Crystallographic and mutational analyses of tannase from Lactobacillus plantarum

Proteins: Structure, Function and Bioinformatics

Volumn 81, Issue 11, 2013, Pages 2052-2058

  Matoba, Yasuyuki ^a   Tanaka, Naomi ^a   Noda, Masafumi ^a   Higashikawa, Fumiko ^a   Kumagai, Takanori ^a   Sugiyama, Masanori ^a  

^a HIROSHIMA UNIVERSITY   (Japan)

Author keywords

hydrolase; Bacteria; Crystal structure; Enzyme; Tannin

Indexed keywords

CRYOPROTECTIVE AGENT; GLYCEROL; TANNASE;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME STRUCTURE; EVOLUTION; GENE MUTATION; HYDROGEN BOND; LACTOBACILLUS PLANTARUM; NONHUMAN; NUCLEOPHILICITY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE;

LACTOBACILLUS PLANTARUM;

BACTERIA; CRYSTAL STRUCTURE; ENZYME; TANNIN; Α/Β-HYDROLASE;

CARBOXYLIC ESTER HYDROLASES; DNA MUTATIONAL ANALYSIS; LACTOBACILLUS PLANTARUM; TANNINS;

EID: 84885858552     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24355     Document Type: Article

References (27)

1. White T. Tannins-their occurrence and significance. J Sci Food Agric 1957;8:377-385.
2. Khanbabaee K, van Ree T. Tannins: classification and definition. Nat Prod Rep 2001;18:641-649.
3. Baxter NJ, Lilley TH, Haslam E, Williamson MP. Multiple interactions between polyphenols and a salivary proline-rich protein repeat result in complexation and precipitation. Biochemistry 1997;36:5566-5577.
4. McDonald M, Mila I, Scalbert A. Precipitation of metal ions by plant polyphenols: optimal conditions and origin of precipitation. J Agric Food Chem 1996;44:599-606.
5. Scalbert A. Antinutritional effects of condensed and hydrolyzable tannins. Phytochemistry 1991;30:3875-3883.
6. Butler LG. Antimicrobial properties of tannins. Basic Life Sci 1992;59:693-698.
7. Aguilar C, Rodríguez R, Gutiérrez-Sánchez G, Augur C, Favela-Torres E, Prado-Barragan LA, Ramírez-Coronel A, Contreras-Esquivel JC. Microbial tannases: advances and perspectives. Appl Microbiol Biotechnol 2007;76:47-59.
8. Banerjee R, Mondal K, Bikas R. Production and characterization of extracellular and intracellular tannase from newly isolated Aspergillus aculeatus DBF9. J Basic Microbiol 2001;6:313-318.
9. Yamada H, Adachi O, Watanabe M, Ogata K. Tannase (tannin acyl hydrolase), a typical serine esterase. Agric Biol Chem 1968;32:257-258.
10. Lekha PK, Lonsane BK. Production and application of tannin acyl hydrolase: state of the art. Adv Appl Microbiol 1997;44:215-260.
11. T. Syst Appl Microbiol 2008;31:269-277.
12. Curiel JA, Rodríguez H, Acebrón I, Mancheño JM, de las Rivas B, Muñoz R. Production and physicochemical properties of recombinant Lactobacillus plantarum tannase. J Agric Food Chem 2009;57:6224-6230.
13. Wu M, Peng X, Wen H, Wang Q, Chen Q, McKinstry WJ, Ren B. Expression, purification, crystallization, and preliminary X-ray analysis of tannase from Lactobacillus plantarum. Acta Crystallogr Sect F Struct Biol Cryst Commun 2013;69:456-459.
14. Sharma S, Bhat TK, Dawra RK. A spectrophotometric method for assay of tannase using rhodanine. Anal Biochem 2000;279:85-89.
15. Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 1997;276:307-326.
16. Collaborative Computational Project Number 4.The CCP4 suite: programs for protein crystallography. Acta Crystallogr Sect D Biol Crystallogr 1994;50:760-763.
17. de la Fottelle E, Bricogne G. Maximum-likelihood heavy-atom parameters refinement in the MIR and MAD methods. Methods Enzymol 1997;276:472-494.
18. McRee DE. A visual protein crystallographic software system for X11/XView. J Mol Graphics 1992;10:44-46.
19. Brünger AT, Adams PD, Clore GM, DeLano WL, Gros P, Grosse-Kunstleve RW, Jiang JS, Kuszewski J, Nilges M, Pannu NS, Read RJ, Rice LM, Simonson T, Warren GL. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr Sect D Biol Crystallogr 1998;54:905-921.
20. Brünger AT. The freeR value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 1992;355:472-475.
21. Heikinheimo P, Goldman A, Jeffries C, Ollis DL. Of barn owls and bankers: a lush variety of α/β hydrolases. Structure 1999;7:R141-R146.
22. Ollis DL, Cheah E, Cygler M, Dijkstra B, Frolow F, Franken SM, Harel M, Remington SJ, Silman I, Schrag J, Sussman JL, Verschueren KHG, Goldman A. The α/β hydrolase fold. Protein Eng 1992;5:197-211.
23. Nardini M, Dijkstra BW. α/β Hydrolase fold enzymes: the family keeps growing. Curr Opin Struct Biol 1999;9:732-737.
24. Holmquist M. α/β-Hydrolase fold enzymes: structures, functions, and mechanisms. Curr Protein Pept Sci 2000;1:209-235.
25. Holm L, Sander C. Protein structure comparison by alignment of distance matrices. J Mol Biol 1993;233:123-138.
26. Zhu X, Larsen NA, Basran A, Bruce NC, Wilson IA. Observation of an arsenic adduct in an acetyl esterase crystal structure. J Biol Chem 2003;278:2008-2014.
27. Akoh CC, Lee GC, Liaw YC, Huang TH, Shaw JF. GDSL family of serine esterases/lipases. Prog Lipid Res 2004;43:534-552.