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evolution
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clustal X-generated dendrogram of bacterial glutamate decarboxylases, overview
evolution
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clustal X-generated dendrogram of bacterial glutamate decarboxylases, overview
evolution
clustal X-generated dendrogram of bacterial glutamate decarboxylases, overview
evolution
Brucella microti belongs to a group of atypical brucellae that possess functional gadB and gadC genes, unlike the most well-known classical Brucella species, which include important human pathogens
evolution
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different morphological, biochemical and chemotaxonomic characteristics of the strains AM and strain B8W22
evolution
the amino acid sequences of GADLbHYE1 shows 48% homology with the GadA family and 99% identity with the GadB family from Lactobacillus brevis
evolution
the enzyme belongs to the fold type I family of PLP-enzymes
evolution
the GAD from Lactobacillus sakei strain A156 contains a highly conserved catalytic domain that belongs to the pyridoxal 5'-phosphate-dependent decarboxylase superfamily. The domain includes a lysine residue essential for pyridoxal 5'-phosphate binding, designated as PLP lysine
evolution
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clustal X-generated dendrogram of bacterial glutamate decarboxylases, overview
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evolution
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different morphological, biochemical and chemotaxonomic characteristics of the strains AM and strain B8W22
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evolution
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Brucella microti belongs to a group of atypical brucellae that possess functional gadB and gadC genes, unlike the most well-known classical Brucella species, which include important human pathogens
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evolution
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the GAD from Lactobacillus sakei strain A156 contains a highly conserved catalytic domain that belongs to the pyridoxal 5'-phosphate-dependent decarboxylase superfamily. The domain includes a lysine residue essential for pyridoxal 5'-phosphate binding, designated as PLP lysine
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evolution
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clustal X-generated dendrogram of bacterial glutamate decarboxylases, overview
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evolution
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the amino acid sequences of GADLbHYE1 shows 48% homology with the GadA family and 99% identity with the GadB family from Lactobacillus brevis
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malfunction
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GAD65 knockout mice show a diminished response to propofol, but not ketamine, indicating that GAD65-mediated 4-aminobutanoate synthesis plays an important role in hypnotic and immobilizing actions of propofol
malfunction
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the GAD65 null mutation affects neural activities during fear memory extinction and examined local field potentials from the lateral amygdala, the CA1 area of the hippocampus, and the infralimbic area of the prefrontal cortex during this process in Gad65deficient mice
malfunction
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survival of the gadB mutant after 60 min in the presence of 0.045 mg/ml nisin powder is approximately 5fold less than that of the parental strain
malfunction
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the DELTAgadD1 mutant is impaired in its ability to tolerate exposure to both sublethal and lethal levels of the lantibiotic nisin
malfunction
at pH values above pH 6.0, GAD is inactive due to conformational change of the hexameric enzyme at its N- and C-termini from acidic to neutral pH. Especially, His465 at the C-terminus of the enzyme together with Glu89 are demonstrated to be involved in the conformational change in a cooperative manner
malfunction
disturbances in GABA levels are responsible for a host of neurologic diseases. A reduction in GABA is also implicated in certain anxiety states such as panic disorder (PD). People suffering from PD have 22% lower GABA levels in the occipital cortex
malfunction
phosphorylation site mutation T95A abolishes the phosphorylation and its effects on enzyme activity. When the phosphorylation site T95 is mutated to glutamic acid, which mimics the phosphorylation status of hGAD65, the enzyme activity is greatly increased. An increase of GAD65 activity by 55% compared to the wild type hGAD65 is observed indicating that mutation of T95 to glutamic acid mimics the effect of phosphorylation
malfunction
transcription levels of genes involved in nitrogen metabolism are upregulated in the DELTAgad enzyme deletion strain. The mutant shows approximately 4 and 8fold increases in the transcript levels of kgd and gabdh encoding a novel 2-oxoglutarate decarboxylase and gamma-aminobutanal dehydrogenase, respectively. Phenotype, overview. In Synechocystis lacking a functional GAD, the gamma-aminobutanal dehydrogenase might serve as an alternative catalytic pathway for GABA synthesis
malfunction
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survival of the gadB mutant after 60 min in the presence of 0.045 mg/ml nisin powder is approximately 5fold less than that of the parental strain
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malfunction
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the DELTAgadD1 mutant is impaired in its ability to tolerate exposure to both sublethal and lethal levels of the lantibiotic nisin
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metabolism
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the 4-aminobutanoate shunt pathway possesses three enzymes encoded by genes gad, gabT, and gabD. Among the three, GAD is the key cytosolic-located enzyme which catalyzes the irreversible decarboxylation of L-glutamate to produce 4-aminobutanoate
metabolism
glutamate decarboxylase is a key enzyme that catalyzes the irreversible alpha-decarboxylation of L-glutamate to 4-aminobutanoate, GABA
metabolism
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glutamate decarboxylase is a key enzyme that catalyzes the irreversible alpha-decarboxylation of L-glutamate to 4-aminobutanoate, GABA
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physiological function
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GAD65-mediated 4-aminobutanoate synthesis plays relatively small but significant roles in nociceptive processing via supraspinal mechanisms
physiological function
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the GAD acid resistance system does not play any role in the survival of Listeria monocytogenes at a low pH
physiological function
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the GAD acid resistance system does not play any role in the survival of Salmonella enterica at a low pH
physiological function
GAD plays a role in hypocotyl and stem development in pine
physiological function
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GAD1 plays an important role in responses to abiotic factors and hormone treatments
physiological function
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possession of the gadD1 gene correlates with a higher degree of tolerance to nisin
physiological function
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possession of the gadD1 gene correlates with a higher degree of tolerance to nisin
physiological function
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the glutamate decarboxylase system is important for the acid resistance of Listeria monocytogenes. Cells accumulate intracellular 4-aminobutanoate as a standard response against acid in any medium. The GADi system is activated at milder pH values of pH 4.5 to pH 5.0 than theGADe system, pH 4.0 to pH 4.5, suggesting that GADi is the more responsive of the two and the first line of defense against acid. Model for the function of the GAD system under severe acid conditions below pH 4.5
physiological function
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the glutamate-dependent acid resistance (GDAR) system is by far the most potent acid resistance system in commensal and pathogenic Escherichia coli and requires the activity of intracellular glutamate decarboxylase GadB performing a proton-consuming decarboxylation reaction and the cognate antiporter GadC, which performs the glutamate/in/gamma-aminobutyrate/out electrogenic antiport, overview
physiological function
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the glutamate-dependent acid resistance (GDAR) system is by far the most potent acid resistance system in commensal and pathogenic Listeria monocytogenes and requires the activity of intracellular glutamate decarboxylase GadB performing a proton-consuming decarboxylation reaction and the cognate antiporter GadC, which performs the glutamate/in/gamma-aminobutyrate/out electrogenic antiport, overview
physiological function
compared to GADs from other organisms, plant GADs possess a unique feature, namely, the presence of a C-terminal calmodulin binding site (CaMBD). This characteristic confers plant GADs an additional regulatory mechanism by making them responsive to cytosolic calcium (Ca2+), thus revealing that at least two mechanisms exist, by which GAD activity can be stimulated in vitro and in vivo, namely, acidic pH and Ca2+/CaM. Transient elevation of cytosolic Ca2+ in response to different types of stress is responsible for GAD activation via CaM
physiological function
enzyme GAD is involved in the maintainence of the cellular pH near neutral values under the acidic environments and its role is especially important for lactic acid bacteria (LAB)
physiological function
gamma-aminobutyric acid with several physiological functions is biosynthesized via the irreversible alpha-decarboxylation of L-glutamate catalysed by glutamate decarboxylase (GAD). Streptococcus salivarius ssp. thermophilus is widely applied to the dairy
physiological function
glutamate decarboxylase (GAD) catalyzes the irreversible decarboxylation of L-glutamate to the valuable food supplement gamma-aminobutyric acid (GABA)
physiological function
glutamate decarboxylase (GAD) is the enzyme responsible for the synthesis of gamma-aminobutyric acid (GABA) in Synechocystis sp. PCC6803
physiological function
glutamate decarboxylase is a key component of the glutamate-dependent acid resistance system in Brucella microti. The glutamate-dependent acid resistance system (GDAR) is the most efficient molecular system in conferring protection from acid stress, structural overview
physiological function
glutamic acid decarboxylase (GAD) is a pyridoxal 5'-phosphate (PLP)-dependent enzyme responsible for the synthesis of gamma-aminobutyric acid (GABA), a crucial inhibitory neurotransmitter in vertebrate brain. GAD produces GABA from the decarboxylation of glutamic acid. GABA is involved in development and regulation of neuroendocrine function
physiological function
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glutamic acid decarboxylase 67 (GAD67), which is a rate-limiting enzyme for GABA synthesis, GAD67 is responsible for maintaining GABA baseline levels for both neurotransmitter and metabolite. Determination of GABAergic neurons in the hippocampal CA1 region at various ages of dogs using GAD67, and extent of alterations in number and function of inhibitory GABAergic interneurons in the hippocampus as a function of age, overview. The reduction of GAD67 immunoreactive neurons in the hippocampal CA1 region may be closely related to highly susceptibility to memory loss in old aged dogs
physiological function
in the GABA synthesis pathway GAD produces GABA from L-glutamate by promoting irreversible alpha-decarboxylation reaction as the most important and rate-limiting step
physiological function
isozyme GAD65 is activated by phosphorylation on Thr95. Protein kinase C isoform epsilon is the protein kinase responsible for phosphorylation and regulation of GAD65. Role of phosphorylation of GAD65 in regulation of GABA neurotransmission. Effect of neuronal stimulation on the level of membrane associated GAD (mGAD and GAD65) and soluble GAD (sGAD and GAD67), overview
physiological function
isozyme GAD65 is activated by phosphorylation on Thr95. Protein kinase C isoform epsilon is the protein kinase responsible for phosphorylation and regulation of GAD65. Role of phosphorylation of GAD65 in regulation of GABA neurotransmission. Effect of neuronal stimulation on the level of membrane associated GAD (mGAD and GAD65) and soluble GAD (sGAD and GAD67), overview
physiological function
isozyme GAD67 is inhibited by phosphorylation. Protein kinase A is the protein kinase responsible for phosphorylation and regulation of GAD67. Role of phosphorylation of GAD65 in regulation of GABA neurotransmission. Effect of neuronal stimulation on the level of membrane associated GAD (mGAD and GAD65) and soluble GAD (sGAD and GAD67), overview
physiological function
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the activity of glutamate decarboxylase (GAD) has the ability to confer tolerance to various stress conditions including soil acidity. This pyridoxal 5'-phosphate based enzyme plays an important role in pH homeostasis by catalysing the decarboxylation of glutamate to gamma-aminobutyrate
physiological function
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the GAD system is the most important system for acid resistance in various microorganisms. GAD also acts as the only enzyme that catalyzes L-glutamate decarboxylation to gamma-aminobutyric acid (GABA)
physiological function
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the activity of glutamate decarboxylase (GAD) has the ability to confer tolerance to various stress conditions including soil acidity. This pyridoxal 5'-phosphate based enzyme plays an important role in pH homeostasis by catalysing the decarboxylation of glutamate to gamma-aminobutyrate
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physiological function
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gamma-aminobutyric acid with several physiological functions is biosynthesized via the irreversible alpha-decarboxylation of L-glutamate catalysed by glutamate decarboxylase (GAD). Streptococcus salivarius ssp. thermophilus is widely applied to the dairy
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physiological function
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glutamate decarboxylase is a key component of the glutamate-dependent acid resistance system in Brucella microti. The glutamate-dependent acid resistance system (GDAR) is the most efficient molecular system in conferring protection from acid stress, structural overview
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physiological function
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glutamate decarboxylase (GAD) catalyzes the irreversible decarboxylation of L-glutamate to the valuable food supplement gamma-aminobutyric acid (GABA)
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physiological function
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possession of the gadD1 gene correlates with a higher degree of tolerance to nisin
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physiological function
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enzyme GAD is involved in the maintainence of the cellular pH near neutral values under the acidic environments and its role is especially important for lactic acid bacteria (LAB)
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physiological function
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isozyme GAD65 is activated by phosphorylation on Thr95. Protein kinase C isoform epsilon is the protein kinase responsible for phosphorylation and regulation of GAD65. Role of phosphorylation of GAD65 in regulation of GABA neurotransmission. Effect of neuronal stimulation on the level of membrane associated GAD (mGAD and GAD65) and soluble GAD (sGAD and GAD67), overview
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physiological function
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the GAD system is the most important system for acid resistance in various microorganisms. GAD also acts as the only enzyme that catalyzes L-glutamate decarboxylation to gamma-aminobutyric acid (GABA)
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physiological function
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possession of the gadD1 gene correlates with a higher degree of tolerance to nisin
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physiological function
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the glutamate decarboxylase system is important for the acid resistance of Listeria monocytogenes. Cells accumulate intracellular 4-aminobutanoate as a standard response against acid in any medium. The GADi system is activated at milder pH values of pH 4.5 to pH 5.0 than theGADe system, pH 4.0 to pH 4.5, suggesting that GADi is the more responsive of the two and the first line of defense against acid. Model for the function of the GAD system under severe acid conditions below pH 4.5
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additional information
absence of a His residue near the C-terminus in Lactobacillus brevis GadB homologue LVIS_0079
additional information
absence of a His residue near the C-terminus in Lactobacillus brevis GadB homologue LVIS_0079
additional information
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at neutral pH the enzyme is in a compact conformation with access to the active site precluded by steric hindrance of some structural elements, a sequence of events lead to the conversion of GadB from the inactive into the active form and vice versa, structural determinants responsible for pH-dependent intracellular activation of GadB, overview. In its inactive form GadB has (i) the N-terminal residues 1-14 of each subunit mainly involved in dimerization and hexamerization, (ii) the C-terminal residues 452-466 ordered and protruding into the active site (with residues His465 and Thr466), like a plug, thus occupying the binding site of the physiological substrate glutamate, (iii) the beta-hairpin 300-313 contacting the C-terminal tail of the other subunit in the dimer as to hold it in place, structure comparisons, overview
additional information
binding of pyridoxal 5'-phosphate as well as to the active site residues Thr215 and Asp246 that promote decarboxylation
additional information
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important role of C-terminal region in the pH-dependent regulation of enzyme activity. Enzyme molecular homology modeling
additional information
residues T215 and D246 are involved in catalysis
additional information
the N-terminal fourteen residues (1-14) of homohexameric GadB forms a triple-helix bundle interdomain at acidic pH and contributes to the thermostability of GadB as the pH shifts from pH 7.6 to pH 4.6
additional information
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the N-terminal fourteen residues (1-14) of homohexameric GadB forms a triple-helix bundle interdomain at acidic pH and contributes to the thermostability of GadB as the pH shifts from pH 7.6 to pH 4.6
additional information
enzyme BmGadB has the necessary structural requirements for the binding of activating chloride ions at acidic pH and for the closure of its active site at neutral pH. BmGadB does not undergo membrane recruitment at acidic pH. For this enzyme to be functional in the glutamate-dependent acid resistance system (GDAR), some structural features must be preserved. The active form of BmGadB has internal aldimine protonated on the imine nitrogen, a pre-requisite for being catalytically competent
additional information
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enzyme BmGadB has the necessary structural requirements for the binding of activating chloride ions at acidic pH and for the closure of its active site at neutral pH. BmGadB does not undergo membrane recruitment at acidic pH. For this enzyme to be functional in the glutamate-dependent acid resistance system (GDAR), some structural features must be preserved. The active form of BmGadB has internal aldimine protonated on the imine nitrogen, a pre-requisite for being catalytically competent
additional information
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enzyme three-dimensional structure modelling, overview
additional information
hexamerization strongly contributes to the stability of the enzyme. Plant GADs possess four conserved basic residues in their first 24 N-terminal amino acid region (H5,H15, R21, and R24 in AtGAD1). Two of the four residues (H15 and R24) are located at the interfaces between dimeric units
additional information
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hexamerization strongly contributes to the stability of the enzyme. Plant GADs possess four conserved basic residues in their first 24 N-terminal amino acid region (H5,H15, R21, and R24 in AtGAD1). Two of the four residues (H15 and R24) are located at the interfaces between dimeric units
additional information
molecular modelling of the active site, docking study, using the crystal structure of isoform A of Escherichia coli GAD (GADA) in complex with glutarate (as glutamate analogue) and pyridoxal 5'-phosphate, PDB ID 1XEY
additional information
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molecular modelling of the active site, docking study, using the crystal structure of isoform A of Escherichia coli GAD (GADA) in complex with glutarate (as glutamate analogue) and pyridoxal 5'-phosphate, PDB ID 1XEY
additional information
pH rise caused by the reaction inactivates the enzyme catalyst, which is active only under acidic conditions, and consequently leads to low reaction conversions. Cross-linked aggregation method is used in order to extend the active range of GAD toward alkaline pH
additional information
structure molecular modeling
additional information
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structure molecular modeling
additional information
the GAD C-terminal region (Ile454-Thr468) plays an important role in the pH dependence of catalysis. Homology modeling of GAD
additional information
three-dimensional enzyme structure analysis, homology modeling using the crystal structure of homohexameric GadB at low pH, PDB ID 1pmm
additional information
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three-dimensional enzyme structure analysis, homology modeling using the crystal structure of homohexameric GadB at low pH, PDB ID 1pmm
additional information
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absence of a His residue near the C-terminus in Lactobacillus brevis GadB homologue LVIS_0079
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additional information
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structure molecular modeling
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additional information
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enzyme three-dimensional structure modelling, overview
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additional information
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enzyme BmGadB has the necessary structural requirements for the binding of activating chloride ions at acidic pH and for the closure of its active site at neutral pH. BmGadB does not undergo membrane recruitment at acidic pH. For this enzyme to be functional in the glutamate-dependent acid resistance system (GDAR), some structural features must be preserved. The active form of BmGadB has internal aldimine protonated on the imine nitrogen, a pre-requisite for being catalytically competent
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additional information
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the GAD C-terminal region (Ile454-Thr468) plays an important role in the pH dependence of catalysis. Homology modeling of GAD
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additional information
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residues T215 and D246 are involved in catalysis
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additional information
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important role of C-terminal region in the pH-dependent regulation of enzyme activity. Enzyme molecular homology modeling
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additional information
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binding of pyridoxal 5'-phosphate as well as to the active site residues Thr215 and Asp246 that promote decarboxylation
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