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Literature summary 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

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.2.25 0.0019
-
 untyrosinated tubulin
-
 Bos taurus
6.3.2.25 0.014
-
 ATP
-
 Bos taurus
6.3.2.25 0.017
-
 L-Tyr
-
 Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
6.3.2.25 Bos taurus
-
-
-

Reaction

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.3.2.25 brain
-
 Bos taurus
-

Substrates and Products (Substrate)

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