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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. 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.

References

1. Argarana CE, Barra HS, Caputto R (January 1980). "Tubulinyl-tyrosine carboxypeptidase from chicken brain: properties and partial purification". Journal of Neurochemistry. 34 (1): 114–8. doi:10.1111/j.1471-4159.1980.tb04628.x. PMID 7452228.
2. Kumar N, Flavin M (July 1981). "Preferential action of a brain detyrosinolating carboxypeptidase on polymerized tubulin". The Journal of Biological Chemistry. 256 (14): 7678–86. doi:10.1016/S0021-9258(19)69014-9. PMID 6114100.
3. Arce CA, Barra HS (June 1983). "Association of tubulinyl-tyrosine carboxypeptidase with microtubules". FEBS Letters. 157 (1): 75–8. doi:10.1016/0014-5793(83)81119-3. PMID 6862022.
4. Rodriguez de la Vega M, Sevilla RG, Hermoso A, Lorenzo J, Tanco S, Diez A, Fricker LD, Bautista JM, Avilés FX (March 2007). "Nna1-like proteins are active metallocarboxypeptidases of a new and diverse M14 subfamily". FASEB Journal. 21 (3): 851–65. doi:10.1096/fj.06-7330com. PMID 17244817.

External links

• Tubulinyl-Tyr+carboxypeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

• Biology

• EC 3.4.17