Expanding the active pH range of Escherichia coli glutamate decarboxylase by breaking the cooperativeness

Journal of Bioscience and Bioengineering

Volumn 115, Issue 2, 2013, Pages 154-158

  Thu Ho, Ngoc Anh ^a   Hou, Chen Yuan ^a   Kim, Woo Hyun ^a   Kang, Taek Jin ^a  

^a Dongguk University   (South Korea)

Author keywords

Enzyme cooperativeness; Enzyme engineering; Gamma aminobutyric acid; Glutamate decarboxylase; PH range expansion

Indexed keywords

ACIDIC ENVIRONMENT; AMINOBUTYRIC ACIDS; BIODIESEL PRODUCTION; COOPERATIVITY; DOUBLE MUTATION; ENZYME ENGINEERING; GAMMA-AMINOBUTYRIC ACIDS; GLUTAMATE DECARBOXYLASE; NEUTRAL PH; PH RANGE; SITE-SPECIFIC; STRUCTURAL DEFORMATION; VALUE ADDED PRODUCTS;

AMINO ACIDS; ESCHERICHIA COLI; GLYCEROL;

ENZYMES;

4 AMINOBUTYRIC ACID; BACTERIAL ENZYME; BIODIESEL; GLUTAMATE DECARBOXYLASE; GLUTAMIC ACID; GLYCEROL;

ARTICLE; BACTERIAL CELL; BACTERIAL GROWTH; BIOFUEL PRODUCTION; CELL GROWTH; COOPERATION; ESCHERICHIA COLI; NONHUMAN; PH; SITE DIRECTED MUTAGENESIS;

BIOFUELS; ESCHERICHIA COLI; GAMMA-AMINOBUTYRIC ACID; GLUTAMATE DECARBOXYLASE; GLUTAMIC ACID; HISTIDINE; HYDROGEN-ION CONCENTRATION; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN ENGINEERING;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 84871938369     PISSN: 13891723     EISSN: 13474421     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2012.09.002     Document Type: Article

References (18)

1. Foster J.W. Escherichia coli acid resistance: tales of an amateur acidophile. Nat. Rev. Microbiol. 2004, 2:898-907.
2. Lin J., Smith M.P., Chapin K.C., Baik H.S., Bennett G.N., Foster J.W. Mechanisms of acid resistance in enterohemorrhagic Escherichia coli. Appl. Environ. Microbiol. 1996, 62:3094-3100.
3. Pennacchietti E., Lammens T.M., Capitani G., Franssen M.C.R., John R.A., Bossa F., De Biase D. Mutation of His465 alters the pH-dependent spectroscopic properties of Escherichia coli glutamate decarboxylase and broadens the range of its activity towards more alkaline pH. J. Biol. Chem. 2009, 284:31287-31596.
4. Gut H., Pennacchietti E., John R.A., Bossa F., Capitani G., De Biase D., Grutter M.G. Escherichia coli acid resistance: pH-sensing, activation by chloride and autoinhibition in GadB. EMBO J. 2006, 25:2643-2651.
5. Shukuya R., Schwert G.W. Glutamic acid decarboxylase. I. Isolation procedures and properties of the enzyme. J. Biol. Chem. 1960, 235:1649-1652.
6. Dutyshev D.I., Darii E.L., Fomenkova N.P., Nikonov S.V., Andreeva N.S., Sukhareva B.S. Structure of Escherichia coli glutamate decarboxylase (GADα) in complex with glutarate at 2.05 å. Acta Crystallogr. D. 2005, 61:230-235.
7. Capitani G., De Biase D., Aurizi C., Gut H., Bossa F., Grutter M.G. Crystal structure and functional analysis of Escherichia coli glutamate decarboxylase. EMBO J. 2003, 22:4027-4037.
8. Tsukatani T., Higuchi T., Matsumoto K. Enzyme-based microtiter plate assay for γ-aminobutyric acid: application to the screening of γ-aminobutyric acid-producing lactic acid bacteria. Anal. Chim. Acta 2005, 540:293-297.
9. De Biase D., Tramonti A., John R.A., Bossa F. Isolation, overexpression, and biochemical characterization of the two isoforms of glutamic acid decarboxylase from Escherichia coli. Protein Expr. Purif. 1996, 8:430-438.
10. Tramonti A., De Biase D., Giartosio A., Bossa F., John R.A. The roles of His-167 and His-275 in the reaction catalyzed by glutamate decarboxylase from Escherichia coli. J. Biol. Chem. 1998, 273:1939-1945.
11. Ueno H. Enzymatic and structural aspects on glutamate decarboxylase. J. Mol. Catal. B: Enzym. 2000, 10:67-79.
12. Gut H., Dominici P., Pilati S., Astegno A., Petoukhov M.V., Svergun D.I., Grutter M.G., Capitani G. A common structural basis for pH- and calmodulin-mediated regulation in plant glutamate decarboxylase. J. Mol. Biol. 2009, 392:334-351.
13. Yu K., Lin L., Hu S., Huang J., Mei L.H. 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.
14. Lammens T.M., De Biase D., Franssen M.C.R., Scott E.L., Sanders J.P.M. The application of glutamic acid α-decarboxylase for the valorization of glutamic acid. Green Chem. 2009, 11:1562-1567.
15. Burrin D.G., Stoll B. Metabolic fate and function of dietary glutamate in the gut. Am. J. Clin. Nutr. 2009, 90:850S-856S.
16. Kawasaki N., Nakayama A., Yamano N., Takeda S., Kawata Y., Yamamoto N., Aiba S. Synthesis, thermal and mechanical properties and biodegradation of branched polyamide 4. Polymer 2005, 46:9987-9993.
17. Yamano N., Nakayama A., Kawasaki N., Yamamoto N., Aiba S. Mechanism and characterization of polyamide 4 degradation by Pseudomonas sp. J. Polym. Environ. 2008, 16:141-146.
18. Takahashi C., Shirakawa J., Tsuchidate T., Okai N., Hatada K., Nakayama H., Tateno T., Ogino C., Kondo A. Robust production of gamma-amino butyric acid using recombinant Corynebacterium glutamicum expressing glutamate decarboxylase from Escherichia coli. Enzyme Microb. Technol. 2012, 51:171-176.