Tubulin—tyrosine ligase
tubulin-tyrosine ligase | |||||||||
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Identifiers | |||||||||
EC number | 6.3.2.25 | ||||||||
CAS number | 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 / EGO | ||||||||
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In enzymology, a tubulin-tyrosine ligase (EC 6.3.2.25) is an enzyme that catalyzes the chemical reaction
- ATP + detyrosinated alpha-tubulin + L-tyrosine alpha-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.
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