EC Number   |
Substrates |
Products |
Reversibility |
|---|
   6.3.2.61 | ATP + acidic nuclear phosphoprotein 32 family, member A + L-glutamate |
very low activity with isoform TTLL4 |
? |
- |
? |
| 6.3.2.61 | ATP + acidic nuclear phosphoprotein 32 family, member A + L-glutamate |
low activity with isoform TTLL5 |
? |
- |
? |
| 6.3.2.61 | ATP + acidic nuclear phosphoprotein 32 family, member B + L-glutamate |
high activity with isoform TTLL4 |
? |
- |
? |
| 6.3.2.61 | ATP + acidic nuclear phosphoprotein 32 family, member B + L-glutamate |
low activity with isoform TTLL5 |
? |
- |
? |
| 6.3.2.61 | ATP + alpha tubulin + L-glutamate |
Ttll1p glutamylase preferentially modifies alpha-tubulin. It shows a chain-initiating activity |
? |
- |
? |
| 6.3.2.61 | ATP + alpha tubulin + L-glutamate |
Ttll9p glutamylase preferentially modifies alpha-tubulin. It has primarily a chain-elongating activity |
? |
- |
? |
| 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 |
L-glutamyl-alpha-tubulin + ADP + phosphate |
- |
? |
| 6.3.2.61 | ATP + alpha-tubulin + L-glutamate |
in an in vitro microtubule glutamylation assay, Ttll1p shows a chain-initiating activity while Ttll9p has primarily a chain-elongating activity. MALDI-TOF mass spectrometry analysis of glutamylated forms of ciliary alpha-tubulin |
L-glutamyl-alpha-tubulin + ADP + phosphate |
- |
? |
| 6.3.2.61 | ATP + B23 nucleophosmin + L-glutamate |
highest activity with isoform TTLL4 |
? |
- |
? |
| 6.3.2.61 | ATP + B23 nucleophosmin + L-glutamate |
low activity with isoform TTLL5 |
? |
- |
? |
