Tubulinyl-Tyr carboxypeptidase
Tubulinyl-Tyr carboxypeptidase (EC 3.4.17.17, carboxypeptidase-tubulin, soluble carboxypeptidase, tubulin-tyrosine carboxypeptidase, tubulin carboxypeptidase, tubulinyltyrosine carboxypeptidase, tyrosinotubulin carboxypeptidase, tyrosyltubulin carboxypeptidase, TTCPase, brain I carboxypeptidase) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
- Cleavage of the -Glu--Tyr bond to release the C-terminal tyrosine residue from the native tyrosinated tubulin. Inactive on Z-Glu-Tyr
This enzyme is active at neutral pH.
This activity has been linked to proteins such as AGTPBP1 in human.[4]
References
- ↑ Argaraña, C.E., Barra, H.S. and Caputto, R. (1980). "Tubulinyl-tyrosine carboxypeptidase from chicken brain: properties and partial purification". J. Neurochem. 34: 114–118. doi:10.1111/j.1471-4159.1980.tb04628.x. PMID 7452228.
- ↑ Kumar, N. and Flavin, M. (1981). "Preferential action of a brain detyrosinolating carboxypeptidase on polymerized tubulin". J. Biol. Chem. 256: 7678–7686. PMID 6114100.
- ↑ Arce, C.A. and Barra, H.S. (1983). "Association of tubulinyl-tyrosine carboxypeptidase with microtubules". FEBS Lett. 157: 75–78. doi:10.1016/0014-5793(83)81119-3. PMID 6862022.
- ↑ Rodriguez de la Vega, M. (2007). "Nna1-like proteins are active metallocarboxypeptidases of a new and diverse M14 subfamily". The FASEB Journal 21: 851–65. doi:10.1096/fj.06-7330com. PMID 17244817.
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