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The family of glutamate transporters is composed of two primary subclasses: the excitatory amino acid transporter (EAAT) family and vesicular glutamate transporter (VGLUT) family. In the brain, EAATs remove glutamate from the synaptic cleft and extrasynaptic sites via glutamate reuptake into glial cells and neurons , while VGLUTs move glutamate ...
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]
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.
For example, SLC1A1 is the first isoform of subfamily A of SLC family 1. An exception occurs with SLC family 21 [ 5 ] (the organic anion transporting polypeptide transporters), which for historical reasons have names in the format SLCOnXm where n = family number, X = subfamily letter, and m = member number.
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 ]
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]
Gamma-glutamyltransferase (also γ-glutamyltransferase, GGT, gamma-GT, gamma-glutamyl transpeptidase; [1] EC 2.3.2.2) is a transferase (a type of enzyme) that catalyzes the transfer of gamma-glutamyl functional groups from molecules such as glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate).