EC Number   |
Natural Substrates |
|---|
   6.3.2.61 | ATP + alpha-tubulin + L-glutamate |
glutamylation on alpha-tubulin is not essential but is required for efficiency of assembly and function of a subset of microtubule-based organelles, the spatial restriction of modifying enzymes appears to be a major mechanism that drives differential glutamylation at the subcellular level |
| 6.3.2.61 | ATP + [alpha/beta-tubulin]-(alpha-L-glutamyl-gamma-L-glutamyl)-L-glutamate + n L-glutamate |
(1c) |
| 6.3.2.61 | ATP + [alpha/beta-tubulin]-(gamma-L-glutamyl)-L-glutamate + L-glutamate |
(1b) |
| 6.3.2.61 | ATP + [alpha/beta-tubulin]-L-glutamate + L-glutamate |
(1a) |
| 6.3.2.61 | more |
Ttll1p and Ttll9p are tubulin tyrosine ligase domain proteins, that act as alpha-tubulin-preferring glutamyl ligase enzymes, TTLL1- and TLLL9-type enzymes are highly conserved but are absent from higher plants and fungi, overview |
| 6.3.2.61 | n ATP + [alpha-tubulin]-L-glutamate + n L-glutamate |
overall reaction |
| 6.3.2.61 | n ATP + [alpha-tubulin]-L-glutamate + n L-glutamate |
overall reaction, higher activity compared to beta-tubulin |
| 6.3.2.61 | n ATP + [alpha/beta-tubulin]-L-glutamate + n L-glutamate |
overall reaction. The enzyme incorporates glutamic acid preferentially into the more acidic variants of both alpha- and beta-tubulins |
| 6.3.2.61 | n ATP + [beta-tubulin]-L-glutamate + n L-glutamate |
overall reaction |
| 6.3.2.61 | n ATP + [tubulin]-L-glutamate + n L-glutamate |
overall reaction, the enzyme has an initiating activity with a preference for alpha-tubulin, but also shows partial activity on beta-tubulin |
