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Crystallization and preliminary X-ray diffraction analysis of the invertase from Saccharomyces cerevisiae.

ABSTRACT: Saccharomyces cerevisiae invertase (ScInv) is an enzyme encoded by the SUC2 gene that releases ?-fructose from the nonreducing termini of various ?-D-fructofuranoside substrates. Its ability to produce 6-kestose by transglycosylation makes this enzyme an interesting research target for applications in industrial biotechnology. The native enzyme, which presents a high degree of oligomerization, was crystallized by vapour-diffusion methods. The crystals belonged to space group P3(1)21, with unit-cell parameters a=268.6, b=268.6, c=224.4?Å. The crystals diffracted to 3.3?Å resolution and gave complete data sets using a synchrotron X-ray source.

SUBMITTER: Sainz-Polo MA 

PROVIDER: S-EPMC3509983 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction analysis of the invertase from Saccharomyces cerevisiae.

Sainz-Polo M Angela MA   Lafraya Alvaro A   Polo Aitana A   Marín-Navarro Julia J   Polaina Julio J   Sanz-Aparicio Julia J  

Acta crystallographica. Section F, Structural biology and crystallization communications 20121119 Pt 12

Saccharomyces cerevisiae invertase (ScInv) is an enzyme encoded by the SUC2 gene that releases β-fructose from the nonreducing termini of various β-D-fructofuranoside substrates. Its ability to produce 6-kestose by transglycosylation makes this enzyme an interesting research target for applications in industrial biotechnology. The native enzyme, which presents a high degree of oligomerization, was crystallized by vapour-diffusion methods. The crystals belonged to space group P3(1)21, with unit-c  ...[more]

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