Target type: biologicalprocess
The removal of a C-terminal, gene-encoded glutamate residue from a protein. [GOC:sp, PMID:21074048]
C-terminal protein deglutamylation is a critical post-translational modification involved in the removal of glutamate residues from the C-terminus of proteins. This process plays a vital role in regulating protein function, stability, and interactions.
**Mechanism of C-terminal Protein Deglutamylation:**
The enzymatic removal of glutamate residues is catalyzed by a family of enzymes known as carboxypeptidases. These enzymes exhibit substrate specificity, targeting proteins with C-terminal glutamate residues. The reaction mechanism involves the hydrolysis of the peptide bond between the penultimate amino acid and the C-terminal glutamate residue.
**Biological Significance:**
* **Protein Stability:** Deglutamylation can influence protein stability by altering the interactions between the protein and its surrounding environment.
* **Protein Function:** The removal of glutamate residues can modulate protein activity by affecting its ability to bind to other molecules or undergo conformational changes.
* **Protein Targeting:** Deglutamylation can regulate the trafficking of proteins to specific cellular compartments.
* **Cellular Signaling:** Deglutamylation is implicated in various cellular signaling pathways, including those involved in growth, differentiation, and stress responses.
**Examples of Deglutamylation Targets:**
* **Histones:** Deglutamylation of histone tails is involved in chromatin remodeling and gene regulation.
* **Tubulin:** Deglutamylation of tubulin affects microtubule dynamics and cytoskeletal organization.
* **Neurotransmitters:** Deglutamylation of neurotransmitter precursors influences neurotransmission.
**Regulation of Deglutamylation:**
The activity of carboxypeptidases, and consequently the rate of deglutamylation, is regulated by various factors, including:
* **Substrate Availability:** The abundance of substrates with C-terminal glutamate residues.
* **Cellular Environment:** pH, temperature, and the presence of cofactors can influence enzyme activity.
* **Post-translational Modifications:** Phosphorylation or acetylation of carboxypeptidases can modulate their activity.
**Conclusion:**
C-terminal protein deglutamylation is a crucial post-translational modification that plays a diverse role in cellular processes. The removal of glutamate residues at protein C-termini can influence protein stability, function, targeting, and signaling, ultimately impacting cellular homeostasis and organismal development.'
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Protein | Definition | Taxonomy |
---|---|---|
Glutamate carboxypeptidase 2 | A glutamate carboxypeptidase 2 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q04609] | Homo sapiens (human) |
Compound | Definition | Classes | Roles |
---|---|---|---|
glutamic acid | glutamic acid : An alpha-amino acid that is glutaric acid bearing a single amino substituent at position 2. Glutamic Acid: A non-essential amino acid naturally occurring in the L-form. Glutamic acid is the most common excitatory neurotransmitter in the CENTRAL NERVOUS SYSTEM. | glutamic acid; glutamine family amino acid; L-alpha-amino acid; proteinogenic amino acid | Escherichia coli metabolite; ferroptosis inducer; micronutrient; mouse metabolite; neurotransmitter; nutraceutical |
quisqualic acid | Quisqualic Acid: An agonist at two subsets of excitatory amino acid receptors, ionotropic receptors that directly control membrane channels and metabotropic receptors that indirectly mediate calcium mobilization from intracellular stores. The compound is obtained from the seeds and fruit of Quisqualis chinensis. | non-proteinogenic alpha-amino acid | |
plasmenylserine | O-phospho-L-serine : The L-enantiomer of O-phosphoserine. O-phosphoserine : A serine derivative that is serine substituted at the oxygen atom by a phosphono group. plasmenylserine: RN given refers to (L)-isomer | O-phosphoserine | EC 1.4.7.1 [glutamate synthase (ferredoxin)] inhibitor; EC 2.5.1.49 (O-acetylhomoserine aminocarboxypropyltransferase) inhibitor; EC 4.3.1.10 (serine-sulfate ammonia-lyase) inhibitor; Escherichia coli metabolite; human metabolite; mouse metabolite; Saccharomyces cerevisiae metabolite |
alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid | |||
serine o-sulfate | L-serine O-sulfate : A non-proteinogenic L-alpha-amino acid that is the O-sulfo derivative of L-serine. serine O-sulfate: RN given refers to (L)-isomer | L-serine derivative; non-proteinogenic L-alpha-amino acid; O-sulfoamino acid | |
isospaglumic acid | Ac-Asp-Glu : A dipeptide composed of N-acetyl-L-aspartic acid and L-glutamic acid joined by a peptide linkage. isospaglumic acid: mediator in the sensitivity of animals to hyperbaric oxygenation; Naaxia is the tradename; apparently can have both a neuroprotective and a neurotoxic effect | dipeptide | human metabolite |
sq 14,603 | 2-benzyl-3-mercaptopropanoic acid: structure; carboxypeptidase inhibitor | ||
willardiine | 3-(uracil-1-yl)-L-alanine : The 3-(uracil-1-yl) derivative of L-alanine. willardiine: isolated from seeds of Acacia willariana; structure | amino acid zwitterion; L-alanine derivative; non-proteinogenic L-alpha-amino acid | |
gamma-glutamyl hydroxamate | glutamine hydroxamate : A hydroxamic acid that is L-glutamine hydroxylated at N-5. | amino acid zwitterion; glutamic acid derivative; hydroxamic acid | |
phenobarbital sodium | 2-(phosphonomethyl)pentanedioic acid: an N-acetylated alpha-linked acidic dipeptidase (NAALADase) antagonist | ||
gpi 5693 | 2-(3-mercaptopropyl)pentanedioic acid: inhibits glutamate carboxypeptidase II; structure in first source | ||
zj43 | ZJ43: N-acetylaspartylglutamate (NAAG) peptidase inhibitor; structure in first source | ||
psma-617 | PSMA-617: inhibits prostate-specific membrane antigen; structure in first source |