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Literature summary for 6.3.2.25 extracted from

  • Deans, N.L.; Allison, R.D.; Purich, D.L.
    Steady-state kinetic mechanism of bovine brain tubulin:tyrosine ligase (1992), Biochem. J., 286, 243-251.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
ADP competitive with respect to ATP, non-competitive with respect to tubulin and L-Tyr Bos taurus
AMP
-
Bos taurus
L-hydroxyphenylalanine
-
Bos taurus
NEM substrate protects Bos taurus
phosphate very weak Bos taurus
tyrosinated tubulin very weak Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0019
-
untyrosinated tubulin
-
Bos taurus
0.014
-
ATP
-
Bos taurus
0.017
-
L-Tyr
-
Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + detyrosinated alpha-tubulin + L-tyrosine = alpha-tubulin + ADP + phosphate random sequential mechanism Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + detyrosinated alpha-tubulin + L-tyrosine
-
Bos taurus alpha-tubulin + ADP + phosphate
-
r