Subsite structure and action mode of the alpha-amylase from Thermoactinomyces vulgaris

The subsite structure of Thermoactinomyces vulgaris alpha -amylase was estimated from its action mode and rate parameters of hydrolysis on maltooligosaccharides. These results led to the conclusion that this alpha -amylase has six subsites with the catalytic site located between the third and fourth...

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Bibliographic Details
Published inAgricultural and biological chemistry Vol. 49; no. 10; pp. 2843 - 2846
Main Authors Sano, M, Sakano, Y, Kobayashi, T
Format Journal Article
LanguageEnglish
Published 1985
Subjects
alpha -amylase
amylases
substrates
Thermoactinomyces vulgaris
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Summary:The subsite structure of Thermoactinomyces vulgaris alpha -amylase was estimated from its action mode and rate parameters of hydrolysis on maltooligosaccharides. These results led to the conclusion that this alpha -amylase has six subsites with the catalytic site located between the third and fourth subsites from the non-reducing end side. Subsite affinities were calculated to be 0.38, 5.46, 2.72 and 0.23 kcal/mol for subsites 1, 2, 5 and 6, respectively, and the sum of the affinities of subsite 3 and 4 to be -3.41 kcal/mol. The unique action mode of this alpha -amylase on various substrates was interpreted in terms of the subsite structure.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0002-1369
1881-1280
DOI:10.1271/bbb1961.49.2843