6.3.2.25: tubulin-tyrosine ligase
This is an abbreviated version!
For detailed information about tubulin-tyrosine ligase, go to the full flat file.
Word Map on EC 6.3.2.25
-
6.3.2.25
-
microtubule
-
detyrosinated
-
hardware
-
non-sentinel
-
d-roms
-
polyglutamylation
-
analysis
-
synthesis
- 6.3.2.25
- microtubule
-
detyrosinated
-
hardware
-
non-sentinel
-
d-roms
-
polyglutamylation
- analysis
- synthesis
Reaction
Synonyms
Synthetase, tubulin-tyrosine, TTL, TTLase, tubulin tyrosine ligase, tubulin-tyrosine ligase, tubulin-tyrosine-ligase, Tubulin:tyrosine ligase, tubuline-tyrosine ligase, Tyrosyltubulin ligase
ECTree
Advanced search results
Inhibitors
Inhibitors on EC 6.3.2.25 - tubulin-tyrosine ligase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
(1R,4aS,6R,8S)-6,8-dihydroxy-5-[(3E)-5-hydroxy-5-(3-hydroxy-5-oxo-2,5-dihydrofuran-2-yl)-3-methylpent-3-en-1-yl]-4a,6-dimethyldecahydronaphthalene-1-carboxylic acid
-
increases the non-tyrosinatable form of alpha-tubulin in human cancer cell cultures indicating to act as an inhibitor of TTL
3-nitro-L-tyrosine
-
50% inhibition of tyrosine incorporation at 50fold higher concentrations of nitrotyrosine
ADP
-
competitive with respect to ATP, non-competitive with respect to tubulin and L-Tyr
-
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
-
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
-