Characterization of glutamate decarboxylase from Lactobacillus plantarum and its C-terminal function for the pH dependence of activity

Sun Mi Shin, Hana Kim, Yunhye Joo, Sang Jae Lee, Yong Jik Lee, Sang Jun Lee, Dong Woo Lee

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

The gadB gene encoding glutamate decarboxylase (GAD) from Lactobacillus plantarum was cloned and expressed in Escherichia coli. The recombinant enzyme exhibited maximal activity at 40°C and pH 5.0. The 3D model structure of L. plantarum GAD proposed that its C-terminal region (Ile454-Thr468) may play an important role in the pH dependence of catalysis. Accordingly, C-terminally truncated (Δ3 and Δ11 residues) mutants were generated and their enzyme activities compared with that of the wild-type enzyme at different pH values. Unlike the wild-type GAD, the mutants showed pronounced catalytic activity in a broad pH range of 4.0-8.0, suggesting that the C-terminal region is involved in the pH dependence of GAD activity. Therefore, this study may provide effective target regions for engineering pH dependence of GAD activity, thereby meeting industrial demands for the production of γ-aminobutyrate in a broad range of pH values.

Original languageEnglish
Pages (from-to)12186-12193
Number of pages8
JournalJournal of Agricultural and Food Chemistry
Volume62
Issue number50
DOIs
Publication statusPublished - 2014 Dec 17

Fingerprint

glutamate decarboxylase
Lactobacillus plantarum
Glutamate Decarboxylase
catalytic activity
Aminobutyrates
Gene encoding
Enzymes
Enzyme activity
Model structures
Escherichia coli
Catalysis
mutants
Catalyst activity
enzymes
engineering
enzyme activity

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Agricultural and Biological Sciences(all)

Cite this

Shin, Sun Mi ; Kim, Hana ; Joo, Yunhye ; Lee, Sang Jae ; Lee, Yong Jik ; Lee, Sang Jun ; Lee, Dong Woo. / Characterization of glutamate decarboxylase from Lactobacillus plantarum and its C-terminal function for the pH dependence of activity. In: Journal of Agricultural and Food Chemistry. 2014 ; Vol. 62, No. 50. pp. 12186-12193.
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abstract = "The gadB gene encoding glutamate decarboxylase (GAD) from Lactobacillus plantarum was cloned and expressed in Escherichia coli. The recombinant enzyme exhibited maximal activity at 40°C and pH 5.0. The 3D model structure of L. plantarum GAD proposed that its C-terminal region (Ile454-Thr468) may play an important role in the pH dependence of catalysis. Accordingly, C-terminally truncated (Δ3 and Δ11 residues) mutants were generated and their enzyme activities compared with that of the wild-type enzyme at different pH values. Unlike the wild-type GAD, the mutants showed pronounced catalytic activity in a broad pH range of 4.0-8.0, suggesting that the C-terminal region is involved in the pH dependence of GAD activity. Therefore, this study may provide effective target regions for engineering pH dependence of GAD activity, thereby meeting industrial demands for the production of γ-aminobutyrate in a broad range of pH values.",
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Characterization of glutamate decarboxylase from Lactobacillus plantarum and its C-terminal function for the pH dependence of activity. / Shin, Sun Mi; Kim, Hana; Joo, Yunhye; Lee, Sang Jae; Lee, Yong Jik; Lee, Sang Jun; Lee, Dong Woo.

In: Journal of Agricultural and Food Chemistry, Vol. 62, No. 50, 17.12.2014, p. 12186-12193.

Research output: Contribution to journalArticle

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AU - Shin, Sun Mi

AU - Kim, Hana

AU - Joo, Yunhye

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AU - Lee, Yong Jik

AU - Lee, Sang Jun

AU - Lee, Dong Woo

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