (TVA II)

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Structure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the alpha-amylase family

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Crystal structures and structural comparison of Thermoactinomyces vulgaris R-47 alpha-amylase 1 (TVAI) at 1.6 A resolution and alpha-amylase 2 (TVAII) at 2.3 A resolution

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Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVAII) hydrolyzing cyclodextrins and pullulan at 2.6 A resolution

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Studies on the hydrolyzing mechanism for cyclodextrins of Thermoactinomyces vulgaris R-47 alpha-amylase 2 (TVAII). X-ray structure of the mutant E354A complexed with beta-cyclodextrin, and kinetic analyses on cyclodextrins

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Structures of Thermoactinomyces vulgaris R-47 alpha-amylase II complexed with substrate analogues

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Crystal structure of a maltogenic amylase provides insights into a catalytic versatility

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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 [...]

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