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
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6.3.2.25
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microtubule
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detyrosinated
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hardware
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non-sentinel
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d-roms
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polyglutamylation
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analysis
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synthesis
- 6.3.2.25
- microtubule
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detyrosinated
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hardware
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non-sentinel
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d-roms
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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
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General Information on EC 6.3.2.25 - tubulin-tyrosine ligase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
malfunction
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mutation of tubulin binding residues largely abolishes the enzyme ability to tyrosinate alpha-tubulin and restrict neurite outgrowth in cultured neurons. The neuronal defects of tubulin tyrosine ligase knockout mice are due to the loss of tubulin tyrosination and not because the enzyme is required to tyrosinate any other substrates. Neurons from TTL-null mice show strong developmental defects, including increased neurite extensions and premature differentiation
physiological function
additional information
the enzyme's tubulin-contacting residues are well conserved. The alpha-tubulin residues alphaGlu441 and alphaGlu449 anchor the tail by forming hydrogen bonds with residues Arg73, Ala75, Ser76, Ser152, and Val179, and Asn10, Ser12, Arg44, and Pro336 of TTL, respectively. When bound to the enzyme, the polypeptide chain of the alpha-tubulin tail adopts a loop-like conformation between the tail-anchoring residues alphaGlu441 and alphaGlu449. The enzyme's orientation on tubulin heterodimers places its catalytic domain near to alpha-tubulin's C-terminal tail, which binds to the enzyme's active site through two glutamate residues missing from beta-tubulin's C-terminus
physiological function
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plays a role in cell division, in particular in cell wall deposition
physiological function
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plays a role in cell division, in particular in cell wall deposition
physiological function
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the enzyme specifically recognizes the C-terminus of alpha-tubulin adding L-tyrosine to modulate the behavior of microtubules, tyrosinated microtubules are more dynamic than detyrosinated filaments in cells. The enzyme is bound at the interface of tubulin alpha- and beta-subunits and specifically recognizes the tubulin dimer's curved conformation
physiological function
the enzyme specifically recognizes the C-terminus of alpha-tubulin adding L-tyrosine to modulate the behavior of microtubules, tyrosinated microtubules are more dynamic than detyrosinated filaments in cells. The enzyme is bound at the interface of tubulin alpha- and beta-subunits and specifically recognizes the tubulin dimer's curved conformation
physiological function
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tubulin tyrosine ligase forms a stable complex with tubulin and inhibits tubulin polymerization, it competes in this function with stathmin
physiological function
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tubulin tyrosine ligase forms a stable complex with tubulin and inhibits tubulin polymerization, it competes in this function with stathmin
physiological function
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tubulin-tyrosine ligase TTL is required to increase the levels of tyrosinated alpha-tubulin at an axon injury site and plays an important role in injury signaling. Preventing the injury-induced increase in tyrosinated alpha-tubulin by knocking down TTL impairs retrograde organelle transport and delays activation of the pro-regenerative transcription factor c-Jun. In the absence of TTL, axon regeneration is reduced severely
