EC 3 - Hydrolases
EC 3.4 - Acting on peptide bonds (peptidases)
EC 3.4.17 - Metallocarboxypeptidases
EC 3.4.17.24 - Tubulin-glutamate carboxypeptidase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 3.4.17.24
Names
Accepted name:
tubulin-glutamate carboxypeptidase
Other
names:
cytosolic carboxypeptidase 1
cytosolic carboxypeptidase 5
cytosolic carboxypeptidase 5
Systematic name:
-
Reactions
- (1) detyrosyl-tubulin + H2O = Delta2-tubulin + L-glutamate
- (2) Delta2-tubulin + H2O = Delta3-tubulin + L-glutamate
Comments:
This is a subfamily of enzymes that cleave C-terminal and/or side chain amino acids from tubulins. The dual-specificity enzymes can cleave both α- and γ-linked L-glutamate from tubulins, removing the posttranslationally added polyglutamyl side chains from the C-terminal regions. In addition, the enzyme removes two glutamate residues from the C-terminus of β-tubulin and detyrosinated α-tubulin (from which the C-terminal L-tyrosine has been removed by EC 3.4.17.17). The latter is cleaved to Δ2-tubulin and further to Δ3-tubulin.
Links to other databases
References
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A family of protein-deglutamylating enzymes associated with neurodegeneration.Cell 143 : 564-578 (2010). [PMID: 21074048]
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Identification of tubulin deglutamylase among Caenorhabditis elegans and mammalian cytosolic carboxypeptidases (CCPs).J. Biol. Chem. 285 : 22936-22941 (2010). [PMID: 20519502]
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Cytosolic carboxypeptidase 1 is involved in processing alpha- and gamma-tubulin.J. Biol. Chem. 287 : 6503-6517 (2012). [PMID: 22170066]
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Cytosolic carboxypeptidase 5 removes alpha- and gamma-linked glutamates from tubulin.J. Biol. Chem. 288 : 30445-30453 (2013). [PMID: 24022482]
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Cytoplasmic carboxypeptidase 5 regulates tubulin glutamylation and zebrafish cilia formation and function.Mol. Biol. Cell 25 : 1836-1844 (2014). [PMID: 24743595]
[EC 3.4.17.24 created 2020]