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
Tubulinyl-Tyr carboxypeptidase
Identifiers
EC number3.4.17.17
CAS number73050-23-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

This enzyme is active at neutral pH.

This activity has been linked to proteins such as AGTPBP1 in human.[4]

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. 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.
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