ArticleThe Journal of biological chemistry2009
Mutation of His465 alters the pH-dependent spectroscopic properties of Escherichia coli glutamate decarboxylase and broadens the range of its activity toward more alkaline pH.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 65 citations in OpenAlex.
- Role of Aspartate 86 in the Catalytic Mechanism ofBiochemistry · 2026Article
- Synthesis of versatile neuromodulatory molecules by a gut microbial glutamate decarboxylase.iScience · 2025Article
- Synthesis and Biological Activity of Homohypotaurine Obtained by the Enzyme-Based Conversion of Homocysteine Sulfinic Acid Using RecombinantMolecules (Basel, Switzerland) · 2024Article
- Genetic Circuits for Feedback Control of Gamma-Aminobutyric Acid Biosynthesis in ProbioticMetabolites · 2024Article
- High-level production of γ-aminobutyric acid via efficient co-expression of the key genes of glutamate decarboxylase system inEngineering microbiology · 2023Article
- Shifting the pH Optima of (International journal of molecular sciences · 2022Article
- Molecular Analysis of Glutamate Decarboxylases inFrontiers in microbiology · 2021Article
- Immobilization and enzymatic properties of glutamate decarboxylase from Enterococcus faecium by affinity adsorption on regenerated chitin.Amino acids · 2020Article
- Comparative Review of the Responses ofGenes · 2020Review
- Enzymatic kinetic resolution of desmethylphosphinothricin indicates that phosphinic group is a bioisostere of carboxyl group.Communications chemistry · 2020Article
- Function and Regulation of Acid Resistance Antiporters.The Journal of membrane biology · 2019Article
- Molecular Basis of Bacillus subtilis ATCC 6633 Self-Resistance to the Phosphono-oligopeptide Antibiotic Rhizocticin.ACS chemical biology · 2019Article
- The Glutaminase-Dependent Acid Resistance System: Qualitative and Quantitative Assays and Analysis of Its Distribution in Enteric Bacteria.Frontiers in microbiology · 2018Article
- Biotechnological advances and perspectives of gamma-aminobutyric acid production.World journal of microbiology & biotechnology · 2017Review
- Metabolic engineering ofMetabolic engineering communications · 2016Article
- Biochemical and spectroscopic properties of Brucella microti glutamate decarboxylase, a key component of the glutamate-dependent acid resistance system.FEBS open bio · 2015Article
- Asymmetry of the active site loop conformation between subunits of glutamate-1-semialdehyde aminomutase in solution.BioMed research international · 2013Article
- Expression, immobilization and enzymatic properties of glutamate decarboxylase fused to a cellulose-binding domain.International journal of molecular sciences · 2012Article
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7 authors at 5 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glutamate decarboxylase (GadB) from Escherichia coli is a hexameric, pyridoxal 5'-phosphate-dependent enzyme catalyzing CO(2) release from the alpha-carboxyl group of L-glutamate to yield gamma-aminobutyrate. GadB exhibits an acidic pH optimum and undergoes a spectroscopically detectable and strongly cooperative pH-dependent conformational change involving at least six protons. Crystallographic studies showed that at mildly alkaline pH GadB is inactive because all active sites are locked by the C termini and that the 340 nm absorbance is an aldamine formed by the pyridoxal 5'-phosphate-Lys(276) Schiff base with the distal nitrogen of His(465), the penultimate residue in the GadB sequence. Herein we show that His(465) has a massive influence on the equilibrium between active and inactive forms, the former being favored when this residue is absent. His(465) contributes with n approximately 2.5 to the overall cooperativity of the system. The residual cooperativity (n approximately 3) is associated with the conformational changes still occurring at the N-terminal ends regardless of the mutation. His(465), dispensable for the cooperativity that affects enzyme activity, is essential to include the conformational change of the N termini into the cooperativity of the whole system. In the absence of His(465), a 330-nm absorbing species appears, with fluorescence emission spectra more complex than model compounds and consisting of two maxima at 390 and 510 nm. Because His(465) mutants are active at pH well above 5.7, they appear to be suitable for biotechnological applications.
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