Directed evolution and mutagenesis of glutamate decarboxylase from Lactobacillus brevis Lb85 to broaden the range of its activity toward a near-neutral pH

Enzyme and Microbial Technology

Volumn 61-62, Issue , 2014, Pages 35-43

  Shi, Feng ^a   Xie, Yilong ^a   Jiang, Junjun ^a   Wang, Nannan ^a   Li, Yongfu ^a   Wang, Xiaoyuan ^a  

^a JIANGNAN UNIVERSITY   (China)

Author keywords

Active pH range; Directed evolution; Error prone PCR; Glutamate decarboxylase; Site specific mutagenesis; Aminobutyric acid

Indexed keywords

AMINO ACIDS; BIOCHEMISTRY; MUTAGENESIS; PH;

AMINOBUTYRIC ACIDS; DIRECTED EVOLUTION; GLUTAMATE DECARBOXYLASE; PH RANGE; SITE-SPECIFIC MUTAGENESIS;

CATALYST ACTIVITY;

4 AMINOBUTYRIC ACID; GLUTAMATE DECARBOXYLASE; GLUTAMIC ACID; INDICATOR; BACTERIAL DNA; BACTERIAL PROTEIN; ESCHERICHIA COLI PROTEIN; GADB PROTEIN, E COLI; MEMBRANE PROTEIN; RECOMBINANT PROTEIN;

ARTICLE; BACTERIAL GENE; BACTERIUM MUTANT; BIOSYNTHESIS; CATALYSIS; CONTROLLED STUDY; CORYNEBACTERIUM GLUTAMICUM; ENZYME ACTIVITY; ERROR PRONE POLYMERASE CHAIN REACTION; GENETIC VARIABILITY; GLUTAMATE DECARBOXYLASE B1 GENE; HIGH THROUGHPUT SCREENING; LACTOBACILLUS BREVIS; MOLECULAR EVOLUTION; NEAR NEUTRAL PH; NONHUMAN; PH; POLYMERASE CHAIN REACTION; SITE DIRECTED MUTAGENESIS; WILD TYPE; AMINO ACID SEQUENCE; CHEMISTRY; DIRECTED MOLECULAR EVOLUTION; ENZYMOLOGY; GENETICS; KINETICS; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BASE SEQUENCE; CORYNEBACTERIUM GLUTAMICUM; DIRECTED MOLECULAR EVOLUTION; DNA, BACTERIAL; ESCHERICHIA COLI PROTEINS; GAMMA-AMINOBUTYRIC ACID; GLUTAMATE DECARBOXYLASE; HYDROGEN-ION CONCENTRATION; KINETICS; LACTOBACILLUS BREVIS; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 84900809065     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2014.04.012     Document Type: Article

References (29)

1. Ueno H. Enzymatic and structural aspects on glutamate decarboxylase. J Mol Catal 2000, 10:67-79.
2. Ge S.Y., Goh E.L.K., Sailor K.A., Kitabatake Y., Ming G.L., Song H.J. GABA regulates synaptic integration of newly generated neurons in the adult brain. Nature 2006, 439:589-593.
3. Baum G., Levyadun S., Fridmann Y., Arazi T., Katsnelson H., Zik M., et al. Calmodulin binding to glutamate decarboxylase is required for regulation of glutamate and GABA metabolism and normal development in plants. EMBO J 1996, 15:2988-2996.
4. Gut H., Pennacchietti E., John R.A., Bossa F., Capitani G., De Biase D., et al. Escherichia coli acid resistance: pH-sensing, activation by chloride and autoinhibition in GadB. EMBO J 2006, 25:2643-2651.
5. Karatzas K.A., Brennan O., Heavin S., Morrissey J., O'byrne C.P. Intracellular accumulation of high levels of γ-aminobutyrate by Listeria monocytogenes 10403S in response to low pH: uncoupling of γ-aminobutyrate synthesis from efflux in a chemically defined medium. Appl Environ Microbiol 2010, 76:3529-3537.
6. Feehily C., Karatzas K.A. Role of glutamate metabolism in bacterial responses towards acid and other stresses. J Appl Microbiol 2013, 114:11-24.
7. Wang Q., Xin Y.Q., Zhang F., Feng Z.Y., Fu J., Luo L., et al. Enhanced γ-aminobutyric acid-forming activity of recombinant glutamate decarboxylase (gadA) from Escherichia coli. World J Microbiol Biotechnol 2011, 27:693-700.
8. Hiraga K., Ueno Y., Oda K. Glutamate decarboxylase from Lactobacillus brevis: activation by ammonium sulfate. Biosci Biotechnol Biochem 2008, 72:1299-1306.
9. Yang S.Y., Lin Q., Lu Z.X., Lu F.X., Bie X.M., Zou X.K., et al. Characterization of a novel glutamate decarboxylase from Streptococcus salivarius ssp. thermophilus Y2. J Chem Technol Biotechnol 2008, 83:855-861.
10. Capitani G., De Biase D., Aurizi C., Gut H., Bossa F., Grütter M.G. Crystal structure and functional analysis of Escherichia coli glutamate decarboxylase. EMBO J 2003, 22:4027-4037.
11. Dutyshev D.I., Darii E.L., Fomenkova N.P., Pechik I.V., Polyakov K.M., Nikonov S.V., et al. Structure of Escherichia coli glutamate decarboxylase (GADα) in complex with glutarate at 2.05Å resolution. Acta Crystallogr D: Biol Crystallogr 2005, 61:230-235.
12. 465 alters the pH-dependent spectroscopic properties of Escherichia coli glutamate decarboxylase and broadens the range of its activity toward more alkaline pH. J Biol Chem 2009, 284:31587-31596.
13. Ho N.A.T., Hou C.Y., Kim W.H., Kang T.J. Expanding the active pH range of Escherichia coli glutamate decarboxylase by breaking the cooperativeness. J Biosci Bioeng 2013, 115:154-158.
14. Kang T.J., Ho N.A.T., Pack S.P. Buffer-free production of gamma-aminobutyric acid using an engineered glutamate decarboxylase from Escherichia coli. Enzyme Microb Technol 2013, 53:200-205.
15. Yu K., Lin L., Hu S., Huang J., Mei L. C-terminal truncation of glutamate decarboxylase from Lactobacillus brevis CGMCC 1306 extends its activity toward near-neutral pH. Enzyme Microb Technol 2012, 50:263-269.
16. Cadwell R.C., Joyce G.F. Mutagenic PCR. PCR Methods Appl 1994, 3:S136-S140.
17. Stemmer W.P.C. Rapid evolution of a protein in vitro by DNA shuffling. Nature 1994, 370:389-391.
18. Shi F., Li Y.X. Synthesis of γ-aminobutyric acid by expressing Lactobacillus brevis-derived glutamate decarboxylase in the Corynebacterium glutamicum strain ATCC13032. Biotechnol Lett 2011, 33:2469-2474.
19. Hermann T. Industrial production of amino acids by coryneform bacteria. J Biotechnol 2003, 104:155-172.
20. Shi F., Jiang J.J., Li Y.X., Li Y.F., Xie Y.L. Enhancement of γ-aminobutyric acid production in recombinant Corynebacterium glutamicum by co-expressing two glutamate decarboxylase genes from Lactobacillus brevis. J Ind Microbiol Biotechnol 2013, 40:1285-1296.
21. Takahashi C., Shirakawa J., Tsuchidate T., Okai N., Hatada K., Nakayama H., et al. Robust production of gamma-amino butyric acid using recombinant Corynebacterium glutamicum expressing glutamate decarboxylase from Escherichia coli. Enzyme Microb Technol 2012, 51:171-176.
22. Drummond D.A., Iverson B.L., Georgiou G., Arnold F.H. Why high-error-rate random mutagenesis libraries are enriched in functional and improved proteins. J Mol Biol 2005, 350:806-816.
23. Edelheit O., Hanukoglu A., Hanukoglu I. Simple and efficient site-directed mutagenesis using two single-primer reactions in parallel to generate mutants for protein structure-function studies. BMC Biotechnol 2009, 9:61.
24. Xu D.Q., Tan Y.Z., Huan X.J., Hu X.Q., Wang X.Y. Construction of a novel shuttle vector for use in Brevibacterium flavum, an industrial amino acid producer. J Microbiol Methods 2010, 80:86-92.
25. Schwede T., Kopp J., Guex N., Peitsch M.C. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res 2003, 31:3381-3385.
26. Lammens T.M., De Biase D., Franssen M.C.R., Scott E.L., Sanders J.P.M. The application of glutamic acid alpha-decarboxylase for the valorization of glutamic acid. Green Chem 2009, 11:1562-1567.
27. Li H.X., Qiu T., Huang G.D., Cao Y.S. Production of gamma-aminobutyric acid by Lactobacillus brevis NCL912 using fed-batch fermentation. Microb Cell Fact 2010, 9:85.
28. Tamura T., Noda M., Ozaki M., Maruyama M., Matoba Y., Kumagai T., et al. Establishment of an efficient fermentation system of gamma-aminobutyric acid by a lactic acid bacterium, Enterococcus avium G-15, isolated from carrot leaves. Biol Pharm Bull 2010, 33:1673-1679.
29. Komatsuzaki N., Nakamura T., Kimura T., Shima J. Characterization of glutamate decarboxylase from a high γ-aminobutyric acid (GABA)-producer, Lactobacillus paracasei. Biosci Biotechnol Biochem 2008, 72:278-285.