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Literature summary extracted from

  • Wloga, D.; Rogowski, K.; Sharma, N.; van Dijk, J.; Janke, C.; Edde, B.; Bre, M.-H.; Levilliers, N.; Redeker, V.; Duan, J.; Gorovsky, M.A.; Jerka-Dziadosz, M.; Gaertig, J.
    Glutamylation on alpha-tubulin is not essential but affects the assembly and functions of a subset of microtubules in Tetrahymena thermophila (2008), Eukaryot. Cell, 7, 1362-1372.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.2.B3 expression of GFP-tagged protein in Tetrahymena thermophila Tetrahymena thermophila
6.3.2.61
-
 Tetrahymena thermophila

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
6.3.2.B3 cilium main localization, GFP-tagged recombinant protein Tetrahymena thermophila 5929
-
6.3.2.B3 flagellar basal body Ttll1 localizes primarily to the basal bodies of oral and somatic cilia Tetrahymena thermophila
-
-
6.3.2.61 cilium Ttll9p is mainly localized in cilia Tetrahymena thermophila 5929
-
6.3.2.61 flagellar basal body Ttll1p localizes primarily to the basal bodies of oral and somatic cilia Tetrahymena thermophila
-
-

Organism

EC Number Organism UniProt Comment Textmining
6.3.2.B3 Tetrahymena thermophila Q23SI8
-
-
6.3.2.B3 Tetrahymena thermophila I7MCG4
-
-
6.3.2.B3 Tetrahymena thermophila SB210 I7MCG4
-
-
6.3.2.B3 Tetrahymena thermophila SB210 Q23SI8
-
-
6.3.2.61 Tetrahymena thermophila Q23SI8
-
-
6.3.2.61 Tetrahymena thermophila I7MCG4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.2.B3 partial purification of recombinant GFP-tagged Ttll1 and GFP-tagged Ttll9 Tetrahymena thermophila
6.3.2.61
-
 Tetrahymena thermophila
6.3.2.61 partial Tetrahymena thermophila

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.2.B3 ATP + alpha-tubulin + L-glutamate
-
 Tetrahymena thermophila L-glutamyl-alpha-tubulin + ADP + phosphate
-
 ?
6.3.2.B3 ATP + alpha-tubulin + L-glutamate
-
 Tetrahymena thermophila SB210 L-glutamyl-alpha-tubulin + ADP + phosphate
-
 ?
6.3.2.61 ATP + alpha tubulin + L-glutamate Ttll1p glutamylase preferentially modifies alpha-tubulin. It shows a chain-initiating activity Tetrahymena thermophila ?
-
 ?
6.3.2.61 ATP + alpha tubulin + L-glutamate Ttll9p glutamylase preferentially modifies alpha-tubulin. It has primarily a chain-elongating activity Tetrahymena thermophila ?
-
 ?
6.3.2.61 ATP + alpha tubulin + L-glutamate Ttll9p glutamylase preferentially modifies alpha-tubulin. It has primarily a chain-elongating activity Tetrahymena thermophila SB210 ?
-
 ?
6.3.2.61 ATP + alpha tubulin + L-glutamate Ttll1p glutamylase preferentially modifies alpha-tubulin. It shows a chain-initiating activity Tetrahymena thermophila SB210 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.3.2.B3 alpha-tubulin polyglutamylase
-
 Tetrahymena thermophila
6.3.2.B3 TTHERM_00773080
-
 Tetrahymena thermophila
6.3.2.B3 TTL domain protein
-
 Tetrahymena thermophila
6.3.2.B3 TTLL1
-
 Tetrahymena thermophila
6.3.2.B3 TTLL9
-
 Tetrahymena thermophila
6.3.2.B3 tubulin glutamylase
-
 Tetrahymena thermophila
6.3.2.B3 tubulin tyrosine ligase domain protein
-
 Tetrahymena thermophila
6.3.2.61 Ttll1p
-
 Tetrahymena thermophila
6.3.2.61 Ttll9p
-
 Tetrahymena thermophila

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.3.2.B3 30
-
 assay at Tetrahymena thermophila

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
6.3.2.B3 30
-
 assay at Tetrahymena thermophila

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3.2.B3 9
-
 assay at Tetrahymena thermophila

General Information

EC Number General Information Comment Organism
6.3.2.B3 physiological function Ttll9 glutamylase preferentially modifies alpha-tubulin. It has primarily a chain-elongating activity. The spatial restriction of modifying enzymes TTLL1 and TTLL9 appears to be a major mechanism that drives differential glutamylation at the subcellular level. Disruption of the isoforms TTLL1 and TTLL9 genes decreases the rates of cell multiplication and phagocytosis. Cells lacking both genes have fewer cortical microtubules and show defects in the maturation of basal bodies. In the TTLL1 and TTLL9 double knockout, a decrease in the levels of glutamylation on alpha-tubulin occurs Tetrahymena thermophila
6.3.2.B3 physiological function Ttll1p glutamylase preferentially modifies alpha-tubulin. It shows a chain-initiating activity. The spatial restriction of modifying enzymes TTLL1 and TTLL9 appears to be a major mechanism that drives differential glutamylation at the subcellular level. Disruption of the isoforms TTLL1 and TTLL9 genes decreases the rates of cell multiplication and phagocytosis. Cells lacking both genes have fewer cortical microtubules and show defects in the maturation of basal bodies. In the TTLL1 and TTLL9 double knockout, a decrease in the levels of glutamylation on alpha-tubulin occurs Tetrahymena thermophila
6.3.2.61 malfunction disruption of the TTLL1 and TTLL9 genes decreases the rates of cell multiplication and phagocytosis. Cells lacking both genes had fewer cortical microtubules and show defects in the maturation of basal bodies Tetrahymena thermophila
6.3.2.61 malfunction disruption of the TTLL1 and TTLL9 genes decreases the rates of cell multiplication and phagocytosis. Cells lacking both genes have fewer cortical microtubules and show defects in the maturation of basal bodies Tetrahymena thermophila
6.3.2.61 physiological function glutamylation on alpha-tubulin is not essential but is required for efficiency of assembly and function of a subset of microtubule-based organelles. Furthermore, the spatial restriction of modifying enzymes appears to be a major mechanism that drives differential glutamylation at the subcellular level Tetrahymena thermophila
6.3.2.61 physiological function glutamylation on alpha-tubulin is not essential but is required for efficiency of assembly and function of a subset of microtubule-based organelles. Furthermore, the spatial restriction of modifying enzymes (TTLL1 and TTLL9) appears to be a major mechanism that drives differential glutamylation at the subcellular level Tetrahymena thermophila