Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.17.24 extracted from

  • Kimura, Y.; Kurabe, N.; Ikegami, K.; Tsutsumi, K.; Konishi, Y.; Kaplan, O.I.; Kunitomo, H.; Iino, Y.; Blacque, O.E.; Setou, M.
    Identification of tubulin deglutamylase among Caenorhabditis elegans and mammalian cytosolic carboxypeptidases (CCPs) (2010), J. Biol. Chem., 285, 22936-22941.
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Caenorhabditis elegans Q09296
-
-
Mus musculus Q09M02
-
-

Source Tissue

Source Tissue Comment Organism Textmining
ciliary body
-
Caenorhabditis elegans
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information CCP5 does not have detyrosinase activity Mus musculus ?
-
?

Synonyms

Synonyms Comment Organism
AGBL5
-
Mus musculus
ccpp-6
-
Caenorhabditis elegans
cytosolic carboxypeptidase 6
-
Caenorhabditis elegans

General Information

General Information Comment Organism
physiological function loss of ccpp-6 gene function, which encodes one of two cytosolic carboxypeptidases, results in elevated levels of ciliary microtubule polyglutamylation. Overexpression of this gene in ciliated cells decreases polyglutamylation signals Caenorhabditis elegans
physiological function overexpression of murine CCP5 causes a dramatic loss of microtubule polyglutamylation in cultured mammalian cells. Recombinantly expressed Myc-tagged CCP5 exhibits deglutamylase biochemical activities Mus musculus