Biology:Tubulinyl-Tyr carboxypeptidase
From HandWiki
| Tubulinyl-Tyr carboxypeptidase | |||||||||
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| Identifiers | |||||||||
| EC number | 3.4.17.17 | ||||||||
| CAS number | 73050-23-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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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.[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
- ↑ "Tubulinyl-tyrosine carboxypeptidase from chicken brain: properties and partial purification". Journal of Neurochemistry 34 (1): 114–8. January 1980. doi:10.1111/j.1471-4159.1980.tb04628.x. PMID 7452228.
- ↑ "Preferential action of a brain detyrosinolating carboxypeptidase on polymerized tubulin". The Journal of Biological Chemistry 256 (14): 7678–86. July 1981. PMID 6114100.
- ↑ "Association of tubulinyl-tyrosine carboxypeptidase with microtubules". FEBS Letters 157 (1): 75–8. June 1983. doi:10.1016/0014-5793(83)81119-3. PMID 6862022.
- ↑ "Nna1-like proteins are active metallocarboxypeptidases of a new and diverse M14 subfamily". FASEB Journal 21 (3): 851–65. March 2007. doi:10.1096/fj.06-7330com. PMID 17244817.
External links
- Tubulinyl-Tyr+carboxypeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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