Structural highlights
Function
B3Y018_LACPN
Publication Abstract from PubMed
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. (c) Proteins 2013;. (c) 2013 Wiley Periodicals, Inc.
Crystallographic and mutational analyses of tannase from Lactobacillus plantarum.,Matoba Y, Tanaka N, Noda M, Higashikawa F, Kumagai T, Sugiyama M Proteins. 2013 Jul 8. doi: 10.1002/prot.24355. PMID:23836494[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Matoba Y, Tanaka N, Noda M, Higashikawa F, Kumagai T, Sugiyama M. Crystallographic and mutational analyses of tannase from Lactobacillus plantarum. Proteins. 2013 Jul 8. doi: 10.1002/prot.24355. PMID:23836494 doi:10.1002/prot.24355