Molecular determinants of substrate recognition in thermostable alpha-glucosidases belonging to glycoside hydrolase family 13.

Molecular determinants of substrate recognition in thermostable alpha-glucosidases belonging to glycoside hydrolase family 13. Research Abstract Details 

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Molecular determinants of substrate recognition in thermostable alpha-glucosidases belonging to glycoside hydrolase family 13. Abstract Text:

Yoshiyuki Tsujimoto,Hiroyuki Tanaka,Reiko Takemura,Tomohiko Yokogawa,Atsushi Shimonaka,Hiroshi Matsui,Shin-ichi Kashiwabara,Kunihiko Watanabe,Yuzuru Suzuki,Yoshiyuki Tsujimoto,Hiroyuki Tanaka,Reiko Takemura,Tomohiko Yokogawa,Atsushi Shimonaka,Hiroshi Matsui,Shin-ichi Kashiwabara,Kunihiko Watanabe,Yuzuru Suzuki,Yoshiyuki Tsujimoto,Hiroyuki Tanaka,Reiko Takemura,Tomohiko Yokogawa,Atsushi Shimonaka,Hiroshi Matsui,Shin-ichi Kashiwabara,Kunihiko Watanabe,Yuzuru Suzuki,

Bacillus stearothermophilus alpha-1,4-glucosidase (BS) is highly specific for alpha-1,4-glucosidic bonds of maltose, maltooligosaccharides and alpha-glucans. Bacillus thermoglucosdasius oligo-1,6-glucosidase (BT) can specifically hydrolyse alpha-1,6 bonds of isomaltose, isomaltooligosaccharides and alpha-limit dextrin. The two enzymes have high homology in primary structure and belong to glycoside hydrolase family 13, which contain four conservative regions (I, II, III and IV). The two enzymes are suggested to be very close in structure, even though there are strict differences in their substrate specificities. Molecular determinants of substrate recognition in these two enzymes were analysed by site-directed mutagenesis. Twenty BT-based mutants and three BS-based mutants were constructed and characterized. Double substitutions in BT of Val200 -->Ala in region II and Pro258 -->Asn in region III caused an appearance of maltase activity compared with BS, and a large reduction of isomaltase activity. The values of k(0)/K(m) (s(-1). mM(-1)) of the BT-mutant for maltose and isomaltose were 69.0 and 15.4, respectively. We conclude that the Val/Ala200 and Pro/Asn258 residues in the alpha-glucosidases may be largely responsible for substrate recognition, although the regions I and IV also exert a slight influence. Additionally, BT V200A and V200A/P258N possessed high hydrolase activity towards sucrose.

Molecular determinants of substrate recognition in thermostable alpha-glucosidases belonging to glycoside hydrolase family 13. Publishing Authors By Initials

Y Tsujimoto,H Tanaka,R Takemura,T Yokogawa,A Shimonaka,H Matsui,S Kashiwabara,K Watanabe,Y Suzuki,Y Tsujimoto,H Tanaka,R Takemura,T Yokogawa,A Shimonaka,H Matsui,S Kashiwabara,K Watanabe,Y Suzuki,Y Tsujimoto,H Tanaka,R Takemura,T Yokogawa,A Shimonaka,H Matsui,S Kashiwabara,K Watanabe,Y Suzuki,

For similar enzymes and coenzymes: enzymes: hydrolases: glycoside hydrolases: glucosidases: alpha-glucosidases research abstracts see: enzymes and coenzymes: enzymes: hydrolases: glycoside hydrolases: glucosidases: alpha-glucosidases research

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Molecular determinants of substrate recognition in thermostable alpha-glucosidases belonging to glycoside hydrolase family 13. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 142

Page Numbers: 87-93

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 24

MONTH: 05

YEAR: 2007

Molecular determinants of substrate recognition in thermostable alpha-glucosidases belonging to glycoside hydrolase family 13. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Molecular determinants of substrate recognition in thermostable alpha-glucosidases belonging to glycoside hydrolase family 13. Keywords Mesh Terms:

KEYWORDS: alpha-Glucosidases

MESH TERMS: metabolism

Chemical & Substance for Abstract: Molecular determinants of substrate recognition in thermostable alpha-glucosidases belonging to glycoside hydrolase family 13. Information

Substance Name: alpha-Glucosidases

Registry Number: EC 3.2.1.20

Grant and Affiliation Information for Molecular determinants of substrate recognition in thermostable alpha-glucosidases belonging to glycoside hydrolase family 13.

AFFILIATION: Department of Applied Biochemistry, Kyoto Prefectural University, Shimogamo, Sakyo, Kyoto 606-8522, Japan. yoshi-t@kpu.ac.jp

Country: Japan

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MEDLINETA: J Biochem (Tokyo)

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