Matoba_2013_Proteins_81_2052

Reference

Title : Crystallographic and mutational analyses of tannase from Lactobacillus plantarum - Matoba_2013_Proteins_81_2052
Author(s) : Matoba Y , Tanaka N , Noda M , Higashikawa F , Kumagai T , Sugiyama M
Ref : Proteins , 81 :2052 , 2013
Abstract : Tannin acylhydrolase (EC 3.1.1.20) referred commonly as tannase catalyzes the hydrolysis of the galloyl ester bond of tannins to release gallic acid. Although the enzyme is useful for various industries, the tertiary structure is not yet determined. In this study, we determined the crystal structure of tannase produced by Lactobacillus plantarum. The tannase structure belongs to a member of alpha/beta-hydrolase superfamily with an additional "lid" domain. A glycerol molecule derived from cryoprotectant solution was accommodated into the tannase active site. The binding manner of glycerol to tannase seems to be similar to that of the galloyl moiety in the substrate. Proteins 2013; 81:2052-2058. (c) 2013 Wiley Periodicals, Inc.
ESTHER : Matoba_2013_Proteins_81_2052
PubMedSearch : Matoba_2013_Proteins_81_2052
PubMedID: 23836494
Gene_locus related to this paper: lacpl-tanL

Related information

Gene_locus related to this paper: lacpl-tanL

Citations formats

Matoba Y, Tanaka N, Noda M, Higashikawa F, Kumagai T, Sugiyama M (2013)
Crystallographic and mutational analyses of tannase from Lactobacillus plantarum
Proteins 81 :2052

Matoba Y, Tanaka N, Noda M, Higashikawa F, Kumagai T, Sugiyama M (2013)
Proteins 81 :2052