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- Title
Crystal structure of a β-fructofuranosidase with high transfructosylation activity from Aspergillus kawachii.
- Authors
Nagaya, Mika; Kimura, Miyoko; Gozu, Yoshifumi; Sato, Shona; Hirano, Katsuaki; Tochio, Takumi; Nishikawa, Atsushi; Tonozuka, Takashi
- Abstract
β-Fructofuranosidases belonging to glycoside hydrolase family (GH) 32 are enzymes that hydrolyze sucrose. Some GH32 enzymes also catalyze transfructosylation to produce fructooligosaccharides. We found thatAspergillus kawachiiIFO 4308 β-fructofuranosidase (AkFFase) produces fructooligosaccharides, mainly 1-kestose, from sucrose. We determined the crystal structure ofAkFFase.AkFFase is composed of an N-terminal small component, a β-propeller catalytic domain, an α-helical linker, and a C-terminal β-sandwich, similar to other GH32 enzymes.AkFFase forms a dimer, and the dimerization pattern is different from those of other oligomeric GH32 enzymes. The complex structure ofAkFFase with fructose unexpectedly showed that fructose binds both subsites −1 and +1, despite the fact that the catalytic residues were not mutated. Fructose at subsite +1 interacts with Ile146 and Glu296 ofAkFFase via direct hydrogen bonds.
- Subjects
CRYSTAL structure; INVERTASE
- Publication
Bioscience, Biotechnology & Biochemistry, 2017, Vol 81, Issue 9, p1786
- ISSN
0916-8451
- Publication type
Article
- DOI
10.1080/09168451.2017.1353405