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Information on EC 6.3.2.61 - tubulin-glutamate ligase
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6.3.2.61 tubulin-glutamate ligaseIUBMB Comments
The eukaryotic tubulin proteins, which polymerize into microtubules, are highly modified by the addition of side-chains. The polyglutamylation reaction catalysed by this group of enzymes consists of two biochemically distinct steps: initiation and elongation. Initiation comprises the formation of an isopeptide bond with the gamma-carboxyl group of the glutamate acceptor site in a glutamate-rich C-terminal region of tubulin, whereas elongation consists of the addition of glutamate residues linked by regular peptide bonds to the gamma-linked residue. This entry describes enzymes that act on both alpha- and beta-tubulins.
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Word Map
- 6.3.2.61
- tubulins
-
polyglutamylation
- microtubule
-
cilia
-
axonemal
-
deglutamylation
- deglutamylase
- ccp1
-
cone-rod
-
polyglycylation
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
ttll5, ttll6, ttll4, ttll1, tubulin polyglutamylase, ttll9, ttll11, tubulin tyrosine ligase like, tubulin tyrosine ligase-like 1, tubulin-tyrosine ligase-like protein, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-tubulin-glutamate ligase
-
-
-
-
TTLL1
TTLL11
TTLL13
Ttll1p
TTLL5
ttll6
TTLL9
Ttll9p
tubulin polyglutamylase
tubulin polyglutamylase complex
-
comprised of a catalytic subunit, tubulin tyrosine ligase-like 1, and four additional subunits, tubulin polyglutamylase complex subunits 1 and 2, leucine rich repeat containing 49 and nicolin 1
additional information
-
tubulin glutamylases belong to the family of TTL domain-carrying proteins named TTLL proteins
TTLL1
-
-
ambiguous
-
TTLL5
-
-
ambiguous
-
ttll6
-
-
ambiguous
-
tubulin polyglutamylase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + [tubulin]-(alpha-L-glutamyl-gamma-L-glutamyl)-L-glutamate + n L-glutamate = [tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
(1c)
-
-
-
ATP + [tubulin]-(gamma-L-glutamyl)-L-glutamate + L-glutamate = [tubulin]-(alpha-L-glutamyl-gamma-L-glutamyl)-L-glutamate + ADP + phosphate
(1b)
-
-
-
ATP + [tubulin]-L-glutamate + L-glutamate = [tubulin]-(gamma-L-glutamyl)-L-glutamate + ADP + phosphate
n ATP + [tubulin]-L-glutamate + n L-glutamate = [tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
overall reaction
-
-
-
ATP + [tubulin]-L-glutamate + L-glutamate = [tubulin]-(gamma-L-glutamyl)-L-glutamate + ADP + phosphate
the enzymatic mechanism of microtubule glutamylation involves two distinct steps: initiation and elongation
-
ATP + [tubulin]-L-glutamate + L-glutamate = [tubulin]-(gamma-L-glutamyl)-L-glutamate + ADP + phosphate
(1a)
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
[tubulin]-L-glutamate:L-glutamate ligase (ADP-forming)
The eukaryotic tubulin proteins, which polymerize into microtubules, are highly modified by the addition of side-chains. The polyglutamylation reaction catalysed by this group of enzymes consists of two biochemically distinct steps: initiation and elongation. Initiation comprises the formation of an isopeptide bond with the gamma-carboxyl group of the glutamate acceptor site in a glutamate-rich C-terminal region of tubulin, whereas elongation consists of the addition of glutamate residues linked by regular peptide bonds to the gamma-linked residue. This entry describes enzymes that act on both alpha- and beta-tubulins.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + EB1 protein + L-glutamate
?
very low activity with isoform TTLL4
-
-
?
ATP + NPN2 protein + L-glutamate
?
high activity with isoform TTLL4
-
-
?
ATP + NPN3 protein + L-glutamate
?
very low activity with isoform TTLL4
-
-
?
ATP + [alpha-tubulin]-L-glutamate + L-glutamate
?
-
the enzyme catalyzes the MgATP-dependent addition of L-glutamate onto tubulin subunits. The enzyme is active with alpha- and beta-tubulin, respectively. Microtubules are much better substrates than unpolymerized tubulin, and the reaction is very specific for glutamate, other amino acids or glutamate analogues not being substrates. Moreover, glutamyl units are added sequentially onto tubulin, leading to progressive elongation of the polyglutamyl side chains. Side chains of one to six or seven glutamyl units are obtained with microtubules, whereas much longer side chains (up to 15-20 units) are formed with unpolymerized tubulin
-
-
?
ATP + [alpha/beta-tubulin]-(alpha-L-glutamyl-gamma-L-glutamyl)-L-glutamate + n L-glutamate
[alpha/beta-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
-
(1c)
-
-
?
ATP + [alpha/beta-tubulin]-(gamma-L-glutamyl)-L-glutamate + L-glutamate
[alpha/beta-tubulin]-(alpha-L-glutamyl-gamma-L-glutamyl)-L-glutamate + ADP + phosphate
-
(1b)
-
-
?
ATP + [alpha/beta-tubulin]-L-glutamate + L-glutamate
[alpha/beta-tubulin]-(gamma-L-glutamyl)-L-glutamate + ADP + phosphate
-
(1a)
-
-
?
ATP + [beta-tubulin]-L-glutamate + L-glutamate
?
-
the enzyme catalyzes the MgATP-dependent addition of L-glutamate onto tubulin subunits. The enzyme is active with alpha- and beta-tubulin, respectively. Microtubules are much better substrates than unpolymerized tubulin, and the reaction is very specific for glutamate, other amino acids or glutamate analogues not being substrates. Moreover, glutamyl units are added sequentially onto tubulin, leading to progressive elongation of the polyglutamyl side chains. Side chains of one to six or seven glutamyl units are obtained with microtubules, whereas much longer side chains (up to 15-20 units) are formed with unpolymerized tubulin
-
-
?
n ATP + [alpha-tubulin]-(alpha-L-glutamyl-gamma-L-glutamyl)-L-glutamate + n L-glutamate
[alpha-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
no initiating activity, high elongation activity. The enzyme modifies both alpha- and beta-tubulin and shows a preference towards alpha-tubulin
-
-
?
n ATP + [alpha-tubulin]-L-glutamate + n L-glutamate
[alpha-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
n ATP + [alpha/beta-tubulin]-L-glutamate + n L-glutamate
[alpha/beta-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
-
overall reaction. The enzyme incorporates glutamic acid preferentially into the more acidic variants of both alpha- and beta-tubulins
-
-
?
n ATP + [beta-tubulin]-(alpha-L-glutamyl-gamma-L-glutamyl)-L-glutamate + n L-glutamate
[beta-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
no initiating activity, high elongation activity. The enzyme modifies both alpha- and beta-tubulin and shows a preference towards alpha-tubulin
-
-
?
n ATP + [beta-tubulin]-L-glutamate + n L-glutamate
[beta-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
n ATP + [tubulin]-L-glutamate + n L-glutamate
[tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
ATP + acidic nuclear phosphoprotein 32 family, member A + L-glutamate
?
low activity with isoform TTLL5
-
-
?
ATP + acidic nuclear phosphoprotein 32 family, member A + L-glutamate
?
very low activity with isoform TTLL4
-
-
?
ATP + acidic nuclear phosphoprotein 32 family, member B + L-glutamate
?
high activity with isoform TTLL4
-
-
?
ATP + acidic nuclear phosphoprotein 32 family, member B + L-glutamate
?
low activity with isoform TTLL5
-
-
?
ATP + alpha tubulin + L-glutamate
?
Ttll1p glutamylase preferentially modifies alpha-tubulin. It shows a chain-initiating activity
-
-
?
ATP + alpha tubulin + L-glutamate
?
Ttll9p glutamylase preferentially modifies alpha-tubulin. It has primarily a chain-elongating activity
-
-
?
ATP + alpha tubulin + L-glutamate
?
-
Ttll9p glutamylase preferentially modifies alpha-tubulin. It has primarily a chain-elongating activity
-
-
?
ATP + alpha tubulin + L-glutamate
?
-
Ttll1p glutamylase preferentially modifies alpha-tubulin. It shows a chain-initiating activity
-
-
?
ATP + alpha-tubulin + L-glutamate
L-glutamyl-alpha-tubulin + ADP + phosphate
-
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
-
-
?
ATP + alpha-tubulin + L-glutamate
L-glutamyl-alpha-tubulin + ADP + phosphate
-
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
-
-
?
ATP + B23 nucleophosmin + L-glutamate
?
highest activity with isoform TTLL4
-
-
?
ATP + B23 nucleophosmin + L-glutamate
?
low activity with isoform TTLL5
-
-
?
ATP + microtubule + L-glutamate
?
highest activity with isoform TTLL5
-
-
?
ATP + NF45 protein + L-glutamate
?
low activity with isoform TTLL5
-
-
?
ATP + NF45 protein + L-glutamate
?
very low activity with isoform TTLL4
-
-
?
ATP + nucleosome assembly protein 1-like 1 + L-glutamate
?
-
-
-
?
ATP + nucleosome assembly protein 1-like 1 + L-glutamate
?
low activity with isoform TTLL5
-
-
?
ATP + nucleosome assembly protein 1-like 4 + L-glutamate
?
-
-
-
?
ATP + nucleosome assembly protein 1-like 4 + L-glutamate
?
high activity with isoform TTLL4
-
-
?
ATP + protein SET + L-glutamate
?
high activity with isoform TTLL5
-
-
?
ATP + protein SET + L-glutamate
?
very low activity with isoform TTLL4
-
-
?
n ATP + [alpha-tubulin]-L-glutamate + n L-glutamate
[alpha-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
-
overall reaction
-
-
?
n ATP + [alpha-tubulin]-L-glutamate + n L-glutamate
[alpha-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
high initiating activity, low elongation activity. High activity with alpha-tubulin, low activity with beta-tubulin. Upon overexpression in HeLa cells, TTLL5 modifies mostly alpha-tubulin
-
-
?
n ATP + [alpha-tubulin]-L-glutamate + n L-glutamate
[alpha-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
low initiating activity, high elongation activity. High activity with alpha-tubulin, low activity with beta-tubulin. Upon overexpression in HeLa cells, TTLL5 modifies mostly alpha-tubulin
-
-
?
n ATP + [alpha-tubulin]-L-glutamate + n L-glutamate
[alpha-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
low initiating activity, high elongation activity. The enzyme modifies both alpha- and beta-tubulin and shows a preference towards alpha-tubulin
-
-
?
n ATP + [alpha-tubulin]-L-glutamate + n L-glutamate
[alpha-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
-
overall reaction, higher activity compared to beta-tubulin
-
-
?
n ATP + [alpha-tubulin]-L-glutamate + n L-glutamate
[alpha-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
overall reaction, the enzyme modifies mostly alpha-tubulin
-
-
?
n ATP + [beta-tubulin]-L-glutamate + n L-glutamate
[beta-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
-
overall reaction
-
-
?
n ATP + [beta-tubulin]-L-glutamate + n L-glutamate
[beta-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
overall reaction
-
-
?
n ATP + [beta-tubulin]-L-glutamate + n L-glutamate
[beta-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
high initiating activity, low elongation activity. High activity with alpha-tubulin, low activity with beta-tubulin
-
-
?
n ATP + [beta-tubulin]-L-glutamate + n L-glutamate
[beta-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
low initiating activity, high elongation activity. High activity with alpha-tubulin, low activity with beta-tubulin
-
-
?
n ATP + [beta-tubulin]-L-glutamate + n L-glutamate
[beta-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
low initiating activity, high elongation activity. The enzyme modifies both alpha- and beta-tubulin and shows a preference towards alpha-tubulin
-
-
?
n ATP + [tubulin]-L-glutamate + n L-glutamate
[tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
-
overall reaction, up to 70 mol of L-glutamate is incorporated per alphabeta-heterodimer
-
-
?
n ATP + [tubulin]-L-glutamate + n L-glutamate
[tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
-
overall reaction, the enzyme initiates microtubule glutamylation specifically on alpha-tubulin
-
-
?
n ATP + [tubulin]-L-glutamate + n L-glutamate
[tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
overall reaction
-
-
?
n ATP + [tubulin]-L-glutamate + n L-glutamate
[tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
-
overall reaction, the enzyme has an initiating activity with a preference for alpha-tubulin, but also shows partial activity on beta-tubulin
-
-
?
additional information
?
-
-
the flagella-associated protein FAP234 functions in stabilization and intraflagellar transport-dependent transport of enzyme form TTLL9 by forming a complex with TTLL9 in the axoneme and cytoplasm
-
-
-
additional information
?
-
-
the flagella-associated protein FAP234 functions in stabilization and intraflagellar transport-dependent transport of enzyme form TTLL9 by forming a complex with TTLL9 in the axoneme and cytoplasm
-
-
-
additional information
?
-
-
synthetic peptides related to the carboxyterminal end of brain alpha- and beta-tubulin are subject to polyglutamylation if they display a free alpha-carboxylate group of a glutamic acid residue
-
-
-
additional information
?
-
-
synthetic peptides with an oligoglutamyl side chain, corresponding to the carboxyterminal end of brain alpha- and beta-tubulins, are accepted by the enzyme, albeit at low efficiency. The enzyme elongates the side chain by up to 3 and 5 residues, respectively. The presence of D-Glu, L-Tyr, Gly, L-Asp in 10-100fold excess over L-Glu do not affect the glutamylation activity. While mammalian brain tubulin is effectively polyglutamylated by the Crithidia enzyme, tubulin from HeLa cells is a poorer substrate
-
-
-
additional information
?
-
EB3 protein and HMG-B1 are no substrates for isoform TTLL4
-
-
-
additional information
?
-
EB3 protein and HMG-B1 are no substrates for isoform TTLL4
-
-
-
additional information
?
-
TTLL1 is an alpha-tubulin preferring polyglutamylase. TTLL1 is solely active as part of a multiprotein complex, that can potentially contain exchangeable regulatory subunits
-
-
?
additional information
?
-
TTLL1 is an alpha-tubulin preferring polyglutamylase. TTLL1 is solely active as part of a multiprotein complex, that can potentially contain exchangeable regulatory subunits
-
-
?
additional information
?
-
TTLL1 is an alpha-tubulin preferring polyglutamylase. TTLL1 is solely active as part of a multiprotein complex, that can potentially contain exchangeable regulatory subunits
-
-
?
additional information
?
-
TTLL1 is an alpha-tubulin preferring polyglutamylase. TTLL1 is solely active as part of a multiprotein complex, that can potentially contain exchangeable regulatory subunits
-
-
?
additional information
?
-
TTLL1 is an alpha-tubulin preferring polyglutamylase. TTLL1 is solely active as part of a multiprotein complex, that can potentially contain exchangeable regulatory subunits
-
-
?
additional information
?
-
-
microtubules are much better substrates than unpolymerized tubulin, and the reaction is very specific for L-glutamate, other amino acids (D-Glu, L-Asp, L-Gln, L-Asn, L-Ser, L-Lys, L-Leu, and L-Gly) or glutamate analogues (RGlu-Glu, çGlu-Glu, Iso-Gln, N-acetyl-Glu, norvaline, GABA, and Gla) not being substrates. Moreover, glutamyl units are added sequentially onto tubulin, leading to progressive elongation of the polyglutamyl side chains. Side chains of 1-6 or 7 glutamyl units are obtained with microtubules, whereas much longer side chains (up to 15-20 units) are formed with unpolymerized tubulin
-
-
-
additional information
?
-
-
the enzyme is able to glutamylate both alpha- and beta-tubulin from mouse brain but only alpha-tubulin from HeLa cells
-
-
-
additional information
?
-
-
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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + alpha-tubulin + L-glutamate
L-glutamyl-alpha-tubulin + ADP + phosphate
-
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
-
-
?
ATP + [alpha/beta-tubulin]-(alpha-L-glutamyl-gamma-L-glutamyl)-L-glutamate + n L-glutamate
[alpha/beta-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
-
(1c)
-
-
?
ATP + [alpha/beta-tubulin]-(gamma-L-glutamyl)-L-glutamate + L-glutamate
[alpha/beta-tubulin]-(alpha-L-glutamyl-gamma-L-glutamyl)-L-glutamate + ADP + phosphate
-
(1b)
-
-
?
ATP + [alpha/beta-tubulin]-L-glutamate + L-glutamate
[alpha/beta-tubulin]-(gamma-L-glutamyl)-L-glutamate + ADP + phosphate
-
(1a)
-
-
?
n ATP + [alpha-tubulin]-L-glutamate + n L-glutamate
[alpha-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
n ATP + [alpha/beta-tubulin]-L-glutamate + n L-glutamate
[alpha/beta-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
-
overall reaction. The enzyme incorporates glutamic acid preferentially into the more acidic variants of both alpha- and beta-tubulins
-
-
?
n ATP + [beta-tubulin]-L-glutamate + n L-glutamate
[beta-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
n ATP + [tubulin]-L-glutamate + n L-glutamate
[tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
additional information
?
-
-
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
-
-
?
n ATP + [alpha-tubulin]-L-glutamate + n L-glutamate
[alpha-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
-
overall reaction
-
-
?
n ATP + [alpha-tubulin]-L-glutamate + n L-glutamate
[alpha-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
-
overall reaction, higher activity compared to beta-tubulin
-
-
?
n ATP + [alpha-tubulin]-L-glutamate + n L-glutamate
[alpha-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
overall reaction, the enzyme modifies mostly alpha-tubulin
-
-
?
n ATP + [beta-tubulin]-L-glutamate + n L-glutamate
[beta-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
-
overall reaction
-
-
?
n ATP + [beta-tubulin]-L-glutamate + n L-glutamate
[beta-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
overall reaction
-
-
?
n ATP + [tubulin]-L-glutamate + n L-glutamate
[tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
-
overall reaction, up to 70 mol of L-glutamate is incorporated per alphabeta-heterodimer
-
-
?
n ATP + [tubulin]-L-glutamate + n L-glutamate
[tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
-
overall reaction, the enzyme initiates microtubule glutamylation specifically on alpha-tubulin
-
-
?
n ATP + [tubulin]-L-glutamate + n L-glutamate
[tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
overall reaction
-
-
?
n ATP + [tubulin]-L-glutamate + n L-glutamate
[tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
-
overall reaction, the enzyme has an initiating activity with a preference for alpha-tubulin, but also shows partial activity on beta-tubulin
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
optimal concentration of 1-2 mM, cannot be replaced by GTP or ATP-gamma-S
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
-
required, 8 mM used in assay conditions. The activity increases markedly with Mg2+ concentrations between 1 and 6 mM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KCl
-
5-10 mM, strong inhibitory effect on the glutamylation reaction. 80 mM, 90% inhibition; strong inhibitory effect
NaCl
-
5-10 mM, strong inhibitory effect on the glutamylation reaction. 40 mM NaCl, 50% inhibition; strong inhibitory effect
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glycerol
-
20% (v/v) leads to 10-15% increase in glutamylation activity
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
beta-tubulin-glutamate ligase deficiency
Glutamylation of deubiquitinase BAP1 controls self-renewal of hematopoietic stem cells and hematopoiesis.
Breast Neoplasms
Tubulin Tyrosine Ligase Like 4 (TTLL4) overexpression in breast cancer cells is associated with brain metastasis and alters exosome biogenesis.
Carcinogenesis
Involvement of the Tubulin Tyrosine Ligase-Like Family Member 4 Polyglutamylase in PELP1 Polyglutamylation and Chromatin Remodeling in Pancreatic Cancer Cells.
Carcinoma
Effect of TTLL6 expression on CDDP sensitivity of EC109/CDDP cells in hypoxia/acidosis microenvironment.
Cholera
Impaired mucociliary motility enhances antigen-specific nasal IgA immune responses to a cholera toxin-based nasal vaccine.
Cone Dystrophy
Novel splice-site mutation in TTLL5 causes cone dystrophy in a consanguineous family.
Cone Dystrophy
Novel TTLL5 Variants Associated with Cone-Rod Dystrophy and Early-Onset Severe Retinal Dystrophy.
Cone-Rod Dystrophies
Mutations in the polyglutamylase gene TTLL5, expressed in photoreceptor cells and spermatozoa, are associated with cone-rod degeneration and reduced male fertility.
Cone-Rod Dystrophies
Novel TTLL5 Variants Associated with Cone-Rod Dystrophy and Early-Onset Severe Retinal Dystrophy.
Hydrocephalus
Tubulin Tyrosine Ligase-Like 1 Deficiency Results in Chronic Rhinosinusitis and Abnormal Development of Spermatid Flagella in Mice.
Infertility
Mutations in the polyglutamylase gene TTLL5, expressed in photoreceptor cells and spermatozoa, are associated with cone-rod degeneration and reduced male fertility.
Infertility, Male
Tubulin Tyrosine Ligase-Like 1 Deficiency Results in Chronic Rhinosinusitis and Abnormal Development of Spermatid Flagella in Mice.
Neoplasm Metastasis
Tubulin Tyrosine Ligase Like 4 (TTLL4) overexpression in breast cancer cells is associated with brain metastasis and alters exosome biogenesis.
Neoplasms
Effect of TTLL6 expression on CDDP sensitivity of EC109/CDDP cells in hypoxia/acidosis microenvironment.
Neoplasms
Whole-exome sequencing combined with functional genomics reveals novel candidate driver cancer genes in endometrial cancer.
Neuroblastoma
Acquired genetic alterations in tumor cells dictate the development of high-risk neuroblastoma and clinical outcomes.
Otitis Media
Tubulin Tyrosine Ligase-Like 1 Deficiency Results in Chronic Rhinosinusitis and Abnormal Development of Spermatid Flagella in Mice.
Pancreatic Neoplasms
Involvement of the Tubulin Tyrosine Ligase-Like Family Member 4 Polyglutamylase in PELP1 Polyglutamylation and Chromatin Remodeling in Pancreatic Cancer Cells.
Prostatic Neoplasms
Tubulin tyrosine ligase like 12, link to prostate cancer through tubulin post-translational modification and chromosome ploidy.
Retinal Dystrophies
Biallelic variants in TTLL5, encoding a tubulin glutamylase, cause retinal dystrophy.
Retinal Dystrophies
Loss of RPGR glutamylation underlies the pathogenic mechanism of retinal dystrophy caused by TTLL5 mutations.
Retinal Dystrophies
Novel TTLL5 Variants Associated with Cone-Rod Dystrophy and Early-Onset Severe Retinal Dystrophy.
Scoliosis
Genetic variant of TTLL11 gene and subsequent ciliary defects are associated with idiopathic scoliosis in a 5-generation UK family.
Spastic Paraplegia, Hereditary
Tau missorting and spastin-induced microtubule disruption in neurodegeneration: Alzheimer Disease and Hereditary Spastic Paraplegia.
Tauopathies
Tau missorting and spastin-induced microtubule disruption in neurodegeneration: Alzheimer Disease and Hereditary Spastic Paraplegia.
tubulin-glutamate ligase deficiency
Ttll9-/- mice sperm flagella show shortening of doublet 7, reduction of doublet 5 polyglutamylation and a stall in beating.
tubulin-glutamate ligase deficiency
Tubulin glutamylation regulates ciliary motility by altering inner dynein arm activity.
tubulin-glutamate ligase deficiency
Tubulin Tyrosine Ligase-Like 1 Deficiency Results in Chronic Rhinosinusitis and Abnormal Development of Spermatid Flagella in Mice.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0003
[alpha/beta-tubulin]-L-glutamate
-
at pH 9.0, temperature not specified in the publication
-
0.8
L-glutamate
-
at pH 9.0, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the high pH optimum observed at low glutamate concentrations is a result of the free amine of glutamate (pK = 9.7 at 25°C) being the substrate for the reaction
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8 - 8.9
-
the enzyme activity increases markedly with the pH going from 6.8 to 8.3, with a large optimum between 8.3 and 8.9, and then decreases sharply. At physiological pH, the activity is 15% of the maximal level
7.5 - 9.2
-
pH 7.5: about 45% of maximal activity, pH 9.2: about 80% of maximal activity. When the glutamate concentration is raised to 6 mM, the activity is less dependent on pH, decreasing by only 40% between pH 8.7 and 6.8
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
TTLL5 localizes to both basal bodies and cilia
brenda
TTLL6 localizes to both basal bodies and cilia
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Ttll1p localizes primarily to the basal bodies of oral and somatic cilia
-
brenda
-
Ttll1p localizes primarily to the basal bodies of oral and somatic cilia
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
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
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
malfunction
knockdown of ttll6 strongly reduces cilia tubulin glutamylation but only partially affects cilia structure and motility. Combined loss of function of ttll3 and ttll6 causes near complete loss of cilia motility and induced a variety of axonemal ultrastructural defects
malfunction
-
along with the loss of axonemal curvature, the axonemes and tracheal epithelial cilia from enzyme knockout mice lose beating asymmetry which results in a reduction of cilia-generated fluid flow in trachea from the knockout mice. The mice display a significant accumulation of mucus in the nasal cavity, and also emit frequent coughing- or sneezing-like noises
malfunction
-
deletion of isoform TTLL1 prevents degeneration of Purkinje cells and of myelinated axons in peripheral nerves ine mice lacking the deglutamylase CCP1. Moreover, loss of TTLL1 leads to increased mitochondria motility in neurons
malfunction
-
isoform TTLL5 mutant flies are viable without any defect in vesicular axonal transport, synapse morphology and larval locomotion. Moreover, isoform TTLL5 mutant flies display normal negative geotaxis behavior and their lifespan is not altered
malfunction
-
loss of the tubulin polyglutamylase complex leads to aberrant, enhanced assembly of microtubules that penetrate the nucleus, which in turn leads to defects in nuclear shape, and disorganization of cytoplasmic actin that disrupts the YAP/TAZ pathway and cilium disassembly
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
-
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
-
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
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
physiological function
-
the enzyme catalyzes the posttranslational formation of polyglutamyl side chains onto alpha- and beta-tubulin. The length of the polyglutamyl side chain regulates the interaction between tubulin and various microtubule-associated proteins
physiological function
-
enzyme-mediated ubulin polyglutamylation is essential for airway ciliary function through the regulation of beating asymmetry
physiological function
-
enzyme-meditated glutamylation of tubulin directly stimulates spastin-mediated severing of microtubules
physiological function
-
isoform TLL1 catalyses the excessive hyperglutamylation found in mice lacking the deglutamylase CCP1
physiological function
-
isoform TTLL5 is the major enzyme responsible for initiating neuronal mictotubule glutamylation specifically on alpha-tubulin
physiological function
-
the enzyme plays mechanistically distinct roles in the regulation of nuclear shape and cilium disassembly
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
-
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
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). I7MCG4_TETTS
Tetrahymena thermophila (strain SB210)
648
0
75425
TrEMBL
Chloroplast (Reliability: 2)
TTLL1_TETTS
Tetrahymena thermophila (strain SB210)
413
0
48267
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
360000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
TTLL6_N705 is a stable and enzymatically active truncated protein version. Unlike the full-length enzyme TTLL6, the truncated protein does not localize to cilia
additional information
TTLL6_N705 is a stable and enzymatically active truncated protein version. Unlike the full-length enzyme TTLL6, the truncated protein does not localize to cilia
additional information
TTLL6_N705 is a stable and enzymatically active truncated protein version. Unlike the full-length enzyme TTLL6, the truncated protein does not localize to cilia
additional information
TTLL6_N705 is a stable and enzymatically active truncated protein version. Unlike the full-length enzyme TTLL6, the truncated protein does not localize to cilia
additional information
TTLL6_N705 is a stable and enzymatically active truncated protein version. Unlike the full-length enzyme TTLL6, the truncated protein does not localize to cilia
additional information
-
disruption of the TTLL1 and TTLL9 genes decrease 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, phenotype, overview
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.7
-
1 h, 50% loss of activity at 20°C and 75% at 30°C. At 30°C, the loss is reduced to 40% in the presence of 0.1 mg/ml microtubules
749873
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
-
pH 8.7, 1 h, 50% loss of activity. Not significant loss of activity within 3 h of incubation at pH 6.8
30
-
pH 8.7, 1 h, 75% loss of activity. No significant loss of activity within 3 h of incubation at pH 6.8
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
at 30°C, the loss of activity is reduced to 40% in the presence of 0.1 mg/ml microtubules, while neither bovine serum albumin nor the other substrates, ATP or glutamate, have any protecting effect
-
C11ORF49/CSTPP1 regulates the assembly and stability of the enzyme complex and thereby modulates polyglutamylation of microtubule, which antagonizes MAP4 binding
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, in the presence of 10% (v/v) glycerol, several months, no loss of activity
-
20°C, in 10 mM Tris (pH 8.7), 1 mM EGTA, 1 mM MgCl2, 1 mM dithiothreitol, and 0.01% TX-100 at pH 8.7, 1 h, 50% loss of activity
-
30°C, in 10 mM Tris (pH 8.7), 1 mM EGTA, 1 mM MgCl2, 1 mM dithiothreitol, and 0.01% TX-100 at pH 8.7, 1 h, 75% loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ATP-affinity chromatography, glycerol-gradient centrifugation and Mono Q ion-exchange chromatography
-
partial purification of recombinant GFP-tagged Ttll1p and GFP-tagged Ttll9p
-
phosphocellulose column chromatography, MgCl2 and sodium citrate precipitation, sucrose gradient sedimentation, and TSK G3000 gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of GFP-tagged Ttll1p mainly in the basal bodies and of GFP-tagged Ttll9p mainly in the cilia of CU428 and B2086 cells
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme activity is maximal in G2-phase and decreases during M-phase of the cell cycle
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Eukaryot. Cell
7
1362-1372
2008
Tetrahymena thermophila
brenda
Regnard, C.; Audebert, S.; Desbruyeres, E.; Denoulet, P.; Edde, B.
Tubulin polyglutamylase partial purification and enzymatic properties
Biochemistry
37
8395-8404
1998
Mus musculus
brenda
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
Eukaryot. Cell
7
1362-1372
2008
Tetrahymena thermophila (I7MCG4), Tetrahymena thermophila (Q23SI8)
-
brenda
Pathak, N.; Austin, C.A.; Drummond, I.A.
Tubulin tyrosine ligase-like genes ttll3 and ttll6 maintain zebrafish cilia structure and motility
J. Biol. Chem.
286
11685-11695
2011
Danio rerio (A8CVX7), Danio rerio
brenda
van Dijk, J.; Rogowski, K.; Miro, J.; Lacroix, B.; Edde, B.; Janke, C.
A targeted multienzyme mechanism for selective microtubule polyglutamylation
Mol. Cell
26
437-448
2007
Mus musculus (A4Q9E8), Mus musculus (A4Q9F4), Mus musculus (A4Q9F6), Mus musculus (Q8CHB8), Mus musculus (Q91V51)
brenda
Wang, L.; Paudyal, S.; Kang, Y.; Owa, M.; Liang, F.; Spektor, A.; Knaut, H.; Sanchez, I.; Dynlacht, B.
Regulators of tubulin polyglutamylation control nuclear shape and cilium disassembly by balancing microtubule and actin assembly
Cell Res.
32
190-209
2022
Homo sapiens
brenda
Bodakuntla, S.; Yuan, X.; Genova, M.; Gadadhar, S.; Leboucher, S.; Birling, M.C.; Klein, D.; Martini, R.; Janke, C.; Magiera, M.M.
Distinct roles of alpha- and beta-tubulin polyglutamylation in controlling axonal transport and in neurodegeneration
EMBO J.
40
e108498
2021
Mus musculus
brenda
Westermann, S.; Plessmann, U.; Weber, K.
Synthetic peptides identify the minimal substrate requirements of tubulin polyglutamylase in side chain elongation
FEBS Lett.
459
90-94
1999
Crithidia fasciculata
brenda
Van Dijk, J.; Miro, J.; Strub, J.; Lacroix, B.; Van Dorsselaer, A.; Edde, B.; Janke, C.
Polyglutamylation is a post-translational modification with a broad range of substrates
J. Biol. Chem.
283
3915-3922
2008
Homo sapiens (Q14679), Homo sapiens (Q6EMB2)
brenda
Lacroix, B.; Van Dijk, J.; Gold, N.; Guizetti, J.; Aldrian-Herrada, G.; Rogowski, K.; Gerlich, D.; Janke, C.
Tubulin polyglutamylation stimulates spastin-mediated microtubule severing
J. Cell Biol.
189
945-954
2010
Mus musculus
brenda
Regnard, C.; Desbruyeres, E.; Denoulet, P.; Edde, B.
Tubulin polyglutamylase isozymic variants and regulation during the cell cycle in HeLa cells
J. Cell Sci.
112 (Pt 23)
4281-4289
1999
Mus musculus
brenda
Westermann, S.; Schneider, A.; Horn, E.K.; Weber, K.
Isolation of tubulin polyglutamylase from Crithidia; binding to microtubules and tubulin, and glutamylation of mammalian brain alpha- and beta-tubulins
J. Cell Sci.
112
2185-2193
1999
Crithidia fasciculata
brenda
Regnard, C.; Fesquet, D.; Janke, C.; Boucher, D.; Desbruyeres, E.; Koulakoff, A.; Insina, C.; Travo, P.; Edde, B.
Characterisation of PGs1, a subunit of a protein complex co-purifying with tubulin polyglutamylase
J. Cell Sci.
116
4181-4190
2003
Mus musculus
brenda
Kubo, T.; Yanagisawa, H.A.; Liu, Z.; Shibuya, R.; Hirono, M.; Kamiya, R.
A conserved flagella-associated protein in Chlamydomonas, FAP234, is essential for axonemal localization of tubulin polyglutamylase TTLL9
Mol. Biol. Cell
25
107-117
2014
Chlamydomonas reinhardtii, Chlamydomonas reinhardtii CC-124
brenda
van Dijk, J.; Rogowski, K.; Miro, J.; Lacroix, B.; Edde, B.; Janke, C.
A targeted multienzyme mechanism for selective microtubule polyglutamylation
Mol. Cell.
26
437-448
2007
Mus musculus (A4Q9E8), Mus musculus (A4Q9F4), Mus musculus (A4Q9F6), Mus musculus (Q8CHB8), Mus musculus (Q91V51)
brenda
Ikegami, K.; Sato, S.; Nakamura, K.; Ostrowski, L.; Setou, M.
Tubulin polyglutamylation is essential for airway ciliary function through the regulation of beating asymmetry
Proc. Natl. Acad. Sci. USA
107
10490-10495
2010
Mus musculus
brenda
Devambez, I.; van Dijk, J.; Benlefki, S.; Layalle, S.; Grau, Y.; Rogowski, K.; Parmentier, M.L.; Soustelle, L.
Identification of DmTTLL5 as a major tubulin glutamylase in the Drosophila nervous system
Sci. Rep.
7
16254
2017
Drosophila melanogaster
brenda
Janke, C.; Rogowski, K.; Wloga, D.; Regnard, C.; Kajava, A.V.; Strub, J.M.; Temurak, N.; van Dijk, J.; Boucher, D.; van Dorsselaer, A.; Suryavanshi, S.; Gaertig, J.; Edde, B.
Tubulin polyglutamylase enzymes are members of the TTL domain protein family
Science
308
1758-1762
2005
Mus musculus
brenda
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