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L-alpha-Methylglutamate
?
-
-
-
-
?
L-alpha-methylglutamate + O2
laevulinic acid + NH3
-
-
-
-
?
L-Cysteic acid
?
-
-
-
-
?
L-Cysteine sulfinic acid
?
L-Glu
4-Aminobutanoate + CO2
L-glutamate
4-aminobutanoate + CO2
additional information
?
-
L-Asp
?
-
3-5% of the activity with L-Glu
-
-
?
L-Asp
?
-
Phe or 6-azauracil decrease specificity for L-Glu and increase specificity to L-Asp
-
-
?
L-Asp
?
-
2% of the activity with L-Glu
-
-
?
L-Cysteine sulfinic acid
?
-
-
-
-
?
L-Cysteine sulfinic acid
?
-
8% of the activity with L-Glu
-
-
?
L-Glu
4-Aminobutanoate + CO2
-
-
-
-
?
L-Glu
4-Aminobutanoate + CO2
-
-
-
-
?
L-Glu
4-Aminobutanoate + CO2
-
-
-
-
?
L-Glu
4-Aminobutanoate + CO2
-
-
-
-
?
L-Glu
4-Aminobutanoate + CO2
-
-
-
?
L-Glu
4-Aminobutanoate + CO2
-
-
-
-
?
L-Glu
4-Aminobutanoate + CO2
-
-
-
-
?
L-Glu
4-Aminobutanoate + CO2
-
-
-
-
?
L-Glu
4-Aminobutanoate + CO2
-
-
-
-
?
L-Glu
4-Aminobutanoate + CO2
-
-
-
-
?
L-Glu
4-Aminobutanoate + CO2
-
rate-limiting enzyme involved in the synthesis of gamma-aminobutyric acid
-
-
?
L-Glu
4-Aminobutanoate + CO2
-
-
-
-
?
L-Glu
4-Aminobutanoate + CO2
-
-
-
-
?
L-Glu
4-Aminobutanoate + CO2
-
-
-
-
?
L-Glu
4-Aminobutanoate + CO2
-
-
-
-
?
L-Glu
4-Aminobutanoate + CO2
-
-
-
-
?
L-Glu
4-Aminobutanoate + CO2
-
-
-
-
?
L-Glu
4-Aminobutanoate + CO2
-
-
-
-
?
L-Glu
4-Aminobutanoate + CO2
-
-
-
-
?
L-Glu
4-Aminobutanoate + CO2
-
6-azauracil or Phe decrease specificity for L-Glu and increased specificity to L-Asp
-
-
?
L-Glu
4-Aminobutanoate + CO2
-
-
-
-
?
L-Glu
4-Aminobutanoate + CO2
-
-
-
-
?
L-Glu
4-Aminobutanoate + CO2
-
-
-
-
?
L-Glu
4-Aminobutanoate + CO2
-
-
-
-
?
L-Glu
?
-
isoenzyme GAD2 may play a unique role in nitrogen metabolism
-
-
?
L-Glu
?
-
the enzyme is under the control of the asexual developmental cycle
-
-
?
L-Glu
?
-
production of 4-aminobutanoate, which is the major inhibitory neurotransmitter in the mammalian brain
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
GAD67 is a rate-limiting enzyme for GABA synthesis, GAD65 is important for the local control of GABA synthesis at the synaptic sites, whereas GAD67 is responsible for maintaining GABA baseline levels for both neurotransmitter and metabolite
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
GAD is the rate-limiting enzyme for GABA biosynthesis
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
GAD is the rate-limiting enzyme for GABA biosynthesis
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
ir
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
ir
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
ir
L-glutamate
4-aminobutanoate + CO2
-
-
-
ir
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
alpha-decarboxylation
-
-
?
L-glutamate
4-aminobutanoate + CO2
alpha-decarboxylation
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
the alpha-carboxyl group, leaving as CO2, is thus replaced by a cytoplasmic proton, yielding 4-aminobutanoate
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
ir
L-glutamate
4-aminobutanoate + CO2
-
the reaction does not occur, when L-glutamate concentration is more than 4fold that of L-glutamine
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
664478, 666116, 697040, 697049, 697617, 697841, 698395, 699647, 699674, 700597, 700956, 703503 -
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
GAD is the key enzyme of GABA synthesis, alterations of GABAergic neurotransmission are assumed to play a crucial role in the pathophysiology of mood disorders, overview. Increased relative density of GAD-immunoreactive neuropil, suggests the diathesis of GABAergic system specific for depressed suicidal patients
-
-
?
L-glutamate
4-aminobutanoate + CO2
GAD is the rate-limiting enzyme in controlling GABA synthesis, GABA is synthesized by GAD67 is used for the other functions such as trophic factor for neuronal development or energy source. GAD67 is constitutively active and is responsible for the basal GABA production
-
-
?
L-glutamate
4-aminobutanoate + CO2
GAD is the rate-limiting enzyme in controlling GABA synthesis, GAD65 is transiently activated in response to the extra demand of GABA in neurotransmission
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
GAD is the rate-limiting enzyme in neurotransmitter gamma-aminobutyric acid, GABA, biosynthesis
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
human glutamic acid decarboxylase 65 is a key autoantigen in type 1 diabetes
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
the isozymes are involved in autoimmune response and diseases, such as diabetes mellitus and Graves' disease, overview. Correlations between anti-GAD autoantibodies and diseases, overview
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
ir
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
ir
L-glutamate
4-aminobutanoate + CO2
-
-
-
ir
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
consumption of one H+
-
-
?
L-glutamate
4-aminobutanoate + CO2
the alpha-carboxyl group, leaving as CO2, is replaced by a cytoplasmic proton, yielding 4-aminobutanoate
-
-
?
L-glutamate
4-aminobutanoate + CO2
the alpha-carboxyl group, leaving as CO2, is thus replaced by a cytoplasmic proton, yielding 4-aminobutanoate
-
-
?
L-glutamate
4-aminobutanoate + CO2
irreversible alpha-decarboxylation of L-glutamate in the presence of a pyridoxal 5'-phosphate (PLP) as coenzyme
-
-
ir
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
the alpha-carboxyl group, leaving as CO2, is thus replaced by a cytoplasmic proton, yielding 4-aminobutanoate
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
ir
L-glutamate
4-aminobutanoate + CO2
irreversible alpha-decarboxylation of L-glutamate in the presence of a pyridoxal 5'-phosphate (PLP) as coenzyme
-
-
ir
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
ir
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
the alpha-carboxyl group, leaving as CO2, is replaced by a cytoplasmic proton, yielding 4-aminobutanoate
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
ir
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
consumption of one H+
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
the alpha-carboxyl group, leaving as CO2, is replaced by a cytoplasmic proton, yielding 4-aminobutanoate
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
695988, 697040, 697807, 699924, 700429, 700471, 700474, 700956, 705287, 705316, 705319, 706836 -
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
GAD is the rate-limiting enzyme in controlling GABA synthesis, GABA is synthesized by GAD67 is used for the other functions such as trophic factor for neuronal development or energy source. GAD67 is constitutively active and is responsible for the basal GABA production while GAD65 is transiently activated in response to the extra demand of GABA in neurotransmission
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
GAD is the rate-limiting enzyme in neurotransmitter gamma-aminobutyric acid, GABA, biosynthesis
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
GAD65-mediated GABA synthesis is critical for the consolidation of stimulus-specific fear memory. This function appears to involve a modulation of neural activity patterns in the amygdalo-hippocampal pathway as indicated by a reduction in theta frequency synchronization between the amygdala and hippocampus of Gad65-/- mice during the expression of generalized fear memory
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
GAD67 is the rate-limiting enzyme of GABA biosynthesis
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
nicotine, by activating nAChRs located on cortical or hippocampal GABAergic interneurons, can up-regulate GAD67 expression via an epigenetic mechanism
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
BmGAD can catalyze transformation of glutamate to GABA with a conversion rate of 28.5% (mol/mol) in 4 h at 30°C
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
BmGAD can catalyze transformation of glutamate to GABA with a conversion rate of 28.5% (mol/mol) in 4 h at 30°C
-
-
?
L-glutamate
4-aminobutanoate + CO2
the enzyme also catalyzes the decarboxylation of L-aspartate with slightly higher efficiency. No activity with D-glutamate
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
ir
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
GAD is the rate-limiting enzyme in controlling GABA synthesis, GABA is synthesized by GAD67 is used for the other functions such as trophic factor for neuronal development or energy source. GAD67 is constitutively active and is responsible for the basal GABA production while GAD65 is transiently activated in response to the extra demand of GABA in neurotransmission
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
GAD is the rate-limiting enzyme in neurotransmitter gamma-aminobutyric acid, GABA, biosynthesis
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
glutamate decarboxylase is the rate-limiting enzyme in the synthesis of gamma-aminobutyric acid, the most important inhibitory neurotransmitter in central nervous system
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
the enzyme activity is higher in hippocampus of old rats compared to young rats
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
ir
L-glutamate
4-aminobutanoate + CO2
irreversible alpha-decarboxylation of L-glutamate, the enzyme is highly specific for L-glutamate, no activity with D-glutamate and 23 other amino acids, overview
-
-
ir
L-glutamate
4-aminobutanoate + CO2
irreversible alpha-decarboxylation of L-glutamate
-
-
ir
L-glutamate
4-aminobutanoate + CO2
-
-
-
ir
L-glutamate
4-aminobutanoate + CO2
irreversible alpha-decarboxylation of L-glutamate
-
-
ir
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
ir
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
ir
additional information
?
-
-
no activity with L-aspartate
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
Enterococcus raffinosus strain TCCC11660 has a strong intrinsic GAD activity and shows a high yield of GABA production
-
-
?
additional information
?
-
-
enzyme GAD has a very high substrate specificity. No activity with L-glutamine, L-aspartic acid, L-arginine, L-cysteine, L-alanine, L-glycine, L-histidine, L-lysine, L-methionine, L-valine, L-phenylalanine, L-isoleucine, L-leucine, L-threonine, L-tryptophan, L-tyrosine, L-serine and L-proline. The protein also does not convert D-glutamic acid, indicating that it is strongly enantioselective as well
-
-
?
additional information
?
-
-
Enterococcus raffinosus strain TCCC11660 has a strong intrinsic GAD activity and shows a high yield of GABA production
-
-
?
additional information
?
-
-
enzyme GAD has a very high substrate specificity. No activity with L-glutamine, L-aspartic acid, L-arginine, L-cysteine, L-alanine, L-glycine, L-histidine, L-lysine, L-methionine, L-valine, L-phenylalanine, L-isoleucine, L-leucine, L-threonine, L-tryptophan, L-tyrosine, L-serine and L-proline. The protein also does not convert D-glutamic acid, indicating that it is strongly enantioselective as well
-
-
?
additional information
?
-
-
GadB together with the antiporter gadC constitutes the gad acid resistance system, which confers the ability for bacterial survival for at least 2 h in a strongly acidic environment
-
-
?
additional information
?
-
-
of the two homolous forms of glutamic acid decarboxylase, GAD65 and GAD67, only GAD65 is a common target of autoimmunity
-
-
?
additional information
?
-
-
isoform GAD65 undergoes a side reaction yielding pyridoxamine 5-phosphate, succinic semialdehyde and inactive apo enzyme
-
-
?
additional information
?
-
-
association of the two GAD isoforms in Irish individuals with Alzheimer's disease and relevant alcohol-related traits in the irish affected Sib pair study of alcohol dependence, overview. Significant association of GAD1 with initial sensitivity and age at onset of Alzheimer's disease
-
-
?
additional information
?
-
-
calpains inhibit the GAD cleavage in vivo, overview
-
-
?
additional information
?
-
-
enhanced anti-GAD antibodies are associated with several neurological diseases, possibly also the indiopathic Opsoclonus-myoclonus-ataxia syndrome, OMS. The anti-GAD antibodies might act via impairing GABAergic transmission in specific brainstem and cerebellar circuits, overview
-
-
?
additional information
?
-
-
GAD1 might be the susceptibility gene or another one being the susceptibility gene for autism, located on chromosome 2q31
-
-
?
additional information
?
-
GAD65 plays an essential role in neurotransmission, and is a typical autoantigen in several human autoimmune diseases, such as insulin-dependent diabetes mellitus, IDDM and Stiffman-Person syndrome, SPS. Posttranslational regulation of the enzyme in brain, overview
-
-
?
additional information
?
-
GAD65 plays an essential role in neurotransmission, and is a typical autoantigen in several human autoimmune diseases, such as insulin-dependent diabetes mellitus, IDDM and Stiffman-Person syndrome, SPS. Posttranslational regulation of the enzyme in brain, overview
-
-
?
additional information
?
-
-
high levels of autoantibodies to glutamic acid decarboxylase are associated with the stiff-person syndrome and type 1 diabetes mellitus and other pathologies, immunological analysis and phenotypes, overview
-
-
?
additional information
?
-
-
high titers, and sustained intrathecal synthesis, of antibodies directed against neuronal glutamic acid decarboxylase, GAD, in paraneoplastic as well as non-paraneoplastic limbic encephalitis, phenotype, overview
-
-
?
additional information
?
-
-
isozyme GAD 65 in the stiff person syndrome causes GAD65-specific T cells accumulation in the central nervous system driving the intrathecal GAD65 IgG production, T cells from the cerebrospinal fluid, mechanism, overview. GAD65-specific T cells and clonally expanded GAD65-specific B cells coexist intrathecally, where they may collaborate in the synthesis of GAD65 IgG
-
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additional information
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latent autoimmune diabetes in adults, LADA, is a form of type 1 diabetes which is associated with autoimmuno response to the glutamate decarboxylase
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additional information
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leucoencephalopathy, transverse myelopathy, and peripheral neuropathy in children with cancer are associated with anti-GAD autoantibodies, overview
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additional information
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the smaller isoform of glutamate decarboxylase, GAD65, is a major autoantigen in type 1 diabetes, antigen presentation of detergent-free glutamate decarboxylase (GAD65) is affected by human serum albumin as carrier protein, immunoresponse analysis, overview
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additional information
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enzyme activity determination by GABase assay, overview
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additional information
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enzyme activity determination by GABase assay, overview
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additional information
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enzyme activity determination by GABase assay, overview
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additional information
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enzyme/transporter pair GAD2/T2 is primarily responsible for surviving severe acid challenge, enzyme GAD1 plays a major role in growth at mildly acidic pH-values
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additional information
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enzyme/transporter pair GAD2/T2 is primarily responsible for surviving severe acid challenge, enzyme GAD1 plays a major role in growth at mildly acidic pH-values
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additional information
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susceptibility of GABAergic neurons or GAD transcript regulation within the context of ischemic injury to neocerebral cortex, overview
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additional information
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isoform GAD65 plays a major role in gamma-aminobutanoate transmission in normal physiological condition. Isoform GAD67 can serve this role under some pathological conditions
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additional information
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cortical GABAergic neurons, surviving pathological insult such as ischemia or brain trauma, exposed to glutamate in vitro, display an NMDA receptor-mediated alteration in the levels of the GABA synthesizing enzyme glutamic acid decarboxylase, isozymes GAD65 and 67, mechanism of glutamate excitotoxicity, overview
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additional information
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GAD65 plays an essential role in neurotransmission, overview
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additional information
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cortical GABAergic neurons, surviving pathological insult such as ischemia or brain trauma, exposed to glutamate in vitro, display an NMDA receptor-mediated alteration in the levels of the GABA synthesizing enzyme glutamic acid decarboxylase, isozymes GAD65 and 67, mechanism of glutamate excitotoxicity, overview
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additional information
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enzyme activity detection by rapid pH indicator method. No activity with D-glutamic acid and 2-methyl-DL-glutamic acid
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additional information
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enzyme activity detection by rapid pH indicator method. No activity with D-glutamic acid and 2-methyl-DL-glutamic acid
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additional information
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the recombinant engineered enzyme shows a broad substrate specificity
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additional information
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calpains inhibit the GAD cleavage in vivo, overview
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additional information
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chronic systemic administration of an agonist of dopamine D1/D5-preferring receptors increases GAD mRNA levels in striatonigral neurons in intact and dopamine-depleted rats. striatal GAD67 mRNA levels were negatively correlated with nigral alpha1 mRNA levels in the dopamine-depleted but not dopamine-intact side. down-regulation of nigral GABAA receptors is linked to the increase in striatal GAD67 mRNA levels in the dopamine-depleted striatum. Different signaling pathways are involved in the modulation by dopamine D1/D5 receptors of GAD65 and GAD67 mRNA levels in striatonigral neurons, overview
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additional information
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GAD65 plays an essential role in neurotransmission, overview
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additional information
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regular performance of exercise results in extensive changes in the forebrain GABAergic system that may be implicated in the changes in stress sensitivity and emotionality observed in exercising subjects, overview
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additional information
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SDF1alpha/CXCR4/G protein/ERK signaling induces the expression of the GAD67 system via Egr1 activation, a mechanism that may promote the maturation of GABAergic neurons during development
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additional information
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the enzyme is highly substrate specific. No activity with D-glutamate and no activity with L-Asp, L-Ser, L-His, Gly, L-Thr, L-Ala, L-Arg, L-Tyr, L-Cys, L-Val, L-Met, L-Trp, L-Phe, L-Ile, L-Leu, L-Lys, and L-Pro
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additional information
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the enzyme is highly substrate specific. No activity with D-glutamate and no activity with L-Asp, L-Ser, L-His, Gly, L-Thr, L-Ala, L-Arg, L-Tyr, L-Cys, L-Val, L-Met, L-Trp, L-Phe, L-Ile, L-Leu, L-Lys, and L-Pro
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additional information
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the activity is closely associated with its developmental status and may represent a link between differentiation events and energy metabolism
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(4Z,7E)-N,N'-dihydroxy-2,2-dimethyl-5,6-dihydro-2H-benzimidazole-4,7-diimine
(5Z)-2-amino-5-(2-nitrobenzylidene)-1,3-thiazol-4(5H)-one
(E)-pent-2-enoic acid
-
20% inhibition at 0.01 mg/ml
(NH4)2SO4
92% inhibition at 2 mM
1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl 2,3,4-tri-O-acetylpentopyranoside
1-(2-nitrobenzyl)-1H-indole-3-carbaldehyde
1-Methylimidazole
-
about 85% residual activity at 5 mM, about 77% residual activity at 10 mM, about 65% residual activity at 20 mM
10H-indeno[2,1-e]tetrazolo[1,5-b][1,2,4]triazin-10-one
2,4-bis[2-(4-hydroxyphenyl)propan-2-yl]phenol
2,6-pyridine dicarboxylic acid
-
-
2-(benzylsulfanyl)-3-(morpholin-4-yl)-2,3-dihydronaphthalene-1,4-dione
2-chloro-N-[5-([2-oxo-2-[(4-sulfamoylphenyl)amino]ethyl]sulfanyl)-1,3,4-thiadiazol-2-yl]acetamide
2-hydroxy-2-(2-hydroxy-6-oxocyclohex-2-en-1-yl)-1H-indene-1,3(2H)-dione
2-Methyl-3,4-didehydroglutamic acid
-
-
2-thioxo-3-[(E)-(3,3,5-trimethylcyclohexylidene)amino]-1,3-thiazolidin-4-one
2-[(2-chloro-5-nitrobenzoyl)amino]-5-iodobenzoic acid
2-[(3-formyl-1H-indol-1-yl)methyl]benzonitrile
3,3'-(4H-1,2,4-triazole-3,5-diyl)bis(4-nitro-1,2,5-oxadiazole)
3,4,5-Trihydroxybenzoic acid
3,4-dihydroxybenzoic acid
3,4-dihydroxyphenylacetic acid
-
-
3,5-Dihydroxybenzoic acid
3-[(2E)-2-[1-(3,4-dimethoxyphenyl)ethylidene]hydrazinyl]benzoic acid
3-[(E)-(2,6-difluorobenzylidene)amino]-2-thioxo-1,3-thiazolidin-4-one
3-[(E)-(4-methoxybenzylidene)amino]-2-thioxo-1,3-thiazolidin-4-one
4'-deoxypyridoxine-5'-phosphate
-
about 60% inhibition of GAD65 at 3.5 mM, GAD67 is hardly affected
4'-O-methylpyridoxine-5'-phosphate
-
decreases activity of GAD65 in unphysiologically high concentrations, about 60% inhibition at 3.5 mM. GAD67 activity is hardly affected
4,4'-(phenylmethanediyl)bis[2-(4-chlorophenyl)-5-methyl-2,4-dihydro-3H-pyrazol-3-one]
4,4'-[(4-hydroxyphenyl)methanediyl]bis(2-heptyl-5-methyl-2,4-dihydro-3H-pyrazol-3-one)
4,5-Dihydroxyisophthalic acid
4-(morpholin-4-yl)naphthalene-1,2-dione
4-(piperidin-1-yl)naphthalene-1,2-dione
4-Aminohex-5-ynoic acid
-
-
4-methylimidazole
-
about 75% residual activity at 5 mM, about 70% residual activity at 10 mM, about 58% residual activity at 20 mM
4-nitro-1,6-dihydrobenzo[1,2-d:3,4-d']bis[1,2,3]triazole
4-nitro-7-[[(1-phenyl-1H-tetrazol-5-yl)sulfanyl]methyl]-2,1,3-benzothiadiazole
4-[(1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl)sulfanyl]butanoic acid
5,5'-dithiobis(2-nitrobenzoate)
5,6-dichloro-2,1,3-benzothiadiazole-4,7-diol
5-[(E)-benzylideneamino]-6-[(2-hydroxyethyl)amino]pyrimidine-2,4(1H,3H)-dione
5-[(E)-[[1-(2-chlorobenzyl)-1H-indol-3-yl]methylidene]amino]-1,3-dihydro-2H-benzimidazol-2-one
5-[[5-hydroxy-3-methyl-1-(4-methylphenyl)-1H-pyrazol-4-yl]methylidene]-1,3-diphenyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
6,11-dioxo-5a,6,11,11a-tetrahydronaphtho[2',3':4,5][1,3]thiazolo[3,2-a]pyridin-12-ium
9H-indeno[1,2-b][1,2,5]oxadiazolo[3,4-e]pyrazin-9-one
Ag+
58.3% residual activity at 2 mM
Al3+
91.2% residual activity at 2 mM
Aminoethylylisothiouronium bromide
-
-
ATP
-
in presence of leupeptin in freshly prepared homogenates. Inhibition of enzyme from homogenates stored without Triton X-100 for 24 h at 4°C
BaCl2
-
1 mM, 78% inhibition
beta-Methylene-DL-Asp
-
-
biphenyl-3,3'-dicarbaldehyde
CdCl2
-
1 mM, 38% inhibition
CH3COOH
57.4% residual activity at 2 mM
Chloroacetamide
-
no inhibition at pH 4.6, marked inhibition at pH 6.0 or higher
Co2+
-
about 70% inhibition of at 5 mM
cyclosporin A
-
up to 0.3 mM, partial inhibition of activity in homogenate, but not in the supernatant obtained after centrifuging the homogenate
Cys
-
enzyme from embryos
D-erythro-4-fluoroglutamate
-
-
DL-4-Amino-4-phosphonobutyrate
-
-
DL-alpha-Aminoadipic acid
-
-
DL-alpha-Methylglutamate
-
-
FeCl3
-
1 mM, 65% inhibition
ginsenosides
-
23% inhibition at 0.01 mg/ml, ethanol extract of Panax quinquefolius, different glycoside derivatives, overview
-
Glutamate gamma-hydroxamate
-
weak
isoniazide
isoniazide-induced seizures are mediated primarily through competition with the cofactor pyridoxal 5'-phosphate resulting in the inhibition of GAD activity
Isonicotinic acid hydrazide
-
-
KCl
5.8% inhibition at 5 mM; 94.2% remaining activity at 5 mM
L-Asn
-
inhibits 4% at 1 mM
L-Asp
-
inhibits 20% at 1 mM
L-aspartate beta-hydroxamate
-
weak
L-Cysteine hydrochloride
-
-
L-cysteine sulfinic acid
-
-
L-erythro-4-fluoroglutamate
-
-
LiCl
6.1% inhibition at 5 mM; 93.9% remaining activity at 5 mM
methyl 2-amino-3-oxo-3H-phenothiazine-1-carboxylate
methyl 2-[[(2-methylimidazo[1,2-a]pyridin-3-yl)carbonyl]amino]benzoate
Mn2+
92.6% residual activity at 2 mM
N-(2-hydroxy-1,3-dioxo-2,3-dihydro-1H-inden-2-yl)benzamide
N-[4,7-dioxo-6-(phenylamino)-4,7-dihydro-2,1,3-benzoxadiazol-5-yl]acetamide
N-[4,7-dioxo-6-(piperidin-1-yl)-4,7-dihydro-2,1,3-benzoxadiazol-5-yl]acetamide
naphtho[2',3':4,5]imidazo[1,2-a]pyridine-6,11-dione
Pb(CH3COO)2
-
1 mM, 37% inhibition
PCMB
-
0.1 mM, 68.5% inhibition at pH 4.6, irreversible
reduced glutathione
-
enzyme from embryos
Substituted dicarboxylic acids
-
-
-
[(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)oxy]acetic acid
(4Z,7E)-N,N'-dihydroxy-2,2-dimethyl-5,6-dihydro-2H-benzimidazole-4,7-diimine
-
(4Z,7E)-N,N'-dihydroxy-2,2-dimethyl-5,6-dihydro-2H-benzimidazole-4,7-diimine
-
(4Z,7E)-N,N'-dihydroxy-2,2-dimethyl-5,6-dihydro-2H-benzimidazole-4,7-diimine
-
(4Z,7E)-N,N'-dihydroxy-2,2-dimethyl-5,6-dihydro-2H-benzimidazole-4,7-diimine
-
(5Z)-2-amino-5-(2-nitrobenzylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-amino-5-(2-nitrobenzylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-amino-5-(2-nitrobenzylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-amino-5-(2-nitrobenzylidene)-1,3-thiazol-4(5H)-one
-
1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl 2,3,4-tri-O-acetylpentopyranoside
-
1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl 2,3,4-tri-O-acetylpentopyranoside
-
1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl 2,3,4-tri-O-acetylpentopyranoside
-
1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl 2,3,4-tri-O-acetylpentopyranoside
-
1-(2-nitrobenzyl)-1H-indole-3-carbaldehyde
-
1-(2-nitrobenzyl)-1H-indole-3-carbaldehyde
-
1-(2-nitrobenzyl)-1H-indole-3-carbaldehyde
-
1-(2-nitrobenzyl)-1H-indole-3-carbaldehyde
-
10H-indeno[2,1-e]tetrazolo[1,5-b][1,2,4]triazin-10-one
-
10H-indeno[2,1-e]tetrazolo[1,5-b][1,2,4]triazin-10-one
-
10H-indeno[2,1-e]tetrazolo[1,5-b][1,2,4]triazin-10-one
-
10H-indeno[2,1-e]tetrazolo[1,5-b][1,2,4]triazin-10-one
-
2,4-bis[2-(4-hydroxyphenyl)propan-2-yl]phenol
-
2,4-bis[2-(4-hydroxyphenyl)propan-2-yl]phenol
-
2,4-bis[2-(4-hydroxyphenyl)propan-2-yl]phenol
-
2,4-bis[2-(4-hydroxyphenyl)propan-2-yl]phenol
-
2-(benzylsulfanyl)-3-(morpholin-4-yl)-2,3-dihydronaphthalene-1,4-dione
-
2-(benzylsulfanyl)-3-(morpholin-4-yl)-2,3-dihydronaphthalene-1,4-dione
-
2-(benzylsulfanyl)-3-(morpholin-4-yl)-2,3-dihydronaphthalene-1,4-dione
-
2-(benzylsulfanyl)-3-(morpholin-4-yl)-2,3-dihydronaphthalene-1,4-dione
-
2-chloro-N-[5-([2-oxo-2-[(4-sulfamoylphenyl)amino]ethyl]sulfanyl)-1,3,4-thiadiazol-2-yl]acetamide
-
2-chloro-N-[5-([2-oxo-2-[(4-sulfamoylphenyl)amino]ethyl]sulfanyl)-1,3,4-thiadiazol-2-yl]acetamide
-
2-chloro-N-[5-([2-oxo-2-[(4-sulfamoylphenyl)amino]ethyl]sulfanyl)-1,3,4-thiadiazol-2-yl]acetamide
-
2-chloro-N-[5-([2-oxo-2-[(4-sulfamoylphenyl)amino]ethyl]sulfanyl)-1,3,4-thiadiazol-2-yl]acetamide
-
2-hydroxy-2-(2-hydroxy-6-oxocyclohex-2-en-1-yl)-1H-indene-1,3(2H)-dione
-
2-hydroxy-2-(2-hydroxy-6-oxocyclohex-2-en-1-yl)-1H-indene-1,3(2H)-dione
-
2-hydroxy-2-(2-hydroxy-6-oxocyclohex-2-en-1-yl)-1H-indene-1,3(2H)-dione
-
2-hydroxy-2-(2-hydroxy-6-oxocyclohex-2-en-1-yl)-1H-indene-1,3(2H)-dione
-
2-mercaptoethanol
-
enzyme form I and II from embryos
2-mercaptoethanol
-
1 mM, 79% inhibition
2-oxoglutarate
-
-
2-thioxo-3-[(E)-(3,3,5-trimethylcyclohexylidene)amino]-1,3-thiazolidin-4-one
-
2-thioxo-3-[(E)-(3,3,5-trimethylcyclohexylidene)amino]-1,3-thiazolidin-4-one
-
2-thioxo-3-[(E)-(3,3,5-trimethylcyclohexylidene)amino]-1,3-thiazolidin-4-one
-
2-thioxo-3-[(E)-(3,3,5-trimethylcyclohexylidene)amino]-1,3-thiazolidin-4-one
-
2-[(2-chloro-5-nitrobenzoyl)amino]-5-iodobenzoic acid
-
2-[(2-chloro-5-nitrobenzoyl)amino]-5-iodobenzoic acid
-
2-[(2-chloro-5-nitrobenzoyl)amino]-5-iodobenzoic acid
-
2-[(2-chloro-5-nitrobenzoyl)amino]-5-iodobenzoic acid
-
2-[(3-formyl-1H-indol-1-yl)methyl]benzonitrile
-
2-[(3-formyl-1H-indol-1-yl)methyl]benzonitrile
-
2-[(3-formyl-1H-indol-1-yl)methyl]benzonitrile
-
2-[(3-formyl-1H-indol-1-yl)methyl]benzonitrile
-
3,3'-(4H-1,2,4-triazole-3,5-diyl)bis(4-nitro-1,2,5-oxadiazole)
-
3,3'-(4H-1,2,4-triazole-3,5-diyl)bis(4-nitro-1,2,5-oxadiazole)
-
3,3'-(4H-1,2,4-triazole-3,5-diyl)bis(4-nitro-1,2,5-oxadiazole)
-
3,3'-(4H-1,2,4-triazole-3,5-diyl)bis(4-nitro-1,2,5-oxadiazole)
-
3,4,5-Trihydroxybenzoic acid
-
weak
3,4,5-Trihydroxybenzoic acid
-
-
3,4,5-Trihydroxybenzoic acid
-
-
3,4-dihydroxybenzoic acid
-
weak
3,4-dihydroxybenzoic acid
-
-
3,4-dihydroxybenzoic acid
-
-
3,5-Dihydroxybenzoic acid
-
weak
3,5-Dihydroxybenzoic acid
-
-
3-Mercaptopropionic acid
-
-
3-Mercaptopropionic acid
-
-
3-Mercaptopropionic acid
-
43% inhibition at 0.1 mM
3-Mercaptopropionic acid
-
3-Mercaptopropionic acid
-
-
3-Mercaptopropionic acid
-
-
3-Mercaptopropionic acid
-
-
3-[(2E)-2-[1-(3,4-dimethoxyphenyl)ethylidene]hydrazinyl]benzoic acid
-
3-[(2E)-2-[1-(3,4-dimethoxyphenyl)ethylidene]hydrazinyl]benzoic acid
-
3-[(2E)-2-[1-(3,4-dimethoxyphenyl)ethylidene]hydrazinyl]benzoic acid
-
3-[(2E)-2-[1-(3,4-dimethoxyphenyl)ethylidene]hydrazinyl]benzoic acid
-
3-[(E)-(2,6-difluorobenzylidene)amino]-2-thioxo-1,3-thiazolidin-4-one
-
3-[(E)-(2,6-difluorobenzylidene)amino]-2-thioxo-1,3-thiazolidin-4-one
-
3-[(E)-(2,6-difluorobenzylidene)amino]-2-thioxo-1,3-thiazolidin-4-one
-
3-[(E)-(2,6-difluorobenzylidene)amino]-2-thioxo-1,3-thiazolidin-4-one
-
3-[(E)-(4-methoxybenzylidene)amino]-2-thioxo-1,3-thiazolidin-4-one
-
3-[(E)-(4-methoxybenzylidene)amino]-2-thioxo-1,3-thiazolidin-4-one
-
3-[(E)-(4-methoxybenzylidene)amino]-2-thioxo-1,3-thiazolidin-4-one
-
3-[(E)-(4-methoxybenzylidene)amino]-2-thioxo-1,3-thiazolidin-4-one
-
4,4'-(phenylmethanediyl)bis[2-(4-chlorophenyl)-5-methyl-2,4-dihydro-3H-pyrazol-3-one]
-
4,4'-(phenylmethanediyl)bis[2-(4-chlorophenyl)-5-methyl-2,4-dihydro-3H-pyrazol-3-one]
-
4,4'-(phenylmethanediyl)bis[2-(4-chlorophenyl)-5-methyl-2,4-dihydro-3H-pyrazol-3-one]
-
4,4'-(phenylmethanediyl)bis[2-(4-chlorophenyl)-5-methyl-2,4-dihydro-3H-pyrazol-3-one]
-
4,4'-[(4-hydroxyphenyl)methanediyl]bis(2-heptyl-5-methyl-2,4-dihydro-3H-pyrazol-3-one)
-
4,4'-[(4-hydroxyphenyl)methanediyl]bis(2-heptyl-5-methyl-2,4-dihydro-3H-pyrazol-3-one)
-
4,4'-[(4-hydroxyphenyl)methanediyl]bis(2-heptyl-5-methyl-2,4-dihydro-3H-pyrazol-3-one)
-
4,4'-[(4-hydroxyphenyl)methanediyl]bis(2-heptyl-5-methyl-2,4-dihydro-3H-pyrazol-3-one)
-
4,5-Dihydroxyisophthalic acid
-
weak
4,5-Dihydroxyisophthalic acid
-
-
4-(morpholin-4-yl)naphthalene-1,2-dione
-
4-(morpholin-4-yl)naphthalene-1,2-dione
-
4-(morpholin-4-yl)naphthalene-1,2-dione
-
4-(morpholin-4-yl)naphthalene-1,2-dione
-
4-(piperidin-1-yl)naphthalene-1,2-dione
-
4-(piperidin-1-yl)naphthalene-1,2-dione
-
4-(piperidin-1-yl)naphthalene-1,2-dione
-
4-(piperidin-1-yl)naphthalene-1,2-dione
-
4-bromoisophthalic acid
-
-
4-bromoisophthalic acid
-
-
4-nitro-1,6-dihydrobenzo[1,2-d:3,4-d']bis[1,2,3]triazole
-
4-nitro-1,6-dihydrobenzo[1,2-d:3,4-d']bis[1,2,3]triazole
-
4-nitro-1,6-dihydrobenzo[1,2-d:3,4-d']bis[1,2,3]triazole
-
4-nitro-1,6-dihydrobenzo[1,2-d:3,4-d']bis[1,2,3]triazole
-
4-nitro-7-[[(1-phenyl-1H-tetrazol-5-yl)sulfanyl]methyl]-2,1,3-benzothiadiazole
-
4-nitro-7-[[(1-phenyl-1H-tetrazol-5-yl)sulfanyl]methyl]-2,1,3-benzothiadiazole
-
4-nitro-7-[[(1-phenyl-1H-tetrazol-5-yl)sulfanyl]methyl]-2,1,3-benzothiadiazole
-
4-nitro-7-[[(1-phenyl-1H-tetrazol-5-yl)sulfanyl]methyl]-2,1,3-benzothiadiazole
-
4-[(1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl)sulfanyl]butanoic acid
-
4-[(1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl)sulfanyl]butanoic acid
-
4-[(1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl)sulfanyl]butanoic acid
-
4-[(1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl)sulfanyl]butanoic acid
-
5,5'-dithiobis(2-nitrobenzoate)
-
0.1 mM, 50.3% inhibition at pH 4.6, irreversible
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,6-dichloro-2,1,3-benzothiadiazole-4,7-diol
-
5,6-dichloro-2,1,3-benzothiadiazole-4,7-diol
-
5,6-dichloro-2,1,3-benzothiadiazole-4,7-diol
-
5,6-dichloro-2,1,3-benzothiadiazole-4,7-diol
-
5-[(E)-benzylideneamino]-6-[(2-hydroxyethyl)amino]pyrimidine-2,4(1H,3H)-dione
-
5-[(E)-benzylideneamino]-6-[(2-hydroxyethyl)amino]pyrimidine-2,4(1H,3H)-dione
-
5-[(E)-benzylideneamino]-6-[(2-hydroxyethyl)amino]pyrimidine-2,4(1H,3H)-dione
-
5-[(E)-benzylideneamino]-6-[(2-hydroxyethyl)amino]pyrimidine-2,4(1H,3H)-dione
-
5-[(E)-[[1-(2-chlorobenzyl)-1H-indol-3-yl]methylidene]amino]-1,3-dihydro-2H-benzimidazol-2-one
-
5-[(E)-[[1-(2-chlorobenzyl)-1H-indol-3-yl]methylidene]amino]-1,3-dihydro-2H-benzimidazol-2-one
-
5-[(E)-[[1-(2-chlorobenzyl)-1H-indol-3-yl]methylidene]amino]-1,3-dihydro-2H-benzimidazol-2-one
-
5-[(E)-[[1-(2-chlorobenzyl)-1H-indol-3-yl]methylidene]amino]-1,3-dihydro-2H-benzimidazol-2-one
-
5-[[5-hydroxy-3-methyl-1-(4-methylphenyl)-1H-pyrazol-4-yl]methylidene]-1,3-diphenyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
5-[[5-hydroxy-3-methyl-1-(4-methylphenyl)-1H-pyrazol-4-yl]methylidene]-1,3-diphenyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
5-[[5-hydroxy-3-methyl-1-(4-methylphenyl)-1H-pyrazol-4-yl]methylidene]-1,3-diphenyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
5-[[5-hydroxy-3-methyl-1-(4-methylphenyl)-1H-pyrazol-4-yl]methylidene]-1,3-diphenyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
6,11-dioxo-5a,6,11,11a-tetrahydronaphtho[2',3':4,5][1,3]thiazolo[3,2-a]pyridin-12-ium
-
6,11-dioxo-5a,6,11,11a-tetrahydronaphtho[2',3':4,5][1,3]thiazolo[3,2-a]pyridin-12-ium
-
6,11-dioxo-5a,6,11,11a-tetrahydronaphtho[2',3':4,5][1,3]thiazolo[3,2-a]pyridin-12-ium
-
6,11-dioxo-5a,6,11,11a-tetrahydronaphtho[2',3':4,5][1,3]thiazolo[3,2-a]pyridin-12-ium
-
9H-indeno[1,2-b][1,2,5]oxadiazolo[3,4-e]pyrazin-9-one
-
9H-indeno[1,2-b][1,2,5]oxadiazolo[3,4-e]pyrazin-9-one
-
9H-indeno[1,2-b][1,2,5]oxadiazolo[3,4-e]pyrazin-9-one
-
9H-indeno[1,2-b][1,2,5]oxadiazolo[3,4-e]pyrazin-9-one
-
AgNO3
44.4% inhibition at 2 mM
AgNO3
79% inhibition at 2 mM
AgNO3
-
1 mM, 68% residual activity
AgNO3
complete inhibition at 5mM
AgNO3
complete inhibition at 5 mM
allylglycine
-
-
Asp
-
-
betulinic acid
-
27% inhibition at 0.01 mg/ml
biphenyl-3,3'-dicarbaldehyde
-
biphenyl-3,3'-dicarbaldehyde
-
biphenyl-3,3'-dicarbaldehyde
-
biphenyl-3,3'-dicarbaldehyde
-
Ca2+
about 5% inhibition at 2 mM
Ca2+
activates at 0.2 mM, slight inhibition above 1 mM
CaCl2
-
1 mM, 31% inhibition
CaCl2
95.4% remaining activity at 5 mM
carboxymethoxylamine
-
Cd2+
-
-
Chelidamic acid
-
weak
Chelidonic acid
-
-
CoCl2
62% inhibition at 5mM
CoCl2
37.9% remaining activity at 5 mM; 62.1% inhibition at 5 mM
Cu2+
-
about 60% inhibition of at 5 mM
Cu2+
almost complete inhibition at 2 mM
Cu2+
strong inhibition at 3 mM
CuCl2
-
CuCl2
-
1 mM, 43% inhibition
CuSO4
56.8% inhibition at 2 mM
CuSO4
93% inhibition at 5mM
CuSO4
92.4% inhibition at 5 mM
D-Glu
-
-
dithiothreitol
-
enzyme from embryos
dithiothreitol
-
1 mM, complete inhibition
DL-Penicillamine
-
-
EDTA
-
1 mM, 77% inhibition
EDTA
91.2% residual activity at 2 mM
EGTA
-
0.5 mM, 20% inhibition
Fe2+
-
over 80% inhibition of at 5 mM
Fe2+
50% inhibition at 2 mM
Fe3+
85% inhibition at 2 mM
FeSO4
92% inhibition at 5mM
FeSO4
91.9% inhibition at 5 mM
Glutarate
-
inhibits 42% at 1 mM
Hg2+
-
-
Hg2+
37.7% residual activity at 2 mM
HgCl2
-
0.01 mM, 80.1% inhibition at pH 4.6, irreversible
HgCl2
-
1 mM, 89% inhibition
HgCl2
-
1 mM, 31.5% residual activity
isophthalic acid
-
-
KI
-
-
KI
-
1 mM, 55% residual activity
L-Glu
-
inhibits 25% at 1 mM
L-Glu
-
substrate inhibition at high concentrations
Mercaptosuccinic acid
-
-
Mercaptosuccinic acid
-
-
methyl 2-amino-3-oxo-3H-phenothiazine-1-carboxylate
-
methyl 2-amino-3-oxo-3H-phenothiazine-1-carboxylate
-
methyl 2-amino-3-oxo-3H-phenothiazine-1-carboxylate
-
methyl 2-amino-3-oxo-3H-phenothiazine-1-carboxylate
-
methyl 2-[[(2-methylimidazo[1,2-a]pyridin-3-yl)carbonyl]amino]benzoate
-
methyl 2-[[(2-methylimidazo[1,2-a]pyridin-3-yl)carbonyl]amino]benzoate
-
methyl 2-[[(2-methylimidazo[1,2-a]pyridin-3-yl)carbonyl]amino]benzoate
-
methyl 2-[[(2-methylimidazo[1,2-a]pyridin-3-yl)carbonyl]amino]benzoate
-
Mg2+
90.1% residual activity at 2 mM
MgCl2
84% inhibition at 2 mM
MgCl2
-
1 mM, 46% inhibition
MnSO4
88% inhibition at 5mM
MnSO4
87.9% inhibition at 5 mM
N-(2-hydroxy-1,3-dioxo-2,3-dihydro-1H-inden-2-yl)benzamide
-
N-(2-hydroxy-1,3-dioxo-2,3-dihydro-1H-inden-2-yl)benzamide
-
N-(2-hydroxy-1,3-dioxo-2,3-dihydro-1H-inden-2-yl)benzamide
-
N-(2-hydroxy-1,3-dioxo-2,3-dihydro-1H-inden-2-yl)benzamide
-
N-[4,7-dioxo-6-(phenylamino)-4,7-dihydro-2,1,3-benzoxadiazol-5-yl]acetamide
-
N-[4,7-dioxo-6-(phenylamino)-4,7-dihydro-2,1,3-benzoxadiazol-5-yl]acetamide
-
N-[4,7-dioxo-6-(phenylamino)-4,7-dihydro-2,1,3-benzoxadiazol-5-yl]acetamide
-
N-[4,7-dioxo-6-(phenylamino)-4,7-dihydro-2,1,3-benzoxadiazol-5-yl]acetamide
-
N-[4,7-dioxo-6-(piperidin-1-yl)-4,7-dihydro-2,1,3-benzoxadiazol-5-yl]acetamide
-
N-[4,7-dioxo-6-(piperidin-1-yl)-4,7-dihydro-2,1,3-benzoxadiazol-5-yl]acetamide
-
N-[4,7-dioxo-6-(piperidin-1-yl)-4,7-dihydro-2,1,3-benzoxadiazol-5-yl]acetamide
-
N-[4,7-dioxo-6-(piperidin-1-yl)-4,7-dihydro-2,1,3-benzoxadiazol-5-yl]acetamide
-
Na2SO4
-
Na2SO4
10% inhibition at 5mM
Na2SO4
9.8% inhibition at 5 mM
NaCl
61.5% inhibition at 10 mM
naphtho[2',3':4,5]imidazo[1,2-a]pyridine-6,11-dione
-
naphtho[2',3':4,5]imidazo[1,2-a]pyridine-6,11-dione
-
naphtho[2',3':4,5]imidazo[1,2-a]pyridine-6,11-dione
-
naphtho[2',3':4,5]imidazo[1,2-a]pyridine-6,11-dione
-
NEM
-
no inhibition at pH 4.6, marked inhibition at pH 6.0 or higher
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
SDS
-
1 mM, 26% inhibition
SDS
66.9% residual activity at 40 mM
ursolic acid
-
11.2% inhibition at 0.01 mg/ml
valerenic acid
-
20% inhibition at 0.01 mg/ml
Zn2+
-
about 80% inhibition of at 5 mM
Zn2+
about 20% inhibition at 2 mM
ZnCl2
-
ZnCl2
-
1 mM, 37% inhibition
ZnSO4
80.4% inhibition at 5mM
ZnSO4
80.4% inhibition at 5 mM
[(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)oxy]acetic acid
-
[(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)oxy]acetic acid
-
[(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)oxy]acetic acid
-
[(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)oxy]acetic acid
-
additional information
inhibitor screening, overview
-
additional information
-
inhibitor screening, overview
-
additional information
inhibitor screening, overview
-
additional information
-
inhibitor screening, overview
-
additional information
the C-terminal domain by entrancing into the active site is responsible for autoinhibition of the enzyme at neutral pH
-
additional information
-
the C-terminal domain by entrancing into the active site is responsible for autoinhibition of the enzyme at neutral pH
-
additional information
-
the glutamate decarboxylase activity of p42 is not inhibited by high concentrations of Mn2+
-
additional information
-
ionomycin inhibits the expression of the full-length enzyme, but not of the truncated mutant, while mu-calpain and calpastatin inhibit the truncated enzyme, but not the full-length wild-type enzyme in the synaptosome, overview
-
additional information
-
enzyme inhibition by glutamic acid decarboxylase autoantibodies, overview
-
additional information
-
aasiaticoside does not inhibit GAD activity even at the highest dose of 0.03 mg/ml. Allylglycine does not inhibit GAD activity even at the highest dose of 0.1 mM; asiaticoside does not inhibit GAD activity even at the highest dose of 0.03 mg/ml, allylglycine exhibits no enzyme inhibition even at the highest dose of 0.1 mM; minor inhibition is seen with the ethanol extract of Panax quinquefolius (23%), betulinic acid (27%), and valerenic acid (20%); minor inhibition is seen with the ethanol extract of Panax quinquefolius (ginsenosides) (23%)
-
additional information
-
identification of inhibitory antibodies, overview
-
additional information
isozyme GAD67 is inhibited by phosphorylation
-
additional information
isozyme GAD67 is inhibited by phosphorylation
-
additional information
-
isozyme GAD67 is inhibited by phosphorylation
-
additional information
ginsenosides in ginseng extract, high content of Rb1, inhibit the enzyme
-
additional information
-
under acidic conditions, glutamate/4-aminobutanoate antiport is impaired in minimal media but not in rich ones
-
additional information
-
-
-
additional information
-
glutamate reduces the expression of isozymes GAD65 and GAD67, glutamate's suppressing effect on GAD protein isoforms is significantly attenuated by preincubation with the cysteine protease inhibitor N-acetyl-L-leucyl-L-leucyl-L-norleucinal via blockade of calpain and cathepsin protease activities, overview
-
additional information
-
downregulation of reelin and GAD67 expression by the increase of DNA-methyltransferase 1-mediated hypermethylation of promoters in GABAergic interneurons of the telencephalon
-
additional information
inhibitor screening, overview; inhibitor screening, overview
-
additional information
inhibitor screening, overview; inhibitor screening, overview
-
additional information
-
inhibitor screening, overview; inhibitor screening, overview
-
additional information
-
ionomycin inhibits the expression of the full-length enzyme, but not of the truncated mutant, while mu-calpain and calpastatin inhibit the truncated enzyme, but not the full-length wild-type enzyme in the synaptosome, overview
-
additional information
-
chronic mild stress leads to 60% reduced enzyme activity in old rats, which is reversible by neuronal nitric oxide synthase inhibitor 7-nitroindazole, overview
-
additional information
inhibitor screening, overview
-
additional information
-
inhibitor screening, overview
-
additional information
poor inhibition by LiCl, CaCl2, and KCl. MgCl2 and NaCl have no effect on enzyme activity
-
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0.0123 - 0.03
(4Z,7E)-N,N'-dihydroxy-2,2-dimethyl-5,6-dihydro-2H-benzimidazole-4,7-diimine
0.0033 - 0.0418
(5Z)-2-amino-5-(2-nitrobenzylidene)-1,3-thiazol-4(5H)-one
0.0038 - 0.012
1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl 2,3,4-tri-O-acetylpentopyranoside
0.0055 - 0.0142
1-(2-nitrobenzyl)-1H-indole-3-carbaldehyde
0.002 - 4
10H-indeno[2,1-e]tetrazolo[1,5-b][1,2,4]triazin-10-one
0.0051 - 0.1
2,4-bis[2-(4-hydroxyphenyl)propan-2-yl]phenol
0.0073 - 0.0209
2-(benzylsulfanyl)-3-(morpholin-4-yl)-2,3-dihydronaphthalene-1,4-dione
0.0052 - 0.1
2-chloro-N-[5-([2-oxo-2-[(4-sulfamoylphenyl)amino]ethyl]sulfanyl)-1,3,4-thiadiazol-2-yl]acetamide
0.0042 - 0.0108
2-hydroxy-2-(2-hydroxy-6-oxocyclohex-2-en-1-yl)-1H-indene-1,3(2H)-dione
0.0075 - 0.014
2-thioxo-3-[(E)-(3,3,5-trimethylcyclohexylidene)amino]-1,3-thiazolidin-4-one
0.0165 - 0.1
2-[(2-chloro-5-nitrobenzoyl)amino]-5-iodobenzoic acid
0.0082 - 0.014
2-[(3-formyl-1H-indol-1-yl)methyl]benzonitrile
0.0002 - 0.0212
3,3'-(4H-1,2,4-triazole-3,5-diyl)bis(4-nitro-1,2,5-oxadiazole)
0.0123
3-Mercaptopropionic acid
0.0202 - 0.1
3-[(2E)-2-[1-(3,4-dimethoxyphenyl)ethylidene]hydrazinyl]benzoic acid
0.0063 - 0.0122
3-[(E)-(2,6-difluorobenzylidene)amino]-2-thioxo-1,3-thiazolidin-4-one
0.0072 - 0.099
4,4'-(phenylmethanediyl)bis[2-(4-chlorophenyl)-5-methyl-2,4-dihydro-3H-pyrazol-3-one]
0.013 - 0.0226
4,4'-[(4-hydroxyphenyl)methanediyl]bis(2-heptyl-5-methyl-2,4-dihydro-3H-pyrazol-3-one)
0.0029 - 0.0045
4-(morpholin-4-yl)naphthalene-1,2-dione
0.003 - 0.0053
4-(piperidin-1-yl)naphthalene-1,2-dione
0.0034 - 0.065
4-nitro-1,6-dihydrobenzo[1,2-d:3,4-d']bis[1,2,3]triazole
0.0055 - 0.1
4-nitro-7-[[(1-phenyl-1H-tetrazol-5-yl)sulfanyl]methyl]-2,1,3-benzothiadiazole
0.0026 - 0.0112
4-[(1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl)sulfanyl]butanoic acid
0.0033 - 0.0083
5,6-dichloro-2,1,3-benzothiadiazole-4,7-diol
0.0069 - 0.0104
5-[(E)-benzylideneamino]-6-[(2-hydroxyethyl)amino]pyrimidine-2,4(1H,3H)-dione
0.0059 - 0.0129
5-[(E)-[[1-(2-chlorobenzyl)-1H-indol-3-yl]methylidene]amino]-1,3-dihydro-2H-benzimidazol-2-one
0.0122 - 0.0593
5-[[5-hydroxy-3-methyl-1-(4-methylphenyl)-1H-pyrazol-4-yl]methylidene]-1,3-diphenyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
0.0021 - 0.0057
6,11-dioxo-5a,6,11,11a-tetrahydronaphtho[2',3':4,5][1,3]thiazolo[3,2-a]pyridin-12-ium
0.0045 - 0.1
9H-indeno[1,2-b][1,2,5]oxadiazolo[3,4-e]pyrazin-9-one
0.0049 - 0.0063
biphenyl-3,3'-dicarbaldehyde
0.0004 - 0.001
carboxymethoxylamine
0.001 - 4
methyl 2-amino-3-oxo-3H-phenothiazine-1-carboxylate
0.005 - 0.0125
methyl 2-[[(2-methylimidazo[1,2-a]pyridin-3-yl)carbonyl]amino]benzoate
0.0076 - 0.0164
N-(2-hydroxy-1,3-dioxo-2,3-dihydro-1H-inden-2-yl)benzamide
0.001 - 0.0022
N-[4,7-dioxo-6-(phenylamino)-4,7-dihydro-2,1,3-benzoxadiazol-5-yl]acetamide
0.0013 - 0.0044
N-[4,7-dioxo-6-(piperidin-1-yl)-4,7-dihydro-2,1,3-benzoxadiazol-5-yl]acetamide
0.0037 - 0.0591
naphtho[2',3':4,5]imidazo[1,2-a]pyridine-6,11-dione
0.0244 - 0.1
[(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)oxy]acetic acid
0.0123
(4Z,7E)-N,N'-dihydroxy-2,2-dimethyl-5,6-dihydro-2H-benzimidazole-4,7-diimine
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0135
(4Z,7E)-N,N'-dihydroxy-2,2-dimethyl-5,6-dihydro-2H-benzimidazole-4,7-diimine
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.0266
(4Z,7E)-N,N'-dihydroxy-2,2-dimethyl-5,6-dihydro-2H-benzimidazole-4,7-diimine
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0274
(4Z,7E)-N,N'-dihydroxy-2,2-dimethyl-5,6-dihydro-2H-benzimidazole-4,7-diimine
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.03
(4Z,7E)-N,N'-dihydroxy-2,2-dimethyl-5,6-dihydro-2H-benzimidazole-4,7-diimine
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.0033
(5Z)-2-amino-5-(2-nitrobenzylidene)-1,3-thiazol-4(5H)-one
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.0033
(5Z)-2-amino-5-(2-nitrobenzylidene)-1,3-thiazol-4(5H)-one
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0037
(5Z)-2-amino-5-(2-nitrobenzylidene)-1,3-thiazol-4(5H)-one
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0057
(5Z)-2-amino-5-(2-nitrobenzylidene)-1,3-thiazol-4(5H)-one
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.0418
(5Z)-2-amino-5-(2-nitrobenzylidene)-1,3-thiazol-4(5H)-one
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0038
1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl 2,3,4-tri-O-acetylpentopyranoside
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.004
1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl 2,3,4-tri-O-acetylpentopyranoside
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.004
1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl 2,3,4-tri-O-acetylpentopyranoside
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0053
1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl 2,3,4-tri-O-acetylpentopyranoside
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.012
1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl 2,3,4-tri-O-acetylpentopyranoside
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0055
1-(2-nitrobenzyl)-1H-indole-3-carbaldehyde
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0069
1-(2-nitrobenzyl)-1H-indole-3-carbaldehyde
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0076
1-(2-nitrobenzyl)-1H-indole-3-carbaldehyde
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.008
1-(2-nitrobenzyl)-1H-indole-3-carbaldehyde
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.0142
1-(2-nitrobenzyl)-1H-indole-3-carbaldehyde
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.002
10H-indeno[2,1-e]tetrazolo[1,5-b][1,2,4]triazin-10-one
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.002
10H-indeno[2,1-e]tetrazolo[1,5-b][1,2,4]triazin-10-one
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.002
10H-indeno[2,1-e]tetrazolo[1,5-b][1,2,4]triazin-10-one
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.002 - 4
10H-indeno[2,1-e]tetrazolo[1,5-b][1,2,4]triazin-10-one
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0047
10H-indeno[2,1-e]tetrazolo[1,5-b][1,2,4]triazin-10-one
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0051
2,4-bis[2-(4-hydroxyphenyl)propan-2-yl]phenol
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.0777
2,4-bis[2-(4-hydroxyphenyl)propan-2-yl]phenol
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.1
2,4-bis[2-(4-hydroxyphenyl)propan-2-yl]phenol
Mus musculus
above, pH 8.0, 37°C, recombinant enzyme
0.1
2,4-bis[2-(4-hydroxyphenyl)propan-2-yl]phenol
Ctenocephalides felis
above, pH 8.0, 37°C, recombinant enzyme
0.1
2,4-bis[2-(4-hydroxyphenyl)propan-2-yl]phenol
Drosophila melanogaster
above, pH 8.0, 37°C, recombinant enzyme
0.0073
2-(benzylsulfanyl)-3-(morpholin-4-yl)-2,3-dihydronaphthalene-1,4-dione
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0089
2-(benzylsulfanyl)-3-(morpholin-4-yl)-2,3-dihydronaphthalene-1,4-dione
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.0112
2-(benzylsulfanyl)-3-(morpholin-4-yl)-2,3-dihydronaphthalene-1,4-dione
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.0115
2-(benzylsulfanyl)-3-(morpholin-4-yl)-2,3-dihydronaphthalene-1,4-dione
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0209
2-(benzylsulfanyl)-3-(morpholin-4-yl)-2,3-dihydronaphthalene-1,4-dione
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0052
2-chloro-N-[5-([2-oxo-2-[(4-sulfamoylphenyl)amino]ethyl]sulfanyl)-1,3,4-thiadiazol-2-yl]acetamide
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0087
2-chloro-N-[5-([2-oxo-2-[(4-sulfamoylphenyl)amino]ethyl]sulfanyl)-1,3,4-thiadiazol-2-yl]acetamide
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0162
2-chloro-N-[5-([2-oxo-2-[(4-sulfamoylphenyl)amino]ethyl]sulfanyl)-1,3,4-thiadiazol-2-yl]acetamide
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0284
2-chloro-N-[5-([2-oxo-2-[(4-sulfamoylphenyl)amino]ethyl]sulfanyl)-1,3,4-thiadiazol-2-yl]acetamide
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.1
2-chloro-N-[5-([2-oxo-2-[(4-sulfamoylphenyl)amino]ethyl]sulfanyl)-1,3,4-thiadiazol-2-yl]acetamide
Rhipicephalus microplus
above, pH 8.0, 37°C, recombinant enzyme
0.0042
2-hydroxy-2-(2-hydroxy-6-oxocyclohex-2-en-1-yl)-1H-indene-1,3(2H)-dione
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0047
2-hydroxy-2-(2-hydroxy-6-oxocyclohex-2-en-1-yl)-1H-indene-1,3(2H)-dione
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.0062
2-hydroxy-2-(2-hydroxy-6-oxocyclohex-2-en-1-yl)-1H-indene-1,3(2H)-dione
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0069
2-hydroxy-2-(2-hydroxy-6-oxocyclohex-2-en-1-yl)-1H-indene-1,3(2H)-dione
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.0108
2-hydroxy-2-(2-hydroxy-6-oxocyclohex-2-en-1-yl)-1H-indene-1,3(2H)-dione
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0075
2-thioxo-3-[(E)-(3,3,5-trimethylcyclohexylidene)amino]-1,3-thiazolidin-4-one
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.01
2-thioxo-3-[(E)-(3,3,5-trimethylcyclohexylidene)amino]-1,3-thiazolidin-4-one
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0127
2-thioxo-3-[(E)-(3,3,5-trimethylcyclohexylidene)amino]-1,3-thiazolidin-4-one
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0139
2-thioxo-3-[(E)-(3,3,5-trimethylcyclohexylidene)amino]-1,3-thiazolidin-4-one
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.014
2-thioxo-3-[(E)-(3,3,5-trimethylcyclohexylidene)amino]-1,3-thiazolidin-4-one
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.0165
2-[(2-chloro-5-nitrobenzoyl)amino]-5-iodobenzoic acid
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0714
2-[(2-chloro-5-nitrobenzoyl)amino]-5-iodobenzoic acid
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.0845
2-[(2-chloro-5-nitrobenzoyl)amino]-5-iodobenzoic acid
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.1
2-[(2-chloro-5-nitrobenzoyl)amino]-5-iodobenzoic acid
Mus musculus
above, pH 8.0, 37°C, recombinant enzyme
0.1
2-[(2-chloro-5-nitrobenzoyl)amino]-5-iodobenzoic acid
Rhipicephalus microplus
above, pH 8.0, 37°C, recombinant enzyme
0.0082
2-[(3-formyl-1H-indol-1-yl)methyl]benzonitrile
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0089
2-[(3-formyl-1H-indol-1-yl)methyl]benzonitrile
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0126
2-[(3-formyl-1H-indol-1-yl)methyl]benzonitrile
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0138
2-[(3-formyl-1H-indol-1-yl)methyl]benzonitrile
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.014
2-[(3-formyl-1H-indol-1-yl)methyl]benzonitrile
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.0002
3,3'-(4H-1,2,4-triazole-3,5-diyl)bis(4-nitro-1,2,5-oxadiazole)
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0004
3,3'-(4H-1,2,4-triazole-3,5-diyl)bis(4-nitro-1,2,5-oxadiazole)
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0148
3,3'-(4H-1,2,4-triazole-3,5-diyl)bis(4-nitro-1,2,5-oxadiazole)
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.0196
3,3'-(4H-1,2,4-triazole-3,5-diyl)bis(4-nitro-1,2,5-oxadiazole)
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0212
3,3'-(4H-1,2,4-triazole-3,5-diyl)bis(4-nitro-1,2,5-oxadiazole)
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.0123
3-Mercaptopropionic acid
Homo sapiens
-
-
0.0123
3-Mercaptopropionic acid
Homo sapiens
-
at 37°C
0.0123
3-Mercaptopropionic acid
Homo sapiens
-
at 37°C, pH not specified in the publication
0.0123
3-Mercaptopropionic acid
Homo sapiens
recombinant MBP-tagged enzyme, pH 8.0, 37°C
0.0202
3-[(2E)-2-[1-(3,4-dimethoxyphenyl)ethylidene]hydrazinyl]benzoic acid
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.1
3-[(2E)-2-[1-(3,4-dimethoxyphenyl)ethylidene]hydrazinyl]benzoic acid
Mus musculus
above, pH 8.0, 37°C, recombinant enzyme
0.1
3-[(2E)-2-[1-(3,4-dimethoxyphenyl)ethylidene]hydrazinyl]benzoic acid
Ctenocephalides felis
above, pH 8.0, 37°C, recombinant enzyme
0.1
3-[(2E)-2-[1-(3,4-dimethoxyphenyl)ethylidene]hydrazinyl]benzoic acid
Drosophila melanogaster
above, pH 8.0, 37°C, recombinant enzyme
0.0063
3-[(E)-(2,6-difluorobenzylidene)amino]-2-thioxo-1,3-thiazolidin-4-one
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.0064
3-[(E)-(2,6-difluorobenzylidene)amino]-2-thioxo-1,3-thiazolidin-4-one
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0079
3-[(E)-(2,6-difluorobenzylidene)amino]-2-thioxo-1,3-thiazolidin-4-one
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0109
3-[(E)-(2,6-difluorobenzylidene)amino]-2-thioxo-1,3-thiazolidin-4-one
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.0122
3-[(E)-(2,6-difluorobenzylidene)amino]-2-thioxo-1,3-thiazolidin-4-one
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0072
4,4'-(phenylmethanediyl)bis[2-(4-chlorophenyl)-5-methyl-2,4-dihydro-3H-pyrazol-3-one]
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.012
4,4'-(phenylmethanediyl)bis[2-(4-chlorophenyl)-5-methyl-2,4-dihydro-3H-pyrazol-3-one]
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0218
4,4'-(phenylmethanediyl)bis[2-(4-chlorophenyl)-5-methyl-2,4-dihydro-3H-pyrazol-3-one]
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0269
4,4'-(phenylmethanediyl)bis[2-(4-chlorophenyl)-5-methyl-2,4-dihydro-3H-pyrazol-3-one]
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.099
4,4'-(phenylmethanediyl)bis[2-(4-chlorophenyl)-5-methyl-2,4-dihydro-3H-pyrazol-3-one]
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.013
4,4'-[(4-hydroxyphenyl)methanediyl]bis(2-heptyl-5-methyl-2,4-dihydro-3H-pyrazol-3-one)
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0138
4,4'-[(4-hydroxyphenyl)methanediyl]bis(2-heptyl-5-methyl-2,4-dihydro-3H-pyrazol-3-one)
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0173
4,4'-[(4-hydroxyphenyl)methanediyl]bis(2-heptyl-5-methyl-2,4-dihydro-3H-pyrazol-3-one)
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0188
4,4'-[(4-hydroxyphenyl)methanediyl]bis(2-heptyl-5-methyl-2,4-dihydro-3H-pyrazol-3-one)
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.0226
4,4'-[(4-hydroxyphenyl)methanediyl]bis(2-heptyl-5-methyl-2,4-dihydro-3H-pyrazol-3-one)
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.0029
4-(morpholin-4-yl)naphthalene-1,2-dione
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.003
4-(morpholin-4-yl)naphthalene-1,2-dione
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.0034
4-(morpholin-4-yl)naphthalene-1,2-dione
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0039
4-(morpholin-4-yl)naphthalene-1,2-dione
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.0045
4-(morpholin-4-yl)naphthalene-1,2-dione
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.003
4-(piperidin-1-yl)naphthalene-1,2-dione
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.003
4-(piperidin-1-yl)naphthalene-1,2-dione
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0038
4-(piperidin-1-yl)naphthalene-1,2-dione
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0047
4-(piperidin-1-yl)naphthalene-1,2-dione
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0053
4-(piperidin-1-yl)naphthalene-1,2-dione
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.0034
4-nitro-1,6-dihydrobenzo[1,2-d:3,4-d']bis[1,2,3]triazole
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.0077
4-nitro-1,6-dihydrobenzo[1,2-d:3,4-d']bis[1,2,3]triazole
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0209
4-nitro-1,6-dihydrobenzo[1,2-d:3,4-d']bis[1,2,3]triazole
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.0211
4-nitro-1,6-dihydrobenzo[1,2-d:3,4-d']bis[1,2,3]triazole
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.065
4-nitro-1,6-dihydrobenzo[1,2-d:3,4-d']bis[1,2,3]triazole
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0055
4-nitro-7-[[(1-phenyl-1H-tetrazol-5-yl)sulfanyl]methyl]-2,1,3-benzothiadiazole
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.0912
4-nitro-7-[[(1-phenyl-1H-tetrazol-5-yl)sulfanyl]methyl]-2,1,3-benzothiadiazole
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0981
4-nitro-7-[[(1-phenyl-1H-tetrazol-5-yl)sulfanyl]methyl]-2,1,3-benzothiadiazole
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.1
4-nitro-7-[[(1-phenyl-1H-tetrazol-5-yl)sulfanyl]methyl]-2,1,3-benzothiadiazole
Mus musculus
above, pH 8.0, 37°C, recombinant enzyme
0.0026
4-[(1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl)sulfanyl]butanoic acid
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.0064
4-[(1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl)sulfanyl]butanoic acid
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0067
4-[(1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl)sulfanyl]butanoic acid
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.0069
4-[(1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl)sulfanyl]butanoic acid
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0112
4-[(1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl)sulfanyl]butanoic acid
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0033
5,6-dichloro-2,1,3-benzothiadiazole-4,7-diol
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0037
5,6-dichloro-2,1,3-benzothiadiazole-4,7-diol
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.0053
5,6-dichloro-2,1,3-benzothiadiazole-4,7-diol
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.0057
5,6-dichloro-2,1,3-benzothiadiazole-4,7-diol
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0083
5,6-dichloro-2,1,3-benzothiadiazole-4,7-diol
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0069
5-[(E)-benzylideneamino]-6-[(2-hydroxyethyl)amino]pyrimidine-2,4(1H,3H)-dione
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0077
5-[(E)-benzylideneamino]-6-[(2-hydroxyethyl)amino]pyrimidine-2,4(1H,3H)-dione
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.0087
5-[(E)-benzylideneamino]-6-[(2-hydroxyethyl)amino]pyrimidine-2,4(1H,3H)-dione
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0104
5-[(E)-benzylideneamino]-6-[(2-hydroxyethyl)amino]pyrimidine-2,4(1H,3H)-dione
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0104
5-[(E)-benzylideneamino]-6-[(2-hydroxyethyl)amino]pyrimidine-2,4(1H,3H)-dione
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.0059
5-[(E)-[[1-(2-chlorobenzyl)-1H-indol-3-yl]methylidene]amino]-1,3-dihydro-2H-benzimidazol-2-one
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0063
5-[(E)-[[1-(2-chlorobenzyl)-1H-indol-3-yl]methylidene]amino]-1,3-dihydro-2H-benzimidazol-2-one
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.0065
5-[(E)-[[1-(2-chlorobenzyl)-1H-indol-3-yl]methylidene]amino]-1,3-dihydro-2H-benzimidazol-2-one
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0066
5-[(E)-[[1-(2-chlorobenzyl)-1H-indol-3-yl]methylidene]amino]-1,3-dihydro-2H-benzimidazol-2-one
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.0129
5-[(E)-[[1-(2-chlorobenzyl)-1H-indol-3-yl]methylidene]amino]-1,3-dihydro-2H-benzimidazol-2-one
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0122
5-[[5-hydroxy-3-methyl-1-(4-methylphenyl)-1H-pyrazol-4-yl]methylidene]-1,3-diphenyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.0144
5-[[5-hydroxy-3-methyl-1-(4-methylphenyl)-1H-pyrazol-4-yl]methylidene]-1,3-diphenyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0149
5-[[5-hydroxy-3-methyl-1-(4-methylphenyl)-1H-pyrazol-4-yl]methylidene]-1,3-diphenyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.0558
5-[[5-hydroxy-3-methyl-1-(4-methylphenyl)-1H-pyrazol-4-yl]methylidene]-1,3-diphenyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0593
5-[[5-hydroxy-3-methyl-1-(4-methylphenyl)-1H-pyrazol-4-yl]methylidene]-1,3-diphenyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0021
6,11-dioxo-5a,6,11,11a-tetrahydronaphtho[2',3':4,5][1,3]thiazolo[3,2-a]pyridin-12-ium
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.0022
6,11-dioxo-5a,6,11,11a-tetrahydronaphtho[2',3':4,5][1,3]thiazolo[3,2-a]pyridin-12-ium
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.0023
6,11-dioxo-5a,6,11,11a-tetrahydronaphtho[2',3':4,5][1,3]thiazolo[3,2-a]pyridin-12-ium
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0029
6,11-dioxo-5a,6,11,11a-tetrahydronaphtho[2',3':4,5][1,3]thiazolo[3,2-a]pyridin-12-ium
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0057
6,11-dioxo-5a,6,11,11a-tetrahydronaphtho[2',3':4,5][1,3]thiazolo[3,2-a]pyridin-12-ium
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0045
9H-indeno[1,2-b][1,2,5]oxadiazolo[3,4-e]pyrazin-9-one
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.0056
9H-indeno[1,2-b][1,2,5]oxadiazolo[3,4-e]pyrazin-9-one
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0089
9H-indeno[1,2-b][1,2,5]oxadiazolo[3,4-e]pyrazin-9-one
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.0143
9H-indeno[1,2-b][1,2,5]oxadiazolo[3,4-e]pyrazin-9-one
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.1
9H-indeno[1,2-b][1,2,5]oxadiazolo[3,4-e]pyrazin-9-one
Mus musculus
above, pH 8.0, 37°C, recombinant enzyme
0.0049
biphenyl-3,3'-dicarbaldehyde
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0053
biphenyl-3,3'-dicarbaldehyde
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.0062
biphenyl-3,3'-dicarbaldehyde
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0063
biphenyl-3,3'-dicarbaldehyde
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.0004
carboxymethoxylamine
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.0005
carboxymethoxylamine
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.001
carboxymethoxylamine
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.001
carboxymethoxylamine
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.001
methyl 2-amino-3-oxo-3H-phenothiazine-1-carboxylate
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0014
methyl 2-amino-3-oxo-3H-phenothiazine-1-carboxylate
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.0015
methyl 2-amino-3-oxo-3H-phenothiazine-1-carboxylate
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0017
methyl 2-amino-3-oxo-3H-phenothiazine-1-carboxylate
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.002 - 4
methyl 2-amino-3-oxo-3H-phenothiazine-1-carboxylate
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.005
methyl 2-[[(2-methylimidazo[1,2-a]pyridin-3-yl)carbonyl]amino]benzoate
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.006
methyl 2-[[(2-methylimidazo[1,2-a]pyridin-3-yl)carbonyl]amino]benzoate
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.0062
methyl 2-[[(2-methylimidazo[1,2-a]pyridin-3-yl)carbonyl]amino]benzoate
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0065
methyl 2-[[(2-methylimidazo[1,2-a]pyridin-3-yl)carbonyl]amino]benzoate
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0125
methyl 2-[[(2-methylimidazo[1,2-a]pyridin-3-yl)carbonyl]amino]benzoate
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0076
N-(2-hydroxy-1,3-dioxo-2,3-dihydro-1H-inden-2-yl)benzamide
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0082
N-(2-hydroxy-1,3-dioxo-2,3-dihydro-1H-inden-2-yl)benzamide
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.0091
N-(2-hydroxy-1,3-dioxo-2,3-dihydro-1H-inden-2-yl)benzamide
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0105
N-(2-hydroxy-1,3-dioxo-2,3-dihydro-1H-inden-2-yl)benzamide
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.0164
N-(2-hydroxy-1,3-dioxo-2,3-dihydro-1H-inden-2-yl)benzamide
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.001
N-[4,7-dioxo-6-(phenylamino)-4,7-dihydro-2,1,3-benzoxadiazol-5-yl]acetamide
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.0011
N-[4,7-dioxo-6-(phenylamino)-4,7-dihydro-2,1,3-benzoxadiazol-5-yl]acetamide
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0011
N-[4,7-dioxo-6-(phenylamino)-4,7-dihydro-2,1,3-benzoxadiazol-5-yl]acetamide
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.0012
N-[4,7-dioxo-6-(phenylamino)-4,7-dihydro-2,1,3-benzoxadiazol-5-yl]acetamide
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0022
N-[4,7-dioxo-6-(phenylamino)-4,7-dihydro-2,1,3-benzoxadiazol-5-yl]acetamide
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0013
N-[4,7-dioxo-6-(piperidin-1-yl)-4,7-dihydro-2,1,3-benzoxadiazol-5-yl]acetamide
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.0018
N-[4,7-dioxo-6-(piperidin-1-yl)-4,7-dihydro-2,1,3-benzoxadiazol-5-yl]acetamide
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0022
N-[4,7-dioxo-6-(piperidin-1-yl)-4,7-dihydro-2,1,3-benzoxadiazol-5-yl]acetamide
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0023
N-[4,7-dioxo-6-(piperidin-1-yl)-4,7-dihydro-2,1,3-benzoxadiazol-5-yl]acetamide
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.0044
N-[4,7-dioxo-6-(piperidin-1-yl)-4,7-dihydro-2,1,3-benzoxadiazol-5-yl]acetamide
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0037
naphtho[2',3':4,5]imidazo[1,2-a]pyridine-6,11-dione
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.0039
naphtho[2',3':4,5]imidazo[1,2-a]pyridine-6,11-dione
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0041
naphtho[2',3':4,5]imidazo[1,2-a]pyridine-6,11-dione
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0073
naphtho[2',3':4,5]imidazo[1,2-a]pyridine-6,11-dione
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.0591
naphtho[2',3':4,5]imidazo[1,2-a]pyridine-6,11-dione
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0244
[(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)oxy]acetic acid
Drosophila melanogaster
pH 8.0, 37°C, recombinant enzyme
0.0257
[(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)oxy]acetic acid
Ctenocephalides felis
pH 8.0, 37°C, recombinant enzyme
0.0284
[(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)oxy]acetic acid
Rhipicephalus microplus
pH 8.0, 37°C, recombinant enzyme
0.1
[(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)oxy]acetic acid
Mus musculus
above, pH 8.0, 37°C, recombinant enzyme
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evolution
-
clustal X-generated dendrogram of bacterial glutamate decarboxylases, overview
evolution
-
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
-
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
-
clustal X-generated dendrogram of bacterial glutamate decarboxylases, overview
-
evolution
-
different morphological, biochemical and chemotaxonomic characteristics of the strains AM and strain B8W22
-
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
-
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
-
clustal X-generated dendrogram of bacterial glutamate decarboxylases, overview
-
evolution
-
the amino acid sequences of GADLbHYE1 shows 48% homology with the GadA family and 99% identity with the GadB family from Lactobacillus brevis
-
malfunction
-
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
-
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
-
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
-
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
-
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
-
the DELTAgadD1 mutant is impaired in its ability to tolerate exposure to both sublethal and lethal levels of the lantibiotic nisin
-
metabolism
-
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
-
glutamate decarboxylase is a key enzyme that catalyzes the irreversible alpha-decarboxylation of L-glutamate to 4-aminobutanoate, GABA
-
physiological function
-
GAD65-mediated 4-aminobutanoate synthesis plays relatively small but significant roles in nociceptive processing via supraspinal mechanisms
physiological function
-
the GAD acid resistance system does not play any role in the survival of Listeria monocytogenes at a low pH
physiological function
-
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
-
GAD1 plays an important role in responses to abiotic factors and hormone treatments
physiological function
-
possession of the gadD1 gene correlates with a higher degree of tolerance to nisin
physiological function
-
possession of the gadD1 gene correlates with a higher degree of tolerance to nisin
physiological function
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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 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
-
glutamate decarboxylase (GAD) catalyzes the irreversible decarboxylation of L-glutamate to the valuable food supplement gamma-aminobutyric acid (GABA)
-
physiological function
-
possession of the gadD1 gene correlates with a higher degree of tolerance to nisin
-
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
-
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
-
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
-
possession of the gadD1 gene correlates with a higher degree of tolerance to nisin
-
physiological function
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
three-dimensional enzyme structure analysis, homology modeling using the crystal structure of homohexameric GadB at low pH, PDB ID 1pmm
additional information
-
absence of a His residue near the C-terminus in Lactobacillus brevis GadB homologue LVIS_0079
-
additional information
-
structure molecular modeling
-
additional information
-
enzyme three-dimensional structure modelling, overview
-
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
-
the GAD C-terminal region (Ile454-Thr468) plays an important role in the pH dependence of catalysis. Homology modeling of GAD
-
additional information
-
residues T215 and D246 are involved in catalysis
-
additional information
-
important role of C-terminal region in the pH-dependent regulation of enzyme activity. Enzyme molecular homology modeling
-
additional information
-
binding of pyridoxal 5'-phosphate as well as to the active site residues Thr215 and Asp246 that promote decarboxylation
-
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homooctamer
-
native PAGE
homotetramer
-
native PAGE
oligomer
-
x * 58000, SDS-PAGE of full-length enzyme
?
-
x * 58000, isoenzyme GAD1, SDS-PAGE
?
-
x * 56000, isoenzyme GAD2, SDS-PAGE
?
x * 53755, sequence calculation, x * 53000, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 53755, sequence calculation, x * 53000, recombinant His-tagged enzyme, SDS-PAGE
-
?
-
x * 52500, SDS-PAGE, x * 52000, calculated
?
-
x * 58000, recombinant His6-tagged fusion enzyme, SDS-PAGE
?
x * 53000, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 53000, SDS-PAGE
-
?
-
x * 53000, recombinant His-tagged enzyme, SDS-PAGE
-
?
x * 53540, sequence calculation, x * 54400, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 53540, sequence calculation, x * 54400, recombinant His-tagged enzyme, SDS-PAGE
-
?
x * 53000, recombinant enzyme, SDS-PAGE
?
x * 54000, recombinant His-tagged enzyme, SDS-PAGE
?
x * 53522, sequence calculation, x * 50000, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 53522, sequence calculation, x * 50000, recombinant His-tagged enzyme, SDS-PAGE
-
?
-
x * 53000, recombinant enzyme, SDS-PAGE
-
?
-
x * 54000, recombinant His-tagged enzyme, SDS-PAGE
-
?
x * 56000-58000, SDS-PAGE
?
x * 57200, calculated from amino acid sequence
?
-
x * 53000, SDS-PAGE
-
?
x * 53000-55000, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 53000-55000, recombinant His-tagged enzyme, SDS-PAGE
-
?
-
x * 40000, SDS-PAGE in presence of 4 M urea and 2-mercaptoethanol
?
-
x * 40000 + x * 80000, SDS-PAGE
?
-
x * 66000, recombinant His-tagged enzyme, SDS-PAGE, x * 65986, sequence calculation
?
-
x * 66000, recombinant His-tagged enzyme, SDS-PAGE, x * 65986, sequence calculation
-
?
x * 57740, sequence calculation, x * 58000, SDS-PAGE
?
-
x * 56200, calculated from amino acid sequence
?
-
x * 61000, His-tagged enzyme, SDS-PAGE
dimer
-
crystallization data
dimer
-
2 * 59000, SDS-PAGE
dimer
-
2 * 67000, SDS-PAGE
dimer
2 * 57000, SDS-PAGE
dimer
-
2 * 57000, SDS-PAGE
-
dimer
2 * 54000, inactive, recombinant His-tagged enzyme, SDS-PAGE
dimer
2 * 54500, recombinant enzyme, SDS-PAGE
dimer
-
2 * 54500, recombinant enzyme, SDS-PAGE
-
dimer
-
2 * 54000, inactive, recombinant His-tagged enzyme, SDS-PAGE
-
dimer
-
2 * 74000, SDS-PAGE
dimer
-
2 * 44000, high speed equilibrium sedimentation after treatment with 6 M guanidine HCl and 0.1 M beta-mercaptoethanol
dimer
-
2 * 40000, SDS-PAGE
dimer
-
dimer-forming interactions are mediated mainly by carboxyl-terminal domain
dimer
-
2 * 43000, SDS-PAGE
dimer
2 * 46900, SDS-PAGE
dimer
-
2 * 60000, SDS-PAGE
hexamer
-
6 * 48000, SDS-PAGE
hexamer
-
6 * 58000, SDS-PAGE, gel filtration in presence of SDS
hexamer
-
GadB is a trimer of dimers, in which monomers from each dimer belong to different layers, structure comparisons, overview
hexamer
6 * 54000, recombinant enzyme, SDS-PAGE
hexamer
-
6 * 54000, recombinant enzyme, SDS-PAGE
-
homodimer
-
gel filtration
homodimer
the basic structural unit of AtGAD1 is a homodimer
homodimer
-
2 * 55000, SDS-PAGE
homodimer
-
2 * 55000, SDS-PAGE
-
homodimer
2 * 53000, recombinant His-tagged enzyme, SDS-PAGE
homodimer
-
2 * 53000, recombinant His-tagged enzyme, SDS-PAGE
-
homodimer
2 * 46850, SDS-PAGE
homodimer
-
2 * 46850, SDS-PAGE
-
homohexamer
X-ray crystallography, 6 * 57066, amino acid sequence
homohexamer
hexamer composed of a trimer of dimers. Hexamerization strongly contributes to the stability of the enzyme
homohexamer
6 x 52000, recombinant enzyme, SDS-PAGE
homohexamer
-
6 x 52000, recombinant enzyme, SDS-PAGE
-
homohexamer
a trimer of dimers
monomer
-
1 * 57000, about, sequence calculation
monomer
-
1 * 57000, about, sequence calculation
-
monomer
-
1 * 33200, SDS-PAGE
monomer
1 * 410000, SDS-PAGE
monomer
-
1 * 42000, SDS-PAGE
monomer
1 * 53000, recombinant enzyme, SDS-PAGE
tetramer
4 * 54000, ammonium sulfate-activated, recombinant His-tagged enzyme, SDS-PAGE
tetramer
Lactobacillus brevis IFO12005 is dimeric in the inactive form and tetrameric in the active form
tetramer
-
Lactobacillus brevis IFO12005 is dimeric in the inactive form and tetrameric in the active form
-
tetramer
-
4 * 54000, ammonium sulfate-activated, recombinant His-tagged enzyme, SDS-PAGE
-
additional information
in solution AtGAD1 is in a dimer-hexamer equilibrium. Binding of Ca2+/CaM1 abolishes the dissociation of the AtGAD1 oligomer. The AtGAD1N-terminal domain is critical for maintaining the oligomeric state. Arg24 in the N-terminal domain is a key residue. The oligomeric state of AtGAD1 is highly responsive to a number of experimental parameters and may have functional relevance in vivo in the light of the biphasic regulation of AtGAD1 activity by pH and Ca2+/CaM1 in plant cells. Tryptic peptide mapping. Effect of pH on the dissociation of hexameric AtGAD1 in the pH range 6.0-8.0, overview. A flexible and exposed stretch spanning residues 1-24 is the minimum region required for assembly of hexamer
additional information
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in solution AtGAD1 is in a dimer-hexamer equilibrium. Binding of Ca2+/CaM1 abolishes the dissociation of the AtGAD1 oligomer. The AtGAD1N-terminal domain is critical for maintaining the oligomeric state. Arg24 in the N-terminal domain is a key residue. The oligomeric state of AtGAD1 is highly responsive to a number of experimental parameters and may have functional relevance in vivo in the light of the biphasic regulation of AtGAD1 activity by pH and Ca2+/CaM1 in plant cells. Tryptic peptide mapping. Effect of pH on the dissociation of hexameric AtGAD1 in the pH range 6.0-8.0, overview. A flexible and exposed stretch spanning residues 1-24 is the minimum region required for assembly of hexamer
additional information
at acidic pH, when the enzyme is maximally active, BmGadB is a hexamer
additional information
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at acidic pH, when the enzyme is maximally active, BmGadB is a hexamer
additional information
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at acidic pH, when the enzyme is maximally active, BmGadB is a hexamer
-
additional information
homohexameric GadB forms a triple-helix bundle interdomain at acidic pH
additional information
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homohexameric GadB forms a triple-helix bundle interdomain at acidic pH
additional information
addition of pyridoxine does not influence the aggregation state of GAD
additional information
Escherichia coli GAD forms a hexamer at acidic pH which consists of three functional dimers. In each dimer there are some special residues from both subunits that contribute in the formation of potential active sites and promote the interaction between the enzyme, cofactor and substrate. The N- and C-terminal domains of each subunit play an important role in conformational changes through pH shift. These conformational changes lead to activation of the enzyme at acidic pH and vice versa. The N-terminal residues involve in dimerization and subsequent migration of GAD to cytoplasmic site of the inner. The C-terminal domain by entrancing into the active site is also responsible for autoinhibition of the enzyme at neutral pH
additional information
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Escherichia coli GAD forms a hexamer at acidic pH which consists of three functional dimers. In each dimer there are some special residues from both subunits that contribute in the formation of potential active sites and promote the interaction between the enzyme, cofactor and substrate. The N- and C-terminal domains of each subunit play an important role in conformational changes through pH shift. These conformational changes lead to activation of the enzyme at acidic pH and vice versa. The N-terminal residues involve in dimerization and subsequent migration of GAD to cytoplasmic site of the inner. The C-terminal domain by entrancing into the active site is also responsible for autoinhibition of the enzyme at neutral pH
additional information
in GadB, the dimer is the functional unit as each active site is made of amino acid residues that are provided by both monomers in the dimer. Structural organization of EcGadB in solution in the pH range 7.5-8.6, overview. Analysis by small angle X-ray scattering combined with size exclusion chromatography and analytical ultracentrifugation analysis shows that the compact and entangled EcGadB hexameric structure undergoes dissociation into dimers as pH alkalinizes. When pyridoxal 5'-phosphate is not present, the dimeric species is the most abundant in solution, though evidence for the occurrence of a likely tetrameric species is also obtained. Molecular modeling
additional information
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in GadB, the dimer is the functional unit as each active site is made of amino acid residues that are provided by both monomers in the dimer. Structural organization of EcGadB in solution in the pH range 7.5-8.6, overview. Analysis by small angle X-ray scattering combined with size exclusion chromatography and analytical ultracentrifugation analysis shows that the compact and entangled EcGadB hexameric structure undergoes dissociation into dimers as pH alkalinizes. When pyridoxal 5'-phosphate is not present, the dimeric species is the most abundant in solution, though evidence for the occurrence of a likely tetrameric species is also obtained. Molecular modeling
additional information
three-dimensional enzyme structure analysis
additional information
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three-dimensional enzyme structure analysis
additional information
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addition of pyridoxine does not influence the aggregation state of GAD
-
additional information
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both isoform GAD65 and GAD67 in vivo build up a protein complex with apocalmodulin
additional information
25 and 44 kDa GAD through differential GAD67 RNA splicing, the 25 kDa is enzymatically inactive and is present usually early in the development, the 44 kDa GAD is enzymatically active
additional information
25 and 44 kDa GAD through differential GAD67 RNA splicing, the 25 kDa is enzymatically inactive and is present usually early in the development, the 44 kDa GAD is enzymatically active
additional information
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mapping of T cell epitopes on GAD65, overview
additional information
sodium glutamate is essential for tetramer formation and its activation
additional information
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sodium glutamate is essential for tetramer formation and its activation
additional information
asymmetrical flow field-flow fractionation (AF4) provides molecular weight (MW) (or size)-based separation of dimer, hexamer, and aggregates of LbGadB, molecular modeling
additional information
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asymmetrical flow field-flow fractionation (AF4) provides molecular weight (MW) (or size)-based separation of dimer, hexamer, and aggregates of LbGadB, molecular modeling
additional information
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asymmetrical flow field-flow fractionation (AF4) provides molecular weight (MW) (or size)-based separation of dimer, hexamer, and aggregates of LbGadB, molecular modeling
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additional information
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sodium glutamate is essential for tetramer formation and its activation
-
additional information
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25 and 44 kDa GAD through differential GAD67 RNA splicing, the 25 kDa is enzymatically inactive and is present usually early in the development, the 44 kDa GAD is enzymatically active
additional information
the C-terminal extension of enzyme plays a role as a strong autoinhibitory domain. Truncation causes the enzyme to act constitutively, with higher activity than wild-type both in vitro and in vivo
additional information
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the C-terminal extension of enzyme plays a role as a strong autoinhibitory domain. Truncation causes the enzyme to act constitutively, with higher activity than wild-type both in vitro and in vivo
additional information
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N-terminal segments of both GAD65 and GAD67 are exposed and flexible
additional information
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25 and 44 kDa GAD through differential GAD67 RNA splicing, the 25 kDa is enzymatically inactive and is present usually early in the development, the 44 kDa GAD is enzymatically active
additional information
the N-terminal amino acid sequence of GAD is NH2-MNEKLFREI
additional information
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the N-terminal amino acid sequence of GAD is NH2-MNEKLFREI
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K496A/K497A
the mutant displays a substantial loss of enzymatic activity, at the pH optimum, the activity of the double mutant is reduced about 3fold
R24A
site-directed mutagenesis of key residue Arg24 in the N-terminal domain to Ala prevents hexamer formation of enzyme AtGAD1 in solution. The dimeric mutant enzyme forms a stable hexamer in the presence of Ca2+/ CaM1
A408F
virtual point mutation, modelling
D304A
virtual point mutation, modelling
D304C
virtual point mutation, modelling
D304I
virtual point mutation, modelling
D304M
virtual point mutation, modelling
D304P
virtual point mutation, modelling
D304S
virtual point mutation, modelling
D304T
virtual point mutation, modelling
D304V
virtual point mutation, modelling
E89A
-
site-directed mutagenesis
E89A/H465A
-
site-directed mutagenesis, the double mutation not only brakes the cooperativity in the activity change but also yields a mutant enzyme that retains the activity at neutral pH. The resulting mutant enzyme, that is active at neutral pH, inhibits the cell growth in a glycerol medium by converting intracellular Glu into 4-aminobutanoate in an uncontrolled manner
E89Q
-
site-directed mutagenesis, double mutation Glu89Gln/DELTA452-466 strongly inhibits the cell growth and shows higher activity than mutant Glu89Gln/His465Ala
E89Q/H465A
-
site-directed mutagenesis, the double mutation not only brakes the cooperativity in the activity change but also yields a mutant enzyme that retains the activity at neutral pH. The resulting mutant enzyme, that is active at neutral pH, inhibits the cell growth in a glycerol medium by converting intracellular Glu into 4-aminobutanoate in an uncontrolled manner
I164D
virtual point mutation, modelling
I164E
virtual point mutation, modelling
I164L
virtual point mutation, modelling
I164P
virtual point mutation, modelling
I164Q
virtual point mutation, modelling
I164R
virtual point mutation, modelling
K168F
virtual point mutation, modelling
K168I
virtual point mutation, modelling
K168L
virtual point mutation, modelling
K276A
-
no decarboxylation of L-Glu. Transition temperature is 11°C higher than that of the wild-type enzyme. Limited proteolysis by trypsin shows that the mutant enzyme is more resistant to proteolytic degradation than the wild-type enzyme. Mutant enzyme contains very little pyridoxal 5'-phosphate
K276H
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no decarboxylation of L-Glu. Transition temperature is 4°C higher than that of the wild-type enzyme. Mutant enzyme contains no pyridoxal 5'-phosphate
K87F
virtual point mutation, modelling
K87W
virtual point mutation, modelling
K87Y
virtual point mutation, modelling
L60F
virtual point mutation, modelling
L60W
virtual point mutation, modelling
N302A
virtual point mutation, modelling
N302C
virtual point mutation, modelling
N302F
virtual point mutation, modelling
N302I
virtual point mutation, modelling
N302L
virtual point mutation, modelling
N302M
virtual point mutation, modelling
N302P
virtual point mutation, modelling
N302S
virtual point mutation, modelling
N302T
virtual point mutation, modelling
N302V
virtual point mutation, modelling
N316F
virtual point mutation, modelling
N316W
virtual point mutation, modelling
N316Y
virtual point mutation, modelling
N83P
virtual point mutation, modelling
N83W
virtual point mutation, modelling
Q309C
virtual point mutation, modelling
Q309I
virtual point mutation, modelling
Q309K
virtual point mutation, modelling
Q309R
virtual point mutation, modelling
Q309S
virtual point mutation, modelling
Q309T
virtual point mutation, modelling
Q309V
virtual point mutation, modelling
Q5D/V6I/T7E
site-directed mutagenesis the mutant shows higher thermostability and increased melting temperature compared to the wild-type, but shows no reduction of catalytic activity
Q5I/V6D/T7Q
mutant M6, site-directed mutagenesis, the mutant shows higher thermostability, with a 5.6times (560%) increase in half-life value at 45°C, 8.7°C rise in melting temperature (Tm) and a 14.3°C rise in the temperature at which 50% of the initial activity remained after 15 min incubation (T15/50), compared to wild-type enzyme. The induced new hydrogen bonds in the same polypeptide chain or between polypeptide chains in Escherichia coli GadB homohexamer may be responsible for the improved thermostability. Increased thermostability contributes to increased GABA conversion ability. After 12 h conversion of 3 mol/l glutamate, 297 g/l GABA is produced and 95% mole conversion rate is catalyzed by mtant M6 whole cells while those by wild-type GAD are 273.5 g/L and 86.2%, respectively
Q5N/V6Y/T7V
mutant M1, site-directed mutagenesis, the mutant shows improved thermostability and increased activity compared to the wild-type enzyme
Q5Y/V6R/T7K
mutant M8, site-directed mutagenesis, the mutant shows improved thermostability and increased activity compared to the wild-type enzyme
R319F
virtual point mutation, modelling
R319I
virtual point mutation, modelling
R319L
virtual point mutation, modelling
R319M
virtual point mutation, modelling
R319W
virtual point mutation, modelling
R319Y
virtual point mutation, modelling
R398F
virtual point mutation, modelling
R398I
virtual point mutation, modelling
R398L
virtual point mutation, modelling
R398M
virtual point mutation, modelling
R398W
virtual point mutation, modelling
R398Y
virtual point mutation, modelling
S246C
virtual point mutation, modelling
S246F
virtual point mutation, modelling
S246I
virtual point mutation, modelling
S246L
virtual point mutation, modelling
S246M
virtual point mutation, modelling
S246V
virtual point mutation, modelling
S246W
virtual point mutation, modelling
S246Y
virtual point mutation, modelling
S396C
virtual point mutation, modelling
S396F
virtual point mutation, modelling
S396I
virtual point mutation, modelling
S396L
virtual point mutation, modelling
S396M
virtual point mutation, modelling
S396R
virtual point mutation, modelling
S396V
virtual point mutation, modelling
S396W
virtual point mutation, modelling
S396Y
virtual point mutation, modelling
T214F
virtual point mutation, modelling
T214L
virtual point mutation, modelling
T410P
virtual point mutation, modelling
T410V
virtual point mutation, modelling
Y393E
virtual point mutation, modelling
Y393K
virtual point mutation, modelling
Y393Q
virtual point mutation, modelling
Y393R
virtual point mutation, modelling
C30A
mutation of Cys30 to Ala abolishes the presynaptic clustering of GAD65 in primary hippocampal neurons
C45A
mutation of Cys30 to Ala abolishes the presynaptic clustering of GAD65 in primary hippocampal neurons
T91A
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abolishes phosphorylation by protein kinase A and subsequent inhibition of enzyme activity
T91D
-
mimics the inhibiting effect of enzyme phosphorylation
T91E
-
mimics the inhibiting effect of enzyme phosphorylation
T95A
site-directed mutagenesis, the mutation T95A of the phosphorylation site abolishes the phosphorylation and its effects on enzyme activity
T95E
site-directed mutagenesis, 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
E312S
-
site-directed mutagenesis
more |
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deletion the C-terminal residues of GAD to generate a mutant, designated as GADDELTAC, which exhibits extended activity toward near-neutral pH compared to the wild-type. The microenvironment of the mutant active site is changed, the substrate entrance of the mutant is probably enlarged, homology modeling, overview. The enzyme deletion mutant GADDELTAC exhibits 4.8fold higher activity at pH 6.0 compared to the wild-type enzyme
T17I/D294G/E312S/Q346H
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site-directed mutagenesis
T17I/D294G/Q346H
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site-directed mutagenesis, the mutant has increased catalytic efficiency, showing 13.1 and 43.2fold of wild-type GadB1 activity at pH 4.6 and pH 6.0, respectively
more |
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deletion the C-terminal residues of GAD to generate a mutant, designated as GADDELTAC, which exhibits extended activity toward near-neutral pH compared to the wild-type. The microenvironment of the mutant active site is changed, the substrate entrance of the mutant is probably enlarged, homology modeling, overview. The enzyme deletion mutant GADDELTAC exhibits 4.8fold higher activity at pH 6.0 compared to the wild-type enzyme
-
E312S
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site-directed mutagenesis
-
T17I/D294G/E312S/Q346H
-
site-directed mutagenesis
-
T17I/D294G/Q346H
-
site-directed mutagenesis, the mutant has increased catalytic efficiency, showing 13.1 and 43.2fold of wild-type GadB1 activity at pH 4.6 and pH 6.0, respectively
-
DELTAC9
-
9 amino acid C-terminal deletion mutant, no formation of complexes larger than 340 kDa, no activation by Ca2+/calmodulin. The ability to bind calmodulin in the presence of Ca2+ is retained, and mutant may be purified by calmodulin affinity chroamtography. 12% of wild-type activity at pH 5.8
DELTAN18
-
18 amino acid N-terminal deletion mutant, activation by Ca2+/calmodulin is reduced by about 50%. 40% of wild-type activity at pH 5.8
D231R
site-directed mutagenesis, the mutation leads to significant decreases in BmGAD protein levels
D38K
site-directed mutagenesis
D92A
site-directed mutagenesis, active site mutant, shows reduced activity at pH 5.0 compared to wild-type GAD
E179K
site-directed mutagenesis, the mutant shows a slight higher activity compared to wild-type GAD in the pH range from pH 5.0-5.5, the activity of decreases sharply at values above pH 5.5
E294R
site-directed mutagenesis, the mutant increased activity of 119% compared to wild-type and shows a higher Vmax value than that of wild-type with 210 U/mg at pH 5.0 and 50°C
H467A
site-directed mutagenesis, the mutant increased activity of 118% compared to wild-type and shows a higher Vmax value than that of wild-type with 180 U/mg at pH 5.0 and 50°C
D38K
-
site-directed mutagenesis
-
D92A
-
site-directed mutagenesis, active site mutant, shows reduced activity at pH 5.0 compared to wild-type GAD
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E294R
-
site-directed mutagenesis, the mutant increased activity of 119% compared to wild-type and shows a higher Vmax value than that of wild-type with 210 U/mg at pH 5.0 and 50°C
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H467A
-
site-directed mutagenesis, the mutant increased activity of 118% compared to wild-type and shows a higher Vmax value than that of wild-type with 180 U/mg at pH 5.0 and 50°C
-
H465A
-
site-directed mutagenesis
H465A
the mutant is active at pH well above 5.7 and shows 78% of wild type specific activity in 0.2 M pyridine/HCl buffer, pH 4.6, at 37°C in the presence of 0.1 mM pyridoxal 5'-phosphate
additional information
removal of the first 24 N-terminal residues of AtGAD1 dramatically affects oligomerization by producing a dimeric enzyme. The deleted mutant retains decarboxylase activity, highlighting the dimeric nature of the basic structural unit of AtGAD1. The dimeric mutant enzyme forms a stable hexamer in the presence of Ca2+/CaM1. Binding of Ca2+/CaM1 appears to restore the hexamer species, since the gel filtration profiles of the mutant AtGAD1-DELTA1-24-Ca2+/CaM1 complex shows the same elution volume of the AtGAD1-Ca2+/CaM1 complex across the entire pH range. The AtGAD1-DELTA1-24 enzyme shows decreased thermal stability compared with the wild-type form
additional information
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removal of the first 24 N-terminal residues of AtGAD1 dramatically affects oligomerization by producing a dimeric enzyme. The deleted mutant retains decarboxylase activity, highlighting the dimeric nature of the basic structural unit of AtGAD1. The dimeric mutant enzyme forms a stable hexamer in the presence of Ca2+/CaM1. Binding of Ca2+/CaM1 appears to restore the hexamer species, since the gel filtration profiles of the mutant AtGAD1-DELTA1-24-Ca2+/CaM1 complex shows the same elution volume of the AtGAD1-Ca2+/CaM1 complex across the entire pH range. The AtGAD1-DELTA1-24 enzyme shows decreased thermal stability compared with the wild-type form
additional information
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determination of single nucleotide polymorphism T1095C in gene GAD2, genotype and allele frequency, overview
additional information
determination of single nucleotide polymorphism T1095C in gene GAD2, genotype and allele frequency, overview
additional information
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determination of single nucleotide polymorphisms in gene GAD1, i.e. A1005G and A399C, genotypes and allele frequencies, overview
additional information
determination of single nucleotide polymorphisms in gene GAD1, i.e. A1005G and A399C, genotypes and allele frequencies, overview
additional information
the mutant GadBDELTAHT (His465 of GadB is deleted together with the last residue in the polypeptide chain, Thr466) is active at pH well above 5.7 and shows 52% of wild type specific activity in 0.2 M pyridine/HCl buffer, pH 4.6, at 37°C in the presence of 0.1 mM pyridoxal 5'-phosphate
additional information
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the mutant GadBDELTAHT (His465 of GadB is deleted together with the last residue in the polypeptide chain, Thr466) is active at pH well above 5.7 and shows 52% of wild type specific activity in 0.2 M pyridine/HCl buffer, pH 4.6, at 37°C in the presence of 0.1 mM pyridoxal 5'-phosphate
additional information
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construction of a synthetic protein complex to improve the 4-aminobutanoate conversion in engineered Escherichia coli strain XL1-Blue, by assembling a single protein-protein interaction domain SH3 to the glutamate decarboxylase (GadA and GadB) and attaching a cognate peptide ligand to the glutamate/4-aminobutanoate antiporter (GadC) at the N-terminus, C-terminus, and the 233rd amino acid residue
additional information
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expanding the active pH range of the enzyme by breaking the cooperativeness
additional information
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generation of a DELTA452-466 deletion mutant, the mutant can convert glycerol into 4-aminobutanoate with minimal growth inhibition to maximize its space-time yield. Double mutation Glu89Gln/DELTA452-466 strongly inhibits the cell growth and shows higher activity than mutant Glu89Gln/His465Ala
additional information
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immobilization of the cellulose binding domain-enzyme fusion protein on a crystalline cellulose resin, with binding capacity of 33 nmol CBD-GAD/g resin, the immobilized enzymes retains 60% of initial activiy after 10 uses
additional information
improvement of the thermostability of GadB through structural optimization ofits N-terminal interdomain. Residues Gln5, Val6, and Thr7 are potential mutational target sites for the optimization of inter- and intra-molecular interactions of the triple-helix bundle. Generation of a deletion mutant of GadB lacking residues 1-14 at the N-terminus, GadBDELTA1-14
additional information
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improvement of the thermostability of GadB through structural optimization ofits N-terminal interdomain. Residues Gln5, Val6, and Thr7 are potential mutational target sites for the optimization of inter- and intra-molecular interactions of the triple-helix bundle. Generation of a deletion mutant of GadB lacking residues 1-14 at the N-terminus, GadBDELTA1-14
additional information
application of site-directed saturation mutagenesis of the N-terminal residues of GadB from Escherichia coli to improve its thermostability. Among the mutants tested, M6 is the most thermostable one
additional information
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application of site-directed saturation mutagenesis of the N-terminal residues of GadB from Escherichia coli to improve its thermostability. Among the mutants tested, M6 is the most thermostable one
additional information
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Corynebacterium glutamicum, the major L-glutamate producing microorganism, has been engineered to achieve direct fermentative production of GABA from glucose, method optimization, overview. In the fed-batch cultivation at pH 5.0, which is not preferable condition for cell growth, much less glutamate might be synthesized, which results in much lower production of GABA compared with that of pH 6.0. In the culture at pH 6.0, increased GAD activity can be balanced for glutamate synthesis to result in high-level production of GABA of up to 38.6 g/l. Corynebacterium glutamicum expressing Escherichia coli GAD mutant under the strong PH36 promoter produces GABA to the concentration of 5.89 g/l in GP1 medium at pH 7.0, which is 17fold higher than that obtained by Corynebacterium glutamicum expressing wild-type Escherichia coli GAD in the same condition (0.34 g/l). Optimized fed-batch culture of Corynebacterium glutamicum expressing Escherichia coli GAD mutant in GP1 medium containing 0.05 mg/l of biotin at pH 6.0, 30°C, results in the highest GABA concentration of 38.6 g/l with the productivity of 0.536 g/l/h
additional information
cross-linked aggregation method is used in order to extend the active range of GAD toward alkaline pH. Cross-linked aggregation activate GAD even at neutral and alkaline pH values. It is a useful method capable of facilitating recovery and reuse of the enzyme as well as increasing the reaction conversion by extending the active pH range of GAD. GAD from Escherichia coli is prepared as cross-linked enzyme aggregate (CLEA) in which the enzyme is precipitated using ammonium sulfate (60% saturation) and then cross-linked with glutaraldehyde (2%) in sodium acetate buffer (0.2 mol/l, pH 4.6). The cross-linked aggregation extends an active pH-range of GAD from pH 5.5 up to pH 8.0. As a result, the reaction conversion of 1 mol/l monosodium L-glutamate into GABA is improved from 13% to 22%. Moreover, the CLEA of GAD is easily recovered after the reaction and reused retaining over 95% of its initial activity during the first four cycles and over 60% activity at the 10th cycle. Method evaluation and optimization, overview
additional information
enhanced production of recombinant Escherichia coli glutamate decarboxylase through optimization of induction strategy and addition of pyridoxine, different induction strategies are investigated, induction is optimal when the temperature is maintained at 30°C, the inducer lactose is fed at a rate of 0.2 g/l/h, and protein expression is induced when the cell density (OD600) reaches 50. Under these conditions, the GAD activity of 1273.8 U/ml is achieved. The supplementing the medium with 2 mM pyridoxine hydrochloride (PN), a cheap and stable PLP precursor, at the initiation of protein expression, and then again 10 h later, results in very high GAD activity of 3193.4 U/ml. Fed-batch cultivation in a 3.6-L fermentor at 37°C and pH 7.0
additional information
-
enhanced production of recombinant Escherichia coli glutamate decarboxylase through optimization of induction strategy and addition of pyridoxine, different induction strategies are investigated, induction is optimal when the temperature is maintained at 30°C, the inducer lactose is fed at a rate of 0.2 g/l/h, and protein expression is induced when the cell density (OD600) reaches 50. Under these conditions, the GAD activity of 1273.8 U/ml is achieved. The supplementing the medium with 2 mM pyridoxine hydrochloride (PN), a cheap and stable PLP precursor, at the initiation of protein expression, and then again 10 h later, results in very high GAD activity of 3193.4 U/ml. Fed-batch cultivation in a 3.6-L fermentor at 37°C and pH 7.0
additional information
expression of gadB2 produced more GABA in Corynebacterium glutamicum than expression of gadB1. Construction of gadB2 expression strains under different RBS sequence and promoters (tacM, sglB, hmp, ilvE, cg1417, gapA, dtsR, tuf, cspB, odhL, uspA, gdh, sod, and pqo), engineering of RBS sequence and promoter, evaluation of GABA production, overview. In recombinant Corynebacterium glutamicum, the optimal pH for cell growth and Glu biosynthesis is about 7.0, whereas that for GAD activity and conversion of Glu to GABA is 5.0-6.0
additional information
expression of gadB2 produced more GABA in Corynebacterium glutamicum than expression of gadB1. Construction of gadB2 expression strains under different RBS sequence and promoters (tacM, sglB, hmp, ilvE, cg1417, gapA, dtsR, tuf, cspB, odhL, uspA, gdh, sod, and pqo), engineering of RBS sequence and promoter, evaluation of GABA production, overview. In recombinant Corynebacterium glutamicum, the optimal pH for cell growth and Glu biosynthesis is about 7.0, whereas that for GAD activity and conversion of Glu to GABA is 5.0-6.0
additional information
GABA is produced from glutamate through decarboxylation catalyzed by the recombinant glutamate decarboxylase (GAD) expressed in Escherichia coli strain BL21(DE3), the GAD-catalyzed reaction is conducted in 0.2 mol/l sodium acetate buffer (pH 4.6) with 1 mol/l monosodium glutamate at 37°C, optimization of GABA production method, overview. When commercial cation-exchange resins as solid acids are simply added to the reaction medium, the conversion improves from 13% to 67% without salt formation. Even when water is used as the reaction medium, acidic ion-exchange resins enhance the reaction conversion significantly. In a salt-free manner, acidic resins suppress the pH rise during the reaction so that they can enhance the reaction conversion. In addition, they can be recovered and reused easily after the reaction. Heterogeneous solid acids make the GABA production processmore economical and eco-friendly
additional information
optimization of the reaction conditions for recombinant GABA production by the homogenously expressed enzyme from Escherichia coli. The activity for GAD produced in media supplemented with 0.05 mM soluble vitamin B6 analogue pyridoxine hydrochloride (GAD-V) is 154.8 U/l, 1.8fold higher than that of GAD obtained without supplementation (GAD-C). Purified GAD-V exhibits increased activity of 193.4 U/mg (1.5fold higher), superior thermostability (2.8fold greater), and higher kcat/Km (1.6fold higher) compared to GAD-C. Under optimal conditions in reactions mixtures lacking added pyridoxal 5'-phosphate, crude GAD-V converts 500 g/l monosodium glutamate to GABA with a yield of 100%, and 750 g/l monosodium glutamate with a yield of 88.7%. Effect of substrate concentration on GABA production by GAD-C and GAD-V, overview
additional information
point mutation is performed virtually in the active site of the Escherichia coli GAD in order to increase thermal stability and catalytic activity of the enzyme, overview. Molecular modelling results indicate that performing mutation separately at positions 164, 302, 304, 393, 396, 398 and 410 increase binding affinity to substrate. The enzyme is predicted to be more thermostable in all 7 mutants based on DDG value. Stabilizing mutations in the active site based on DDG value, and binding energy levels, overview. Cavity volume change analysis for selected mutants
additional information
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point mutation is performed virtually in the active site of the Escherichia coli GAD in order to increase thermal stability and catalytic activity of the enzyme, overview. Molecular modelling results indicate that performing mutation separately at positions 164, 302, 304, 393, 396, 398 and 410 increase binding affinity to substrate. The enzyme is predicted to be more thermostable in all 7 mutants based on DDG value. Stabilizing mutations in the active site based on DDG value, and binding energy levels, overview. Cavity volume change analysis for selected mutants
additional information
production method optimization, overexpression of Escherichia coli gene gadB in strain BL21(DE3), overview. Some GadB proteins overexpressed in BL21(DE3)/pET20b-pelB-gadB might not be functional. The highest extracellular GadB activity (1.39 U/mL) is found in BL21(DE3)/pET20b-torAgadB with 0.7 mM IPTG induction
additional information
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production method optimization, overexpression of Escherichia coli gene gadB in strain BL21(DE3), overview. Some GadB proteins overexpressed in BL21(DE3)/pET20b-pelB-gadB might not be functional. The highest extracellular GadB activity (1.39 U/mL) is found in BL21(DE3)/pET20b-torAgadB with 0.7 mM IPTG induction
additional information
the Escherichia coli glutamate decarboxylase is expressed in Corynebacterium glutamicum for production of gamma-aminobutyric acid (GABA), a building block of the biodegradable plastic polyamide 4. Disruption of gene pknG, encoding serine/threonine protein kinase G (EC 2.7.11.1), enhances recombinant production of gamma-aminobutyric acid through reduction of the 2-oxoglutarate dehydrogenase complex (ODHC) activity regulation, PknG catalyzes the phosphorylation of OdhI, a 15 kDa subunit of ODHC, which reverses the inhibition of the ODHC activity. Strain GAD produces 13.06 g/l of GABA in 120 hours, consuming 83.62 g/l of glucose, strain GADDELTApknG produces 0.272 g/l of GABA in 120 hours, consuming less glucose
additional information
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the Escherichia coli glutamate decarboxylase is expressed in Corynebacterium glutamicum for production of gamma-aminobutyric acid (GABA), a building block of the biodegradable plastic polyamide 4. Disruption of gene pknG, encoding serine/threonine protein kinase G (EC 2.7.11.1), enhances recombinant production of gamma-aminobutyric acid through reduction of the 2-oxoglutarate dehydrogenase complex (ODHC) activity regulation, PknG catalyzes the phosphorylation of OdhI, a 15 kDa subunit of ODHC, which reverses the inhibition of the ODHC activity. Strain GAD produces 13.06 g/l of GABA in 120 hours, consuming 83.62 g/l of glucose, strain GADDELTApknG produces 0.272 g/l of GABA in 120 hours, consuming less glucose
additional information
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optimization of the reaction conditions for recombinant GABA production by the homogenously expressed enzyme from Escherichia coli. The activity for GAD produced in media supplemented with 0.05 mM soluble vitamin B6 analogue pyridoxine hydrochloride (GAD-V) is 154.8 U/l, 1.8fold higher than that of GAD obtained without supplementation (GAD-C). Purified GAD-V exhibits increased activity of 193.4 U/mg (1.5fold higher), superior thermostability (2.8fold greater), and higher kcat/Km (1.6fold higher) compared to GAD-C. Under optimal conditions in reactions mixtures lacking added pyridoxal 5'-phosphate, crude GAD-V converts 500 g/l monosodium glutamate to GABA with a yield of 100%, and 750 g/l monosodium glutamate with a yield of 88.7%. Effect of substrate concentration on GABA production by GAD-C and GAD-V, overview
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additional information
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production method optimization, overexpression of Escherichia coli gene gadB in strain BL21(DE3), overview. Some GadB proteins overexpressed in BL21(DE3)/pET20b-pelB-gadB might not be functional. The highest extracellular GadB activity (1.39 U/mL) is found in BL21(DE3)/pET20b-torAgadB with 0.7 mM IPTG induction
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additional information
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a hybrid cDNA is created by fusing a cDNA for amino acids 1-101 of GAD67 to a human cDNA for amino acids 96-585 of GAD65. The recombinant rGAD67/65 protein is expressed in yeast and has equivalent immunoreactivity to mammalian brain GAD with diabetes sera. rGAD67/65 has enzymatic properties similar to that of the mixed isoforms of GAD preparations from mammalian brain
additional information
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creation of a hybrid form of GAD consisting of amino acids 1-101 of the human GAD67 protein fused to amino acids 96-585 of the human GAD65 protein, and modification of this to include a C-terminal hexa-His tag sequence. The hybrid GAD67/65-H6 is expressed in two yeast hosts: consitutively under the control of the plasmid oxidase promoter PGK1 in Saccharomyces cerevisiae, and inducibly under the control of the chromosomal alcohol oxidase promoter AOX1 in Pichia pastoris. The hybrid GAD67/65 is isolated at high specific activity and moderate yield, and the addition of the His6 tag sequence of the choice of the yeast strain does not appreciably affect enzyme activity, percentage recovery of GAD, protein purification or utility in diagnosis of diabetes in terms of specificity and sensitivity to the various sera
additional information
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expression and characterization of naturally occurring shorter forms of enzyme. Isoform GAD67 with N-terminal deletion of 70 or 90 amino acids has about 20% of wild-type activity
additional information
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construction of a truncated enzyme version
additional information
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crystallization data of N-terminally truncated isoform GAD67, expressing amino acids 90-594, catalytically active, and of N-terminally truncated isoform GAD65 expressing amino acids 84-585
additional information
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construction of transgenic Chlamydomonas reinhardtii expressing the human enzyme in chloroplasts, expression analysis and immunohistochemic protein detection, overview
additional information
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detection of a naturally occuring mutant with nine single nucleotide polymorphisms spanning the promoter region of the GAD1 gene to the 3'-UTR
additional information
the optimal fermentation conditions for GABA production from recombinant Lactobacillus plantarum strain overexpressing the Lactobacillus plantarum enzyme using response surface methodology are a glutamic acid concentration of 497.973 mM, temperature 36°C, pH 5.31, and time 60 h. Under these conditions, maximum GABA concentration obtained is 11.09 mM. GAD activity of the cell extract released by the recombinant strain (167.2 units/ml/min) is sevenfold greater than the GAD activity of wild-type cells (23.5 units/ml/min). Modelling of recombinant enzyme production, overview
additional information
generation of C-terminally truncated (DELTA3 and DELTA11 residues) mutants, their enzyme activities are compared with that of the wild-type enzyme at different pH values. Unlike the wild-type GAD, the mutants show 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
additional information
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generation of C-terminally truncated (DELTA3 and DELTA11 residues) mutants, their enzyme activities are compared with that of the wild-type enzyme at different pH values. Unlike the wild-type GAD, the mutants show 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
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additional information
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the optimal fermentation conditions for GABA production from recombinant Lactobacillus plantarum strain overexpressing the Lactobacillus plantarum enzyme using response surface methodology are a glutamic acid concentration of 497.973 mM, temperature 36°C, pH 5.31, and time 60 h. Under these conditions, maximum GABA concentration obtained is 11.09 mM. GAD activity of the cell extract released by the recombinant strain (167.2 units/ml/min) is sevenfold greater than the GAD activity of wild-type cells (23.5 units/ml/min). Modelling of recombinant enzyme production, overview
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additional information
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directed evolution of GadB1 using site-specific mutagenesis, mutant screening
additional information
immobilization of recombinant GadA on a nickel affinity Sepharose resin for usage in L-glutamate conversions in a packed-bed reactor, method evaluation. The immobilization yield of GadA on the resin reaches 95.8% when the conditions are as follows: coupling time of 1 h at 25°C in working buffer, containing 50 mM sodium acetate, pH 4.0, 50 mM ammonium sulfate, and 0.1 mM pyridoxal 5'-phosphate, and enzyme loading of 42 mgGadA/g wet resin
additional information
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immobilization of recombinant GadA on a nickel affinity Sepharose resin for usage in L-glutamate conversions in a packed-bed reactor, method evaluation. The immobilization yield of GadA on the resin reaches 95.8% when the conditions are as follows: coupling time of 1 h at 25°C in working buffer, containing 50 mM sodium acetate, pH 4.0, 50 mM ammonium sulfate, and 0.1 mM pyridoxal 5'-phosphate, and enzyme loading of 42 mgGadA/g wet resin
additional information
the production of gamma-aminobutyric acid in Escherichia coli BL21 harboring gadlbhye1/pET28a is increased by adding pyridoxine as a cheaper coenzyme
additional information
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the production of gamma-aminobutyric acid in Escherichia coli BL21 harboring gadlbhye1/pET28a is increased by adding pyridoxine as a cheaper coenzyme
additional information
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immobilization of recombinant GadA on a nickel affinity Sepharose resin for usage in L-glutamate conversions in a packed-bed reactor, method evaluation. The immobilization yield of GadA on the resin reaches 95.8% when the conditions are as follows: coupling time of 1 h at 25°C in working buffer, containing 50 mM sodium acetate, pH 4.0, 50 mM ammonium sulfate, and 0.1 mM pyridoxal 5'-phosphate, and enzyme loading of 42 mgGadA/g wet resin
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additional information
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the production of gamma-aminobutyric acid in Escherichia coli BL21 harboring gadlbhye1/pET28a is increased by adding pyridoxine as a cheaper coenzyme
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additional information
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directed evolution of GadB1 using site-specific mutagenesis, mutant screening
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additional information
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isoform GAD65 knock-out mice show upregulated level of vesicular gamma-aminobutanoate transporter, and no change in the synaptic vesicles-associated isoform GAD67. In mutant mice, synaptic vesicles transport cytosolic gamma-aminobutanoate much more efficiently than wild-type
additional information
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construction of cells overexpressing the GFP-tagged enzyme in membranes of cell somata, dendrites, axons and synaptic terminals of dentate neurons, subcellular localization, correlation to the amount of voltage-gated potassium channels Kv3.1b and Kv3.3, overview
additional information
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construction of cerebellum-selective GAD67-knockout mice, selective GAD67 deletion in the cerebellum iss achieved using a Cre-loxP strategy. GABA level is reduced to 16-44% in the cerebellum but not in the cerebrum, inhibitory synaptic transmission to Purkinje cells is seriously impaired, however, the morphology of Purkinje cells and the density of synaptic terminals in the cerebellar cortex appears unaffected, phenotype, overview
additional information
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construction of GFP-tagged GAD67 overexpressing mutant mice
additional information
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targeted ablation of the GAD65 gene in Gad65-/- mice results in a pronounced context-independent, intramodal generalization of auditory fear memory during long-term/24 h or 14 d but not short-term/30 min memory retrieval, phenotype analysis, overview
additional information
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construction of cells overexpressing the GFP-tagged enzyme in membranes of cell somata, dendrites, axons and synaptic terminals of dentate neurons, subcellular localization, correlation to the amount of voltage-gated potassium channels Kv3.1b and Kv3.3, overview
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additional information
mutant lacking 31 amino acids at C-terminal extension shows 40fold higher activity than wild-type at physiological pH value. Rice plants overexpressing the mutant enzyme have aberrant phenotypes such as dwarfism, etiolated leaves, and sterility
additional information
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mutant lacking 31 amino acids at C-terminal extension shows 40fold higher activity than wild-type at physiological pH value. Rice plants overexpressing the mutant enzyme have aberrant phenotypes such as dwarfism, etiolated leaves, and sterility
additional information
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method evaluation for production of plant enzyme in bacteria at industrial scale
additional information
a constructed mutant DELTA466-467 shows reduced activity at pH 5.0 compared to wild-type GAD
additional information
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a constructed mutant DELTA466-467 shows reduced activity at pH 5.0 compared to wild-type GAD
additional information
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a constructed mutant DELTA466-467 shows reduced activity at pH 5.0 compared to wild-type GAD
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additional information
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development of a hyperthermostable enzyme for industrial applications, overview
additional information
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improvement of gamma-amino butyric acid production by an overexpression of glutamate decarboxylase from Pyrococcus horikoshii in Escherichia coli, optimization of GABA production method, overview. The highest final GABA concentration, 5.07 g/l, is obtained from 10 g/l of monosodium glutamate with a GABA yield of 83% at 30ºC and pH 3.5. When Pyrococcus horikoshii glutamate decarboxylase is introduced into a GABA aminotransferase knockout Escherichia coli XBT strain, 5.69 g/l of GABA is produced with a GABA yield of 93%
additional information
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construction of a truncated enzyme version
additional information
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construction of a C-terminal 44-kDa truncated GAD, i.e. GAD44. GAD25 corresponds to the putative regulatory domain of the full-length protein, GAD44 contains the cofactor-binding site and enzymatic activity for synthesis of gamma-butyric acid
additional information
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the recombinant human enzyme injected into LEW.1A rats shows a half-life of 2.77 h
additional information
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the recombinant human enzyme injected into LEW.1A rats shows a half-life of 2.77 h
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additional information
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optimization of bioproduction of gamma-GABA using recombinant Escherichia coli expressing a GAD enzyme derived from eukaryote. The optimal medium for Escherichia coli-ScGAD cultivation and expression is 10 g/l lactose, 5 g/l glycerol, 20 g/l yeast extract, and 10 g/l sodium chloride, resulting in an activity of 55 U/ml medium, three times higher than that of using Luria-Bertani (LB) medium. The maximal concentration of gamma-GABA is 245 g/l whereas L-glutamic acid is near completely converted
additional information
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optimization of bioproduction of gamma-GABA using recombinant Escherichia coli expressing a GAD enzyme derived from eukaryote. The optimal medium for Escherichia coli-ScGAD cultivation and expression is 10 g/l lactose, 5 g/l glycerol, 20 g/l yeast extract, and 10 g/l sodium chloride, resulting in an activity of 55 U/ml medium, three times higher than that of using Luria-Bertani (LB) medium. The maximal concentration of gamma-GABA is 245 g/l whereas L-glutamic acid is near completely converted
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additional information
generation of an enzyme deletion strain, DELTAgad, transcription levels of genes involved in nitrogen metabolism are upregulated in the mutant strain
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6*His-tagged isoforms GAD65 and GAD67 expressed in Saccharomyces cerevisiae
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a hybrid cDNA is created by fusing a cDNA for amino acids 1-101 of GAD67 to a human cDNA for amino acids 96-585 of GAD65. The recombinant rGAD67/65 protein is expressed in yeast and has equivalent immunoreactivity to mammalian brain GAD with diabetes sera
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creation of a hybrid form of GAD consisting of amino acids 1-101 of the human GAD67 protein fused to amino acids 96-585 of the human GAD65 protein, and modification of this to include a C-terminal hexa-His tag sequence. The hybrid GAD67/65-H6 is expressed in two yeast hosts: constitutively under the control of the plasmid oxidase promoter PGK1 in Saccharomyces cerevisiae, and inducibly under the control of the chromosomal alcohol oxidase promoter AOX1 in Pichia pastoris. The hybrid GAD67/65 is isolated at high specific activity and moderate yield, and the addition of the His6 tag sequence of the choice of the yeast strain does not appreciably affect enzyme activity, percentage recovery of GAD, protein purification or utility in diagnosis of diabetes in terms of specificity and sensitivity to the various sera
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expressed in Corynebacterium glutamicum strain ATCC 13032
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expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21-codonPlus-(DE3)-RIL cells
expressed in Escherichia coli DH5alpha cells
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expressed in Escherichia coli JM109 cells
expressed in Lactobacillus sakei strain B2-16
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expression as glutathione S-transferase-fusion protein
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expression as maltose binding protein-fusion protein
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expression in Bacillus subtilis
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expression in Escherichia coli
expression in Escherichia coli (DE3)
expression in Sacchaormyces cerevisiae, His-tag
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Expression of aggregation-prone deletion mutant protein (amino acids 448-585) using RNA polymerase sigma factor (RpoS) or glutathione S-transferase as fusion partners in Escherichia coli strain BL21 (DE3).
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expression of deletion mutant (rGAD65)C45A/DELTA1-38 and (rGAD65)DELTA1-101, expression in COS-7 cells
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expression of labeled GAD65 in CHO cells
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expression of the full-length and truncated mutant enzymes, expression analysis
GAD65 and GAD67 expression analysis in embryo and adult hippocampi
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GAD67 gene fragments from a TT2 cell genomic library, overexpression of the coding sequence of the EGFP-poly(A) gene in TT2 ES cells
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gene DjGAD, DNA and amino acid sequence determination and analysis
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gene gabB, recombinant expression in Escherichia coli strain BL21(DE3), intracellular and extracellular expression of GadB from BL21(DE3)/pET20b-gadB, BL21(DE3)/pET20b-pelBgadB, and BL21(DE3)/pET20b-torA-gadB, subcloning in Escherichia coli strain JM109
gene gad, cloned from genomic DNA, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
gene gad, cloning from germinated faba bean, DNA and amino acid sequence determination and analysis, sequence comparisons
gene gad, cloning in Escherichia coli strain DH5alpha, overexpression of His-tagged wild-type and mutant in Escherichia coli strain BL21(DE3)
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gene gad, DNA and amino acid sequence determimation and analysis, sequence comparisons, recombinant overexpression in Lactobacillus plantarum strain Taj-Apis362
gene gad, DNA and amino acid sequence determination and analysis, cloning in Escherichia coli strain DH5alpha, expression of His-tagged enzyme in Escherichia coli strain M15
gene gad, DNA and amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene gad, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree
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gene gad, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant overexpression in Escherichia coli strain BL21(DE3), real-time PCR enzyme expression analysis
gene gad, DNA and amino acid sequence determination and analysis, sequence comparisons, expression in Escherichia coli strains BL21 and JM109
gene gad, DNA and amino acid sequence determination and analysis, sequence comparisons, functional recombinant expression of soluble His-tagged enzyme in Escherichia coli strain BL21(DE3)
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gene gad, DNA and amino acid sequence determination and analysis, the protein sequence is identical to the LbGadB of the strain ATCC 367, recombinant expression of His-tagged enzyme in Escherichia coli strain Origami 2 (DE3)
gene gad, expression of enzyme as maltose-bindig protein fusion protein in Escherichia coli strain TB1
gene gad, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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gene gad, recombinant lactose-induced overexpression of enzyme GAD in Escherichia coli strain BL21(DE3)
gene gad, RT-PCR expression analysis
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gene gad, the enzyme is fused to the cellulose-binding domain and a linker of Trichoderma harzianum endoglucanase II, or S3N10 peptide replacing the native linker to prevent proteolytic cleavage, functional expression of the His6-tagged fusion construct in Escherichia coli strain BL21(DE3)
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gene GAD1, DNA and amino acid sequence determination and analysis, genotyping
gene GAD1, genomic organization, the gene located within chromosome 2q31 encodes the isozyme GAD67
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gene gad1, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)pLysS
gene GAD2, DNA and amino acid sequence determination and analysis, genotyping
gene gad65, expression of the enzyme as maltose-bindig protein fusion protein in Escherichia coli strain TB1
gene GAD65, recombinant expression of full-length human GAD65 in Chlamydomonas reinhardtii strain 137c chloroplast genome under the control of the Chlamydomonas reinhardtii chloroplast rbcL promoter and 5'- and 3'-UTRs by particle bombardment
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gene GAD65, recombinant expression of GST-tagged or MBP-fusion wild-type enzyme, a 1757-bp hGAD65 insert from the pET-5C plasmid subcloned into the pMAL-c2X protein fusion system, in Escherichia coli strain DH5alpha, 1.6fold higher hGAD65 activity of the purified MBP-tagged enzyme construct compared to GST-tagged enzyme
gene GAD65, recombinant expression of GST-tagged wild-type and mutant isozymes in Escherichia coli strain DH5alpha or strain BL21
gene GAD67, cloning of four GAD67 transcripts, GAD67-C1, -C2, -C3, and -C4, produced by alternative splicing and polyadenlyation and translating a GAD protein with truncated pyridoxal 5'-phosphate binding domain, which leads to a lack of glutamate decarboxylase activity, expression in HEK-293 cells
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gene GAD67, expression analysis
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gene gad67, expression of the isozyme as maltose-bindig protein fusion protein in Escherichia coli strain TB1
gene GAD67, recombinant expression of GST-tagged wild-type isozyme in Escherichia coli strain DH5alpha or strain BL21
gene gadA, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21-CodonPlus (DE3)
gene gadB, DNA and amin acid sequence determination and analysis, expression in Escherichia coli strain DH5alpha
gene gadB, DNA and amin acid sequence determination and analysis, expression of the His-tagged enzyme in Escherichia coli strains Rosetta-gami B (DE3) ad JM109
gene gadB, DNA and amino acid sequence determination and analysis
gene gadB, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene gadB, DNA and amino acid sequence determination and analysis, sequence comparisons, operon structure of gadCB, RT-PCR expression analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3). The gadC gene is amplified from the genomic DNA by using a primer set based on gadC from Lactobacillus brevis strain ATCC 367
gene gadB, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression in Escherichia coli strain BL21(DE3)
gene gadB, expression in Escherichia coli strain DH5alpha using plasmids pMAL-c2X and the pGEX-3X and fusion to the maltose binding protein or GST, cytoplasmic targeting, overview
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gene gadB, expression in Escherichia coli strain W3110 in glucose medium without the addition of glutamate. Addition of 0.1 mM pyridoxal 5'-phosphate enhances the production of 4-aminobutanoate, whereas Tween 40 is unnecessary for the fermentation productivity, different cultivation methods, overview
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gene gadB, expression of C-terminally His-tagged wild-type and mutant enzyme in Escherichia coli strain BL21(DE3), cloning in Escherichia coli strain DH5alpha
gene gadB, recombinant cytoplasmic expression in Escherichia coli strain BL21(DE3), using vectors pMD18-T and pET-24a(+) and IPTG induction, subcloning in Escherichia coli strain JM109
gene gadB, recombinant expression in Corynebacterium glutamicum strain ATCC 13032 with or without gene pknG knockout
gene gadB, recombinant expression in Escherichia coli strain BL21(DE3)
gene gadB, recombinant expression in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
gene gadB, recombinant expression in GABA aminotransferase-knockout Escherichia coli strain XBT from plasmid pHBP, subcloning in Escherichia coli strain XL-1 Blue
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gene gadB, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), that lacks endogenous GAD enzyme activity. The Escherichia coli strain Gad-negative phenotype might arise either from the single nucleotide polymorphisms detected in the promoter region of gadA (at position -50 relative to the transcription start site) and gadB (at position -190 relative to the transcription start site) genes or from reduced activity/expression of the transcriptional regulators necessary to trigger the expression of the GDAR system
gene gadB, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
gene gadB, recombinant expression of holoenzyme
gene gadB, recombinnat enzyme expression in Corynebacterium glutamicum, evaluation of PH36, PI16, and PL26 promoters for optimal expression and different pH value for engineered cultures
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gene gadB, sequence comparisons, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3). The expression level of both truncated mutants in Escherichia coli at 25°C is much higher than that at 37°C
gene gadB1, expression of wild-type and mutant enzymes in Corynebacterium glutamicum strain ATCC 13032 leads to increased 4-aminobutanoate levels in the transgenic bacterium
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gene gadB1, recombinant expression in Corynebacterium glutamicum strain SH, subcloning in Escherichia coli strain JM109
gene gadB2, recombinant expression in Corynebacterium glutamicum strain SH, subcloning in Escherichia coli strain JM109. Construction of gadB2 expression strains under different RBS sequence and promoter, expression of gadB2 with bicistronic expression cassette, overview
gene gadlbhye1, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
genes GAd65 and GAD67, expression analysis in brain tissues
genes gadA and gadB, co-overexpression of the enzyme fused to a protein-protein interaction domain SH3 in Escherichia coli strain XL1-Blue with gene gadC encoding an antiporter
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genes gadD1, gadD2, and gadD3 encode glutamate decarboxylases, the genes are organized in three separate genetic loci, gadD1T1, gadT2D2, and gadD3, with the two genes gadT1 and gadT2 encoding for antiporters. Strain-to-strain differences in gad gene transcription, real-time RT-PCR determination of gad gene transcription in response to pH value, overview
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genotyping and expression analysis of isozyme GAD1 and GAD2 genes in individuals from Ireland and North Ireland, detailed overview
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GST-GAD fusion protein expressed in Escherichia coli
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IPTG-induced functional recombinant expression of His-tagged Oryza sativa GAD isozymes in Escherichia coli strain MC1061 at 28°C and 37°C, method optimization
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recombinant expression and sequence comparisons
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recombinant expression of isozyme GAD65 using the Spodoptera frugiperda transfection method
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tissue expression pattern of GAD67, overview
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truncated enzyme, recloned into the Escherichia coli expression vector pET11a, the N-terminal 77-84 amino acid residues encoded by the cloned gene have been deleted
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
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expression of the full-length and truncated mutant enzymes, expression analysis
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expression of the full-length and truncated mutant enzymes, expression analysis
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expression of the full-length and truncated mutant enzymes, expression analysis
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gene gad, DNA and amino acid sequence determination and analysis, cloning in Escherichia coli strain DH5alpha, expression of His-tagged enzyme in Escherichia coli strain M15
gene gad, DNA and amino acid sequence determination and analysis, cloning in Escherichia coli strain DH5alpha, expression of His-tagged enzyme in Escherichia coli strain M15
genes GAd65 and GAD67, expression analysis in brain tissues
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genes GAd65 and GAD67, expression analysis in brain tissues
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