Enzymes
UniProtKB help_outline | 4,252 proteins |
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Name help_outline
(L-glutamyl)n-γ-L-glutamyl-L-glutamate residue
Identifier
CHEBI:143623
Charge
-3
Formula
(C5H6NO3)n.C10H12N2O6
Search links
Involved in 4 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:15675Polymer name: (L-glutamyl)(n+1)-γ-L-glutamyl-L-glutamyl-[protein]Polymerization index help_outline n+1Formula C10H12N2O6(C5H6NO3)n+1Charge (-2)(-1)n+1Mol File for the polymer
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Identifier: RHEA-COMP:15519Polymer name: (L-glutamyl)(n)-γ-L-glutamyl-L-glutamyl-[protein]Polymerization index help_outline nFormula C10H12N2O6(C5H6NO3)nCharge (-2)(-1)nMol File for the polymer
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- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,048 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-glutamate Identifier CHEBI:29985 (CAS: 11070-68-1) help_outline Charge -1 Formula C5H8NO4 InChIKeyhelp_outline WHUUTDBJXJRKMK-VKHMYHEASA-M SMILEShelp_outline [NH3+][C@@H](CCC([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 242 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:60004 | RHEA:60005 | RHEA:60006 | RHEA:60007 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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The cytosolic carboxypeptidases CCP2 and CCP3 catalyze posttranslational removal of acidic amino acids.
Tort O., Tanco S., Rocha C., Bieche I., Seixas C., Bosc C., Andrieux A., Moutin M.J., Aviles F.X., Lorenzo J., Janke C.
The posttranslational modification of carboxy-terminal tails of tubulin plays an important role in the regulation of the microtubule cytoskeleton. Enzymes responsible for deglutamylating tubulin have been discovered within a novel family of mammalian cytosolic carboxypeptidases. The discovery of t ... >> More
The posttranslational modification of carboxy-terminal tails of tubulin plays an important role in the regulation of the microtubule cytoskeleton. Enzymes responsible for deglutamylating tubulin have been discovered within a novel family of mammalian cytosolic carboxypeptidases. The discovery of these enzymes also revealed the existence of a range of other substrates that are enzymatically deglutamylated. Only four of six mammalian cytosolic carboxypeptidases had been enzymatically characterized. Here we complete the functional characterization of this protein family by demonstrating that CCP2 and CCP3 are deglutamylases, with CCP3 being able to hydrolyze aspartic acids with similar efficiency. Deaspartylation is a novel posttranslational modification that could, in conjunction with deglutamylation, broaden the range of potential substrates that undergo carboxy-terminal processing. In addition, we show that CCP2 and CCP3 are highly regulated proteins confined to ciliated tissues. The characterization of two novel enzymes for carboxy-terminal protein modification provides novel insights into the broadness of this barely studied process. << Less
Mol. Biol. Cell 25:3017-3027(2014) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Cytosolic carboxypeptidase 5 removes alpha- and gamma-linked glutamates from tubulin.
Berezniuk I., Lyons P.J., Sironi J.J., Xiao H., Setou M., Angeletti R.H., Ikegami K., Fricker L.D.
Cytosolic carboxypeptidase 5 (CCP5) is a member of a subfamily of enzymes that cleave C-terminal and/or side chain amino acids from tubulin. CCP5 was proposed to selectively cleave the branch point of glutamylated tubulin, based on studies involving overexpression of CCP5 in cell lines and detecti ... >> More
Cytosolic carboxypeptidase 5 (CCP5) is a member of a subfamily of enzymes that cleave C-terminal and/or side chain amino acids from tubulin. CCP5 was proposed to selectively cleave the branch point of glutamylated tubulin, based on studies involving overexpression of CCP5 in cell lines and detection of tubulin forms with antisera. In the present study, we examined the activity of purified CCP5 toward synthetic peptides as well as soluble α- and β-tubulin and paclitaxel-stabilized microtubules using a combination of antisera and mass spectrometry to detect the products. Mouse CCP5 removes multiple glutamate residues and the branch point glutamate from the side chains of porcine brain α- and β-tubulin. In addition, CCP5 excised C-terminal glutamates from detyrosinated α-tubulin. The enzyme also removed multiple glutamate residues from side chains and C termini of paclitaxel-stabilized microtubules. CCP5 both shortens and removes side chain glutamates from synthetic peptides corresponding to the C-terminal region of β3-tubulin, whereas cytosolic carboxypeptidase 1 shortens the side chain without cleaving the peptides' γ-linked residues. The rate of cleavage of α linkages by CCP5 is considerably slower than that of removal of a single γ-linked glutamate residue. Collectively, our data show that CCP5 functions as a dual-functional deglutamylase cleaving both α- and γ-linked glutamate from tubulin. << Less
J. Biol. Chem. 288:30445-30453(2013) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.
Comments
The reaction continues until n=0. n is normally in the range of 3-8. For tubulin, the highest number known is n=21.