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ATP + alpha-tubulin + L-glutamate
L-glutamyl-alpha-tubulin + ADP + phosphate
-
-
-
?
ATP + [alpha-tubulin]-L-glutamate + L-glutamate
[alpha-tubulin]-(gamma-L-glutamyl)-L-glutamate + ADP + phosphate
high initiating activity, no elongation activity. The enzyme modifies both alpha- and beta-tubulin and shows a preference towards beta-tubulin
-
-
?
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
(1c)
-
-
?
ATP + [beta-tubulin]-(gamma-L-glutamyl)-L-glutamate + L-glutamate
[beta-tubulin]-(alpha-L-glutamyl-gamma-L-glutamyl)-L-glutamate + ADP + phosphate
(1b)
-
-
?
ATP + [beta-tubulin]-L-glutamate + L-glutamate
[beta-tubulin]-(gamma-L-glutamyl)-L-glutamate + ADP + phosphate
ATP + [beta-tubulin]-L-glutamate + L-glutamate
[tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + ADP + phosphate
the enzyme performs both initiation and elongation in the polyglutamylation reaction on beta-tubulin through a random sequential pathway
-
-
?
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 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
high initiating activity, low elongation activity. The enzyme modifies both alpha- and beta-tubulin and shows a preference towards beta-tubulin
-
-
?
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 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
additional information
?
-
-
the enzyme does not glutamylate alpha-tubulin
-
-
-
ATP + [beta-tubulin]-L-glutamate + L-glutamate
[beta-tubulin]-(gamma-L-glutamyl)-L-glutamate + ADP + phosphate
(1a)
-
-
?
ATP + [beta-tubulin]-L-glutamate + L-glutamate
[beta-tubulin]-(gamma-L-glutamyl)-L-glutamate + ADP + phosphate
high initiating activity, no elongation activity. The enzyme modifies both alpha- and beta-tubulin and shows a preference towards 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
-
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
overall reaction. There are two main glutamylation sites in beta-tubulin: E434 and E441. E442 and E443 are also modified, but with much lower frequency
-
-
?
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
the enzyme is required for the growth of MAP2-positive neurites in PC12 cells
-
-
?
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. The enzyme modifies both alpha- and beta-tubulin and shows a preference towards 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
the enzyyme catalyzes tubulin polyglutamylation with high preference to beta-tubulin in vitro. When expressed in HEK293T cells, TTLL7 demonstrates specificity for beta-tubulin and not for alpha-tubulin or nucleosome assembly protein 1
-
-
?
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, the enzyme prefers 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
overall reaction. The enzyme shows specificity for 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
the whole activity to microtubules is about 2.5fold higher than that to unpolymerized tubulin. When microtubules are used as substrates, recombinant enzyme exhibits activity highly preferential to beta-tubulin. The substrate preference drastically decreases when unpolymerized tubulin dimers are used as substrates
-
-
?
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. The enzyme shows specificity for 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
-
overall reaction. Ttll6Ap is a beta-tubulin-preferring polyglutamylase
-
-
?
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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
(1c)
-
-
?
ATP + [beta-tubulin]-(gamma-L-glutamyl)-L-glutamate + L-glutamate
[beta-tubulin]-(alpha-L-glutamyl-gamma-L-glutamyl)-L-glutamate + ADP + phosphate
(1b)
-
-
?
ATP + [beta-tubulin]-L-glutamate + L-glutamate
[beta-tubulin]-(gamma-L-glutamyl)-L-glutamate + ADP + phosphate
(1a)
-
-
?
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 + [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
-
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
the enzyme is required for the growth of MAP2-positive neurites in PC12 cells
-
-
?
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, the enzyme prefers 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
overall reaction. The enzyme shows specificity for 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
the whole activity to microtubules is about 2.5fold higher than that to unpolymerized tubulin. When microtubules are used as substrates, recombinant enzyme exhibits activity highly preferential to beta-tubulin. The substrate preference drastically decreases when unpolymerized tubulin dimers are used as substrates
-
-
?
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. The enzyme shows specificity for 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
-
overall reaction. Ttll6Ap is a beta-tubulin-preferring polyglutamylase
-
-
?
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Adenylyl imidodiphosphate
pH 7.0, 30°C, at a 600fold higher concentration compared with the ATP concentration, almost completely inhibits the enzyme. Competitive inhibition for ATP. Noncompetitive inhibitor for glutamate and tubulin
ADP
about 98% inhibition at 30 mM; pH 7.0, 30°C, at a 600fold higher concentration compared with the ATP concentration, almost completely inhibits the enzyme
AMP
about 98% inhibition at 30 mM; pH 7.0, 30°C, at a 600fold higher concentration compared with the ATP concentration, almost completely inhibits the enzyme
AMP-PNP
about 98% inhibition at 30 mM, competitive inhibitor for ATP, noncompetitive inhibitorn for glutamate and tubulin
ATAEEEGEMYEDDDEESEAQGPK
about 80% inhibition at 10 mM
-
C-terminal peptide of class III-tubulin
competitive inhibitor for tubulin. Noncompetitive inhibition against glutamate and ATP
-
DATAEEGEFEEEAEEEVA L
about 70% inhibition at 10 mM
-
gamma-L-glutamyl-L-cysteine
about 58% inhibition at 10 mM
gamma-L-glutamyl-L-glutamate
pH 7.0, 30°C, competitive inhibitor for glutamate. Noncompetitive inhibitor for ATP and tubulin
gamma-L-glutamyl-L-leucine
about 60% inhibition at 10 mM
-
gammaGlu-Glu
80% inhibition at 10 mM, noncompetitive inhibitor for ATP and tubulin
-
Gly
less than 10% inhibition at 10 mM
L-Asp
about 35% inhibition at 10 mM
L-Gln
about 50% inhibition at 10 mM
L-His
about 40% inhibition at 10 mM
L-Leu
about 15% inhibition at 10 mM
L-Tyr
about 10% inhibition at 10 mM
NaCl
the polyglutamylase activity of the recombinant enzyme is inhibited by NaCl in proportion to the concentrations of NaCl: 100 mM NaCl suppresses the enzyme activity at 40%, and 200 mM NaCl suppressed it at 90%
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0.0128 - 20.2
L-glutamate
0.0125 - 21.8
[beta-tubulin]-L-glutamate
0.0133
ATP
at pH 7.0 and 30°C
7.5
ATP
pH 7.0, 30°C, enzyme from adult brain, 0.006 mM L-glutamate
16
ATP
pH 7.0, 30°C, enzyme from newborn brain, 0.05 mM L-glutamate
19.1
ATP
pH 7.0, 30°C, enzyme from adult brain, 0.017 mM tubulin
26.5
ATP
pH 7.0, 30°C, enzyme from newborn brain, 0.017 mM tubulin
0.0128
L-glutamate
at pH 7.0 and 30°C
4.4
L-glutamate
pH 7.0, 30°C, enzyme from newborn brain, 0.05 mM ATP
5.4
L-glutamate
pH 7.0, 30°C, enzyme from adult brain, 0.05 mM ATP
19.6
L-glutamate
pH 7.0, 30°C, enzyme from newborn brain, 0.017 mM tubulin
20.2
L-glutamate
pH 7.0, 30°C, enzyme from adult brain, 0.017 mM tubulin
0.0125
[beta-tubulin]-L-glutamate
at pH 7.0 and 30°C
3.1
[beta-tubulin]-L-glutamate
pH 7.0, 30°C, enzyme from adult brain, 0.006 mM L-glutamate
6.7
[beta-tubulin]-L-glutamate
pH 7.0, 30°C, enzyme from newborn brain, 0.05 mM L-glutamate
15.8
[beta-tubulin]-L-glutamate
pH 7.0, 30°C, enzyme from newborn brain, 0.05 mM ATP
21.8
[beta-tubulin]-L-glutamate
pH 7.0, 30°C, enzyme from adult brain, 0.05 mM ATP
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Schumacher, D.; Helma, J.; Mann, F.A.; Pichler, G.; Natale, F.; Krause, E.; Cardoso, M.C.; Hackenberger, C.P.; Leonhardt, H.
Versatile and efficient site-specific protein functionalization by tubulin tyrosine ligase
Angew. Chem. Int. Ed. Engl.
54
13787-13791
2015
Homo sapiens (Q6ZT98)
brenda
Mukai, M.; Ikegami, K.; Sugiura, Y.; Takeshita, K.; Nakagawa, A.
Mitsutoshi Setou Recombinant mammalian tubulin polyglutamylase TTLL7 performs both initiation and elongation of polyglutamylation on - tubulin through a random sequential pathway
Biochemistry
48
1084-1093
2009
Mus musculus, Mus musculus (A4Q9F0)
brenda
Ikegami, K.; Mukai, M.; Tsuchida, J.; Heier, R.L.; Macgregor, G.R.; Setou, M.
TTLL7 is a mammalian beta-tubulin polyglutamylase required for growth of MAP2-positive neurites
J. Biol. Chem.
281
30707-30716
2006
Mus musculus, Mus musculus (A4Q9F0), Rattus norvegicus
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 (A4Q9F0), Mus musculus (Q80UG8), Tetrahymena thermophila (Q23MT7)
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
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
4281-4289
1999
Homo sapiens
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
brenda
Garnham, C.P.; Yu, I.; Li, Y.; Roll-Mecak, A.
Crystal structure of tubulin tyrosine ligase-like 3 reveals essential architectural elements unique to tubulin monoglycylases
Proc. Natl. Acad. Sci. USA
114
6545-6550
2017
Homo sapiens (Q6ZT98)
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
Tetrahymena thermophila
brenda