X‐ray diffraction structure of a plant glycosyl hydrolase family 32 protein: fructan 1‐exohydrolase IIa of Cichorium intybus
2004; Wiley; Volume: 41; Issue: 3 Linguagem: Inglês
10.1111/j.1365-313x.2004.02304.x
ISSN1365-313X
AutoresMaureen Verhaest, Wim Van den Ende, Katrien Le Roy, C. J. De Ranter, André Van Laere, Anja Rabijns,
Tópico(s)Food composition and properties
ResumoSummary Fructan 1‐exohydrolase, an enzyme involved in fructan degradation, belongs to the glycosyl hydrolase family 32. The structure of isoenzyme 1‐FEH IIa from Cichorium intybus is described at a resolution of 2.35 Å. The structure consists of an N‐terminal fivefold β ‐propeller domain connected to two C‐terminal β ‐sheets. The putative active site is located entirely in the β ‐propeller domain and is formed by amino acids which are highly conserved within glycosyl hydrolase family 32. The fructan‐binding site is thought to be in the cleft formed between the two domains. The 1‐FEH IIa structure is compared with the structures of two homologous but functionally different enzymes: a levansucrase from Bacillus subtilis (glycosyl hydrolase family 68) and an invertase from Thermotoga maritima (glycosyl hydrolase family 32).
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