Glutamate amino acid family

Kanai Y, Hediger MA (2004) The glutamate/neutral amino acid transporter family SLC1 molecular, physiological and pharmacological aspects. Pfliigers Arch 447 469-479... 

There are six families of amino acids glutamate, serine, aspartate, pyruvate, the aromatics, and histidine. The nonessential amino acids are derived from precursor molecules available in many organisms. The essential amino acids are synthesized from metabolites produced only in plants and some microorganisms. 

Kanai, Y, and M. A. Hediger. The glutamate and neutral amino acid transporter family Physiological and pharmacological implications. 479(1-3),... 

Drosophila DDC belongs to a family of pyridoxal-dependent decarboxylases that extends from prokaryotes to eukaryotic plants and animals. The members of this family show significant sequence similarity over much of their length, even though the individual proteins have quite different substrate specificities, including the amino acids tyrosine, tryptophan, phenylalanine, histidine, and glutamate, and the amino acid derivatives... 

FIGURE 2.3 The three main families of mammalian G-protein-coupled 7TM receptors in mammals. No obvious sequence identity is found between the rhodopsin-like family A, the glucagon/VIP/calcitonin family B, and the metabotropic glutamate/chemosensor family C of G-protein-coupled 7TM receptors, with the exception of the disulfide bridge between the top of TM-III and the middle of extracellular loop-2 (see Figure 2.2). Similarly, no apparent sequence identity exists among members of these three families and, for example the 7TM bitter taste receptors, the V1R pheromone receptors, and the 7TM frizzled proteins, which all are either known or believed to be G-protein-coupled receptors. Bacteriorhodopsins, which are not G-protein-coupled proteins but proton pumps, are totally different in respect to amino-acid sequence but have a seven-helical bundle arranged rather similarly to that for the G-protein-coupled receptors. 

Arriza, J. L., Kavanaugh, M. P., Fairman, W. A., Wu, Y.-N., Murdoch, G. H., North, R. A., and Amara, S. G. (1993) Cloning and expression of a human neutral amino acid transporter with structural similarity to the glutamate transporter gene family. J. Biol. Chem. 268, 15329-15332. 

Amino Acid Biosynthesis Aromatic amino acid family Aspartate family Glutamate family Pyruvate family Serine family Histidine family Other... 

Unlike the AAOs, whose very name implies a breadth of substrate specificity, the aaDHs tend to be rather more specific and are each named after their optimal amino acid substrate. In particular, the archetype in this enzyme family, GDH, shows poor activity with most substrates other than glutamate. However, the availability of X-ray crystallographic structures for several aaDHs ° has opened the door to site-directed mutagenesis and altered substrate specificities. " ... 

Trypsin inhibitors in cucumber were first found in a study by Walker-Simmons et /. " after wounding of leaves and treatment with proteinase inhibitor-inducing factor (PIIF). The amino acid sequence of two inhibitors isolated from Cucurhita maxima (winter squash) were determined by Wilusz et at The peptides named ITD I and ITD 111 each comprised a 29-residue sequence with six cysteine residues. The only difference between the two peptides is in position 9, which is lysine in ITD I and glutamic acid in ITD III. The reactive site is located at the peptide bond between Arg5 and Ile6. Owing to their discovery and distribution in Cucurbitaceae the inhibitor family has been named squash inhibitors. Since the initial discoveries many other members of the squash family have been found. 

In addition to the 0-methylation of aspartate and glutamate residues, the C-terminal carboxyl group of GTPases are methylated. In the G-protein family C-terminal cysteines are prenylated at the sequence CZZX, where Z is a hydrophobic amino acid and X represents any residue. Once the ZZX sequence is cleaved by a special protease, the isoprenylcysteine carboxymethyltransferase (Icmt) methylates the C-terminal carboxyl group and effectively creates a more hydrophobic enzyme. ... 

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