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Literature summary extracted from

  • Szyk, A.; Piszczek, G.; Roll-Mecak, A.
    Tubulin tyrosine ligase and stathmin compete for tubulin binding in vitro (2013), J. Mol. Biol., 425, 2412-2414.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.2.25 stathmin inhibits the enzyme's tubulin tyrosination activity in vitro suggesting either that tubulin tyrosine ligase and stathmin have a partially overlapping footprint on the tubulin dimer or that stathmin induces a tubulin conformation incompatible with stable tubulin tyrosine ligase binding Bos taurus
6.3.2.25 stathmin inhibits the enzyme's tubulin tyrosination activity in vitro suggesting either that tubulin tyrosine ligase and stathmin have a partially overlapping footprint on the tubulin dimer or that stathmin induces a tubulin conformation incompatible with stable tubulin tyrosine ligase binding Sus scrofa

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.2.25 Mg2+ required Sus scrofa
6.3.2.25 Mg2+ required Bos taurus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.2.25 ATP + detyrosinated alpha-tubulin + L-tyrosine Sus scrofa
-
 alpha-tubulin + ADP + phosphate
-
 ?
6.3.2.25 ATP + detyrosinated alpha-tubulin + L-tyrosine Bos taurus
-
 alpha-tubulin + ADP + phosphate
-
 ?

Organism

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

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
-
 Sus scrofa alpha-tubulin + ADP + phosphate
-
 ?
6.3.2.25 ATP + detyrosinated alpha-tubulin + L-tyrosine
-
 Bos taurus alpha-tubulin + ADP + phosphate
-
 ?
6.3.2.25 additional information full-length stathmin and tubulin tyrosine ligase compete for binding to tubulin and fail to make a stable tubulin:stathmin:tubulin tyrosine ligase triple complex in solution Sus scrofa ?
-
 ?
6.3.2.25 additional information full-length stathmin and tubulin tyrosine ligase compete for binding to tubulin and fail to make a stable tubulin:stathmin:tubulin tyrosine ligase triple complex in solution Bos taurus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.3.2.25 TTL
-
 Sus scrofa
6.3.2.25 TTL
-
 Bos taurus
6.3.2.25 tubulin tyrosine ligase
-
 Sus scrofa
6.3.2.25 tubulin tyrosine ligase
-
 Bos taurus

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.2.25 ATP
-
 Sus scrofa
6.3.2.25 ATP
-
 Bos taurus

General Information

EC Number General Information Comment Organism
6.3.2.25 physiological function tubulin tyrosine ligase forms a stable complex with tubulin and inhibits tubulin polymerization, it competes in this function with stathmin Sus scrofa
6.3.2.25 physiological function tubulin tyrosine ligase forms a stable complex with tubulin and inhibits tubulin polymerization, it competes in this function with stathmin Bos taurus