Literature DB >> 18997332

Crystallization and preliminary X-ray analysis of isomaltase from Saccharomyces cerevisiae.

Keizo Yamamoto1, Hideo Miyake, Masami Kusunoki, Shigeyoshi Osaki.   

Abstract

Isomaltase from Saccharomyces cerevisiae is an oligo-1,6-glucosidase that preferentially hydrolyzes isomaltose, with little activity towards isomaltotriose or longer oligosaccharides. An amino-acid sequence analysis of the isomaltase revealed that it belongs to glucoside hydrolase family 13. Recombinant isomaltase was purified and crystallized by the hanging-drop vapour-diffusion method with PEG 3350 as the precipitant. The crystals belonged to space group C2, with unit-cell parameters a = 95.67, b = 115.42, c = 61.77 A, beta = 91.17 degrees . X-ray diffraction data were collected to 1.35 A resolution from a single crystal on a synchrotron-radiation source.

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Year:  2008        PMID: 18997332      PMCID: PMC2581680          DOI: 10.1107/S174430910803114X

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  14 in total

Review 1.  Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes.

Authors:  E A MacGregor; S Janecek; B Svensson
Journal:  Biochim Biophys Acta       Date:  2001-03-09

2.  Nucleotide sequence of the dextran glucosidase (dexB) gene of Streptococcus mutans.

Authors:  R R Russell; J J Ferretti
Journal:  J Gen Microbiol       Date:  1990-05

3.  The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 A resolution: structural characterization of proline-substitution sites for protein thermostabilization.

Authors:  K Watanabe; Y Hata; H Kizaki; Y Katsube; Y Suzuki
Journal:  J Mol Biol       Date:  1997-05-30       Impact factor: 5.469

4.  Structural elements in dextran glucosidase responsible for high specificity to long chain substrate.

Authors:  Wataru Saburi; Haruhide Mori; Saori Saito; Masayuki Okuyama; Atsuo Kimura
Journal:  Biochim Biophys Acta       Date:  2006-01-30

5.  Characterization of dextran glucosidase (1,6-a-D-glucan glucohydrolase) of Streptococcus mitis.

Authors:  L Linder; M L Sund
Journal:  Caries Res       Date:  1981       Impact factor: 4.056

6.  Purification and characterization of maltase and alpha-methyl glucosidase from yeast.

Authors:  N A Khan; N R Eaton
Journal:  Biochim Biophys Acta       Date:  1967-09-12

7.  Purification and characterization of an alpha-glucosidase from Saccharomyces carlsbergensis.

Authors:  R B Needleman; H J Federoff; T R Eccleshall; B Buchferer; J Marmur
Journal:  Biochemistry       Date:  1978-10-31       Impact factor: 3.162

8.  Structure and possible catalytic residues of Taka-amylase A.

Authors:  Y Matsuura; M Kusunoki; W Harada; M Kakudo
Journal:  J Biochem       Date:  1984-03       Impact factor: 3.387

9.  Substrate recognition mechanism of alpha-1,6-glucosidic linkage hydrolyzing enzyme, dextran glucosidase from Streptococcus mutans.

Authors:  Hironori Hondoh; Wataru Saburi; Haruhide Mori; Masayuki Okuyama; Toshitaka Nakada; Yoshiki Matsuura; Atsuo Kimura
Journal:  J Mol Biol       Date:  2008-03-18       Impact factor: 5.469

10.  Val216 decides the substrate specificity of alpha-glucosidase in Saccharomyces cerevisiae.

Authors:  Keizo Yamamoto; Akifumi Nakayama; Yuka Yamamoto; Shiro Tabata
Journal:  Eur J Biochem       Date:  2004-08
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