BRENDA - Enzyme Database show
show all sequences of 6.3.2.25

Tubulin tyrosination in Crithidia: modifying enzymes and modification states of tubulin

Chang, S.; Flavin, M.; Cell Motil. Cytoskeleton 10, 400-409 (1988)

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + detyrosinated alpha-tubulin + L-Tyr
Crithidia fasciculata
terminal Tyr is present in about 5% of flagellar alpha-chain from cells in stationary phase and 20% from cells from midlog phase. None is detected in tubulin from cytosol or the subpellicular corset. In contrast to mammalian cells, in which higher state of tyrosinylation characterizes recently assembled or unstable microtubules, terminal Tyr is present only in the most stable polymer, the flagellar double microtubules
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Crithidia fasciculata
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + detyrosinated alpha-tubulin + L-Tyr
tyrosinates Crithidia tubulin but not brain tubulin and is specific for the alpha chain
1169
Crithidia fasciculata
alpha-tubulin + ADP + phosphate
-
-
-
-
ATP + detyrosinated alpha-tubulin + L-Tyr
terminal Tyr is present in about 5% of flagellar alpha-chain from cells in stationary phase and 20% from cells from midlog phase. None is detected in tubulin from cytosol or the subpellicular corset. In contrast to mammalian cells, in which higher state of tyrosinylation characterizes recently assembled or unstable microtubules, terminal Tyr is present only in the most stable polymer, the flagellar double microtubules
1169
Crithidia fasciculata
?
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-
-
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + detyrosinated alpha-tubulin + L-Tyr
Crithidia fasciculata
terminal Tyr is present in about 5% of flagellar alpha-chain from cells in stationary phase and 20% from cells from midlog phase. None is detected in tubulin from cytosol or the subpellicular corset. In contrast to mammalian cells, in which higher state of tyrosinylation characterizes recently assembled or unstable microtubules, terminal Tyr is present only in the most stable polymer, the flagellar double microtubules
?
-
-
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + detyrosinated alpha-tubulin + L-Tyr
tyrosinates Crithidia tubulin but not brain tubulin and is specific for the alpha chain
1169
Crithidia fasciculata
alpha-tubulin + ADP + phosphate
-
-
-
-
ATP + detyrosinated alpha-tubulin + L-Tyr
terminal Tyr is present in about 5% of flagellar alpha-chain from cells in stationary phase and 20% from cells from midlog phase. None is detected in tubulin from cytosol or the subpellicular corset. In contrast to mammalian cells, in which higher state of tyrosinylation characterizes recently assembled or unstable microtubules, terminal Tyr is present only in the most stable polymer, the flagellar double microtubules
1169
Crithidia fasciculata
?
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Other publictions for EC 6.3.2.25
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
745324
Song
Tubulin-tyrosine ligase (TTL) ...
Mus musculus
J. Biol. Chem.
290
14765-14775
2015
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728025
Prota
Structural basis of tubulin ty ...
Gallus gallus, Mus musculus
J. Cell Biol.
200
259-270
2013
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728153
Szyk
Tubulin tyrosine ligase and st ...
Bos taurus, Sus scrofa
J. Mol. Biol.
425
2412-2414
2013
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709317
Jovanovic
Plant cell division is specifi ...
Nicotiana tabacum, Oryza sativa Japonica Group
J. Exp. Bot.
61
901-909
2010
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2
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709442
Dal Piaz
Sesterterpenes as tubulin tyro ...
Homo sapiens
J. Med. Chem.
52
3814-3828
2009
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686295
Utreras
Microtubule-associated protein ...
Mus musculus
Dev. Neurosci.
30
200-210
2008
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673831
Chen
The testis-specific apoptosis ...
Homo sapiens
Gene
370
58-63
2006
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675003
Gordon-Weeks
Tubulin tyrosination is a majo ...
Mus musculus
J. Cell Biol.
174
839-849
2006
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663250
Erck
A vital role of tubulin-tyrosi ...
Homo sapiens, Mus musculus
Proc. Natl. Acad. Sci. USA
102
7853-7858
2005
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653353
Mas
Cloning of rat olfactory bulb ...
Rattus norvegicus
Neurochem. Res.
27
1453-1458
2002
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650316
Kalisz
Incorporation of nitrotyrosine ...
Sus scrofa
Biochim. Biophys. Acta
1481
131-138
2000
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650790
Idriss
Phosphorylation of tubulin tyr ...
Sus scrofa
Cell Motil. Cytoskeleton
46
1-5
2000
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653350
Erck
Tubulin-tyrosine ligase, a lon ...
Sus scrofa
Neurochem. Res.
25
5-10
2000
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652600
Lafanechere
Suppression of tubulin tyrosin ...
Homo sapiens, Sus scrofa
J. Cell Sci.
111
171-181
1998
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486115
MacRae
Tubulin post-translational mod ...
Rattus norvegicus, Sus scrofa
Eur. J. Biochem.
244
265-278
1997
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1179
Monasterio
Tubulin-tyrosine catalyzes cov ...
Gallus gallus
FEBS Lett.
374
165-168
1995
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1167
Rudiger
The carboxy-terminal peptide o ...
Sus scrofa
Eur. J. Biochem.
220
309-320
1994
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1172
Ersfeld
Characterization of the tubuli ...
Bos taurus, Sus scrofa
J. Cell Biol.
120
725-732
1993
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1177
Rudiger
Characterization of the post-t ...
Sus scrofa
Eur. J. Biochem.
218
107-116
1993
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1178
Deans
Steady-state kinetic mechanism ...
Bos taurus
Biochem. J.
286
243-251
1992
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1168
Joniau
Reaction of alpha-tubulin with ...
Sus scrofa
Anal. Biochem.
184
325-329
1990
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1180
Coudijzer
3 Azido-L-tyrosine as a photoi ...
Sus scrofa
FEBS Lett.
268
95-98
1990
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1169
Chang
Tubulin tyrosination in Crithi ...
Crithidia fasciculata
Cell Motil. Cytoskeleton
10
400-409
1988
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1173
Wehland
Tubulin-tyrosine ligase has a ...
Sus scrofa
J. Cell Biol.
104
1059-1067
1987
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