G7509
GABase from Pseudomonas fluorescens
lyophilized powder, Protein ≥30 % by biuret
Synonym(s):
GABase Enzyme, GABase from Pseudomonas, Pseudomonas GABase
biological source
Pseudomonas fluorescens
assay
≥30 % (biuret)
form
lyophilized powder
specific activity
≥0.5 units/mg protein
composition
Protein, ≥30% biuret
technique(s)
inhibition assay: suitable
storage temp.
−20°C
Quality Level
General description
Research area: Neuroscience
GABase is a commercially available mixture composed of γ-aminobutyric acid aminotransferase (GABGT) and succinic semialdehyde dehydrogenase (SSDH) obtained from Pseudomonas fluorescens.
GABase is a commercially available mixture composed of γ-aminobutyric acid aminotransferase (GABGT) and succinic semialdehyde dehydrogenase (SSDH) obtained from Pseudomonas fluorescens.
Application
GABase from Pseudomonas fluorescens has been used for GABase assay to quantify the extracellular and intracellular concentration of GABA (γ-aminobutyric acid).
Biochem/physiol Actions
GABase catalyzes the conversion of γ-aminobutyric acid (GABA) to succinic acid in the central nervous system. It is used to measure GABA levels in various biological samples. p-Hydroxybenzaldehyde (HBA) is known to be a potential inhibitor on GABase.
Physical form
Partially purified lyophilized powder containing buffer salts and stabilizer
Other Notes
One unit will convert 1.0 μmole of γ-aminobutyric acid (GABA) to succinic semialdehyde and then to succinate per min with a stoichiometric reduction of 1.0 μmole of NADP+ at pH 8.6 at 25 °C.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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A Vidal-Cros et al.
The Biochemical journal, 229(3), 675-678 (1985-08-01)
L-threo-3-Fluoroglutamate and L-erythro-3-fluoroglutamate were tested with glutamate decarboxylase from Escherichia coli. Both isomers were substrates: the threo isomer was decarboxylated into optically active 4-amino-3-fluorobutyrate, whereas the erythro isomer lost the fluorine atom during the reaction, yielding succinic semialdehyde after hydrolysis
GABase and glutaminase inhibitory activities of herbal extracts and acylated flavonol monoglycosides isolated from the leaves of Laurus nobilis L
Shimada A, et al.
Zeitschrift fur Naturforschung. C, Journal of biosciences, 78(9-10), 377-381 (2023)
Mingu Gordon Park et al.
Journal of enzyme inhibition and medicinal chemistry, 36(1), 2016-2024 (2021-09-14)
Many studies have focussed on modulating the activity of γ-aminobutyric acid transaminase (GABA-T), a GABA-catabolizing enzyme, for treating neurological diseases, such as epilepsy and drug addiction. Nevertheless, human GABA-T synthesis and purification have not been established. Thus, biochemical and drug
Structural and Mechanistic Basis for the Inactivation of Human Ornithine Aminotransferase by (3 S,4 S)-3-Amino-4-fluorocyclopentenecarboxylic Acid
Shen S, et al.
Molecules (Basel), 28(3) (2023)
Nicolaie Moldovan et al.
Sensors and actuators. B, Chemical, 337 (2022-05-24)
Glutamate (GLU) and gamma-aminobutyric acid (GABA) are neurotransmitters (NTs) with an essential role in signal transmission in the brain. Brain disorders, such as epilepsy, Alzheimer's and Parkinson's diseases, and traumatic brain injury can be linked to imbalances in the GLU-GABA
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