Mutational analysis of the role of calcium ions in the  Lactobacillus reuteri  strain 121 fructosyltransferase (levansucrase and inulosucrase) enzymes | Zendy

Ozimek L.K. | Zendy; Euverink G.J.W. | Zendy; van der Maarel M.J.E.C. | Zendy; Dijkhuizen L. | Zendy

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Mutational analysis of the role of calcium ions in the Lactobacillus reuteri strain 121 fructosyltransferase (levansucrase and inulosucrase) enzymes

Author(s) -

Ozimek L.K.,

Euverink G.J.W.,

van der Maarel M.J.E.C.,

Dijkhuizen L.

Publication year - 2005

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1016/j.febslet.2004.11.113

Subject(s) - lactobacillus reuteri , levansucrase , bacillus subtilis , biochemistry , enzyme , chemistry , lipid ii , cofactor , bacteria , biology , lactobacillus , peptidoglycan , genetics , fermentation

Bacterial fructosyltransferase enzymes belonging to glycoside hydrolase family 68 (GH68) are not known to require a metal cofactor. Here, we show that Ca 2+ ions play an important structural role in the Lactobacillus reuteri 121 levansucrase (Lev) and inulosucrase (Inu) enzymes. Analysis of the Bacillus subtilis Lev 3D structure [Meng, G. and Futterer, K. (2003) Nat. Struct. Biol. 10, 935–941] has provided evidence for the presence of a bound metal ion, most likely Ca 2+ . Characterization of site‐directed mutants in the putative Ca 2+ ion‐binding sites of Lb. reuteri Lev and Inu revealed that the Inu Asp520 and Lev Asp500 residues play an important role in Ca 2+ binding. Sequence alignments of family GH68 proteins showed that this Ca 2+ ion‐binding site is (largely) present only in proteins of Gram‐positive origin.

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