BRENDA - Enzyme Database
show all sequences of 2.3.1.108

Molecular basis for age-dependent microtubule acetylation by tubulin acetyltransferase

Szyk, A.; Deaconescu, A.M.; Spector, J.; Goodman, B.; Valenstein, M.L.; Ziolkowska, N.E.; Kormendi, V.; Grigorieff, N.; Roll-Mecak, A.; Cell 157, 1405-1415 (2014)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
cocrystal structures with bisubstrate analogs, consisting of a substrate peptide covalently linked to CoA through Lys40, to 1.35 A resolution. Substrate residue Lys40 is engaged in a suboptimal active site
Homo sapiens
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
microtubule
lumen of microtubule
Homo sapiens
5874
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
Q5SQI0
-
-
Crystallization (Commentary) (protein specific)
Crystallization
Organism
cocrystal structures with bisubstrate analogs, consisting of a substrate peptide covalently linked to CoA through Lys40, to 1.35 A resolution. Substrate residue Lys40 is engaged in a suboptimal active site
Homo sapiens
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
microtubule
lumen of microtubule
Homo sapiens
5874
-
General Information
General Information
Commentary
Organism
physiological function
despite the confined intraluminal location of microtubule residue Lys40, TAT efficiently scans the microtubule bidirectionally and acetylates stochastically without preference for ends. TAT catalytic activity, not constrained luminal diffusion, is rate limiting for acetylation
Homo sapiens
General Information (protein specific)
General Information
Commentary
Organism
physiological function
despite the confined intraluminal location of microtubule residue Lys40, TAT efficiently scans the microtubule bidirectionally and acetylates stochastically without preference for ends. TAT catalytic activity, not constrained luminal diffusion, is rate limiting for acetylation
Homo sapiens
Other publictions for EC 2.3.1.108
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)
736728
Nakakura
Intracellular localization of ...
Rattus norvegicus
Med. Mol. Morphol.
49
133-143
2016
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735638
Yuzawa
Structural basis of cofactor-m ...
Homo sapiens
Biochem. J.
467
103-113
2015
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735908
Neumann
Loss of MEC-17 leads to microt ...
Caenorhabditis elegans
Cell Rep.
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93-103
2014
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735916
Szyk
Molecular basis for age-depend ...
Homo sapiens
Cell
157
1405-1415
2014
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1
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736637
Davenport
Structural and functional char ...
Homo sapiens
J. Mol. Biol.
426
2605-2616
2014
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1
33
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20
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3
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1
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18
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18
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19
19
736778
Howes
Effects of tubulin acetylation ...
Homo sapiens
Mol. Biol. Cell
25
257-266
2014
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736872
Wang
Microtubule acetylation amplif ...
Mus musculus
Nat. Commun.
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3479
2014
1
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1
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735631
Yang
Regulation of adipogenesis by ...
Mus musculus
Biochem. J.
449
605-612
2013
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736795
Kalebic
Tubulin acetyltransferase alph ...
Mus musculus
Mol. Cell. Biol.
33
1114-1123
2013
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1
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736870
Kalebic
alphaTAT1 is the major alpha-t ...
Mus musculus
Nat. Commun.
4
1962
2013
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1
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736879
Montagnac
alphaTAT1 catalyses microtubul ...
Homo sapiens
Nature
502
567-570
2013
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719320
Topalidou
Genetically separable function ...
Caenorhabditis elegans
Curr. Biol.
22
1057-1065
2012
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2
2
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719403
Castro-Castro
ATAT1/MEC-17 acetyltransferase ...
Homo sapiens
Eur. J. Cell Biol.
91
950-960
2012
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2
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3
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706413
Solinger
The Caenorhabditis elegans elo ...
Caenorhabditis elegans
PLoS Genet.
6
e1000820
2010
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1
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720540
Akella
MEC-17 is an alpha-tubulin ace ...
Caenorhabditis elegans, Chlamydomonas reinhardtii, Danio rerio, Mus musculus, Tetrahymena thermophila
Nature
467
218-222
2010
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2
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5
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6
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9
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5
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1
13
13
1
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720906
Leroux
Tubulin acetyltransferase disc ...
Caenorhabditis elegans, Homo sapiens, Tetrahymena sp.
Proc. Natl. Acad. Sci. USA
107
21238-21239
2010
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3
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1
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4
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3
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6
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3
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3
3
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1
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6
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3
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6
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7
7
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720907
Shida
The major alpha-tubulin K40 ac ...
Caenorhabditis elegans, no activity in Potorous tridactylis
Proc. Natl. Acad. Sci. USA
107
21517-21522
2010
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1
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1
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6
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3
3
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486115
MacRae
Tubulin post-translational mod ...
Bos taurus, Chlamydomonas reinhardtii
Eur. J. Biochem.
244
265-278
1997
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1
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3
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2
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2
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1
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1
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3
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1
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486116
Lloyd
Assay of tubulin acetyltransfe ...
Bos taurus
Anal. Biochem.
216
42-46
1994
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1
1
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1
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3
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3
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486117
Maruta
The acetylation of alpha-tubul ...
Chlamydomonas reinhardtii
J. Cell Biol.
103
571-579
1986
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3
1
3
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486118
Greer
Alpha-tubulin acetylase activi ...
Chlamydomonas reinhardtii 21 gr, Chlamydomonas reinhardtii
J. Cell Biol.
101
2081-2084
1985
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