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beta-fructosidase superfamily: homology with some alpha-L-arabinases and beta-D-xylosidases.
State Institute for Genetics and Selection of Industrial Microorganisms, Moscow, Russia. daniil_naumoff@yahoo.com
Comparison of the amino acid sequences of four families of glycosyl hydrolases reveals that they are homologous and have several common conserved regions. Two of these families contain beta-fructosidases (glycosyl hydrolase families GH32 and GH68) and the other two include alpha-L-arabinases and beta-xylosidases (families GH43 and GH62). The latter two families are proposed to be grouped together with the former two into the beta-fructosidase (furanosidase) superfamily. Several ORFs can be considered as a fifth family of the superfamily on the basis of sequence similarity. It is shown for the first time that a glycosyl hydrolase superfamily can include enzymes with both inversion and retention mechanism of action. Composition of the active center for enzymes of the superfamily is discussed.
PMID: 11093261 [PubMed - indexed for MEDLINE]
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Cited by 6 PubMed Central articles
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Unraveling the difference between invertases and fructan exohydrolases: a single amino acid (Asp-239) substitution transforms Arabidopsis cell wall invertase1 into a fructan 1-exohydrolase.
Le Roy K, Lammens W, Verhaest M, De Coninck B, Rabijns A, Van Laere A, Van den Ende W.
Plant Physiol. 2007 Nov; 145(3):616-25. Epub 2007 Sep 14.
[Plant Physiol. 2007]
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Molecular and biochemical characterization of a novel intracellular invertase from Aspergillus niger with transfructosylating activity.
Goosen C, Yuan XL, van Munster JM, Ram AF, van der Maarel MJ, Dijkhuizen L.
Eukaryot Cell. 2007 Apr; 6(4):674-81. Epub 2007 Feb 9.
[Eukaryot Cell. 2007]
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Crystallization and preliminary X-ray diffraction study of a cell-wall invertase from Arabidopsis thaliana.
Verhaest M, Le Roy K, Sansen S, De Coninck B, Lammens W, De Ranter CJ, Van Laere A, Van den Ende W, Rabijns A.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Aug 1; 61(Pt 8):766-8. Epub 2005 Jul 30.
[Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005]
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