3.4.17.24: tubulin-glutamate carboxypeptidase

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For detailed information about tubulin-glutamate carboxypeptidase, go to the full flat file.

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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 alpha- and gamma-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 beta-tubulin and detyrosinated alpha-tubulin (from which the C-terminal L-tyrosine has been removed by EC 3.4.17.17, tubulinyl-Tyr carboxypeptidase). The latter is cleaved to delta2-tubulin and further to delta3-tubulin. =

Synonyms

AGBL5, CCP1, CCP5, CCPP-1, ccpp-6, cytosolic carboxypeptidase 1, cytosolic carboxypeptidase 5, cytosolic carboxypeptidase 6, cytosolic carboxypeptidase CCP1, cytosolic carboxypeptidase-like protein 5, deglutamylase, Nna1, tubulinyl-Glu carboxypeptidase

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.17 Metallocarboxypeptidases

                3.4.17.24 tubulin-glutamate carboxypeptidase

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Results	in table
3051	AA Sequence
4	Cloned(Commentary)
23	Disease/ Diagnostics
1	Expression
14	General Information
1	Inhibitors
5	kcat/KM [mM/s]
4	KM Value [mM]
6	Localization
1	Molecular Weight [Da]
15	Organism
1	pH Optimum
2	Purification (Commentary)
2	Reaction
14	Reference
19	Source Tissue
41	Substrates and Products (Substrate)
23	Synonyms
1	Temperature Optimum [°C]
4	Turnover Number [1/s]