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Glutamate transporters are a family of neurotransmitter transporter proteins that move glutamate – the principal excitatory neurotransmitter – across a membrane. The family of glutamate transporters is composed of two primary subclasses: the excitatory amino acid transporter ( EAAT ) family and vesicular glutamate transporter ( VGLUT ) family.
The sodium/glutamate symporter, also known as glutamate permease, is a transmembrane protein family found in bacteria and archaea. These proteins are symporters that are responsible for the sodium-dependent uptake of extracellular glutamate into the cell. They are integral membrane proteins located in the bacterial inner membrane. [1]
These proteins are predicted to have 12 alpha-helical transmembrane regions, some of the animal proteins may have an additional C-terminal helix. [4] The X-ray structure of the NorM was determined to 3.65 Å, revealing an outward-facing conformation with two portals open to the outer leaflet of the membrane and a unique topology of the predicted 12 transmembrane helices distinct from any other ...
In animals, fungi, and bacteria, GABA-T helps facilitate a reaction that moves an amine group from GABA to 2-oxoglutarate, and a ketone group from 2-oxoglutarate to GABA. [4] [5] [6] This produces succinate semialdehyde and L-glutamate. [4] In plants, pyruvate and glyoxylate can be used in the place of 2-oxoglutarate.
Excitatory amino acid transporter 1 (EAAT1) is a protein that, in humans, is encoded by the SLC1A3 gene. [5] EAAT1 is also often called the GLutamate ASpartate Transporter 1 ( GLAST-1 ). EAAT1 is predominantly expressed in the plasma membrane, allowing it to remove glutamate from the extracellular space. [ 6 ]
The basic fold of the MFS transporter is built around 12, [4] or in some cases, 14 transmembrane helices [5] (TMH), with two 6- (or 7- ) helix bundles formed by the N and C terminal homologous domains [6] of the transporter which are connected by an extended cytoplasmic loop. The two halves of the protein pack against each other in a clam-shell ...
In bacteria, the ammonia is assimilated to amino acids via glutamate and aminotransferases. [2] In plants, the enzyme can work in either direction depending on environment and stress. [ 3 ] [ 4 ] Transgenic plants expressing microbial GLDHs are improved in tolerance to herbicide, water deficit, and pathogen infections. [ 5 ]
Glutamate racemase performs the additional function of gyrase inhibition, preventing gyrase from binding to DNA. [3] Glutamate racemase (MurI) serves two distinct metabolic functions: primarily, it is a critical enzyme in cell wall biosynthesis, [2] but also plays a role in gyrase inhibition. [3]