The Enzyme Database

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Accepted name: tubulin-glutamate carboxypeptidase
Reaction: 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, tubulinyl-Tyr carboxypeptidase). The latter is cleaved to δ2-tubulin and further to δ3-tubulin.
Other name(s): cytosolic carboxypeptidase 5; CCP5; Agtpbp1 (gene name); AGBL5 (gene name)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Rogowski, K., van Dijk, J., Magiera, M.M., Bosc, C., Deloulme, J.C., Bosson, A., Peris, L., Gold, N.D., Lacroix, B., Bosch Grau, M., Bec, N., Larroque, C., Desagher, S., Holzer, M., Andrieux, A., Moutin, M.J. and Janke, C. A family of protein-deglutamylating enzymes associated with neurodegeneration. Cell 143 (2010) 564–578. [PMID: 21074048]
2.  Kimura, Y., Kurabe, N., Ikegami, K., Tsutsumi, K., Konishi, Y., Kaplan, O.I., Kunitomo, H., Iino, Y., Blacque, O.E. and Setou, M. Identification of tubulin deglutamylase among Caenorhabditis elegans and mammalian cytosolic carboxypeptidases (CCPs). J. Biol. Chem. 285 (2010) 22936–22941. [PMID: 20519502]
3.  Pathak, N., Austin-Tse, C.A., Liu, Y., Vasilyev, A. and Drummond, I.A. Cytoplasmic carboxypeptidase 5 regulates tubulin glutamylation and zebrafish cilia formation and function. Mol. Biol. Cell 25 (2014) 1836–1844. [PMID: 24743595]
[EC created 2020]

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