Tubulin—tyrosine ligase
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| Tubulin—tyrosine ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.3.2.25 | ||||||||
| CAS no. | 60321-03-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a tubulin—tyrosine ligase (EC 6.3.2.25) is an enzyme that catalyzes the chemical reaction
- ATP + detyrosinated α-tubulin + L-tyrosine α-tubulin + ADP + phosphate
The 3 substrates of this enzyme are ATP, detyrosinated alpha-tubulin, and L-tyrosine, whereas its 3 products are alpha-tubulin, ADP, and phosphate.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is alpha-tubulin:L-tyrosine ligase (ADP-forming).
References
- Wehland J, Schroder HC, Weber K (1986). "Isolation and purification of tubulin tyrosine ligase". Methods Enzymol. 134: 170–9. doi:10.1016/0076-6879(86)34086-2. PMID 3821560.
- Rudiger M, Wehland J, Weber K (1994). "The carboxy-terminal peptide of detyrosinated alpha tubulin provides a minimal system to study the substrate specificity of tubulin-tyrosine ligase". Eur. J. Biochem. 220 (2): 309–20. doi:10.1111/j.1432-1033.1994.tb18627.x. PMID 7510228.
