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Crystallographic and mutational analyses of tannase from Lactobacillus plantarum
Author(s) -
Matoba Yasuyuki,
Tanaka Naomi,
Noda Masafumi,
Higashikawa Fumiko,
Kumagai Takanori,
Sugiyama Masanori
Publication year - 2013
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24355
Subject(s) - tannase , lactobacillus plantarum , hydrolase , tannin , chemistry , glycerol , biochemistry , gallic acid , hydrolysis , moiety , substrate (aquarium) , enzyme , stereochemistry , food science , lactic acid , bacteria , biology , ecology , genetics , antioxidant
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 α/β‐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. © 2013 Wiley Periodicals, Inc.