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Literature summary for 6.3.2.25 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
Search for more literature for 6.3.2.25

Inhibitors

Inhibitors Comment Organism Structure
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
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

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Sus scrofa
-
-
-

Substrates and Products (Substrate)

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

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

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Sus scrofa
ATP
-
 Bos taurus

General Information

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