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Literature summary for 6.3.2.62 extracted from

  • 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 (2009), Biochemistry, 48, 1084-1093 .
    View publication on PubMed
Search for more literature for 6.3.2.62

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Rosetta (DE3) cells Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
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 Mus musculus
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 Mus musculus
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 Mus musculus
AMP-PNP about 98% inhibition at 30 mM, competitive inhibitor for ATP, noncompetitive inhibitorn for glutamate and tubulin Mus musculus
ATAEEEGEMYEDDDEESEAQGPK about 80% inhibition at 10 mM Mus musculus
C-terminal peptide of class III-tubulin competitive inhibitor for tubulin. Noncompetitive inhibition against glutamate and ATP Mus musculus
DATAEEGEFEEEAEEEVA L about 70% inhibition at 10 mM Mus musculus
gamma-L-glutamyl-L-cysteine about 58% inhibition at 10 mM Mus musculus
gamma-L-glutamyl-L-glutamate pH 7.0, 30°C, competitive inhibitor for glutamate. Noncompetitive inhibitor for ATP and tubulin Mus musculus
gamma-L-glutamyl-L-leucine about 60% inhibition at 10 mM Mus musculus
gammaGlu-Glu 80% inhibition at 10 mM, noncompetitive inhibitor for ATP and tubulin Mus musculus
Gly less than 10% inhibition at 10 mM Mus musculus
L-Asp about 35% inhibition at 10 mM Mus musculus
L-Gln about 50% inhibition at 10 mM Mus musculus
L-His about 40% inhibition at 10 mM Mus musculus
L-Leu about 15% inhibition at 10 mM Mus musculus
L-Tyr about 10% inhibition at 10 mM Mus musculus
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% Mus musculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0125
-
 [beta-tubulin]-L-glutamate at pH 7.0 and 30°C Mus musculus
0.0128
-
 L-glutamate at pH 7.0 and 30°C Mus musculus
0.0133
-
 ATP at pH 7.0 and 30°C Mus musculus
3.1
-
 [beta-tubulin]-L-glutamate pH 7.0, 30°C, enzyme from adult brain, 0.006 mM L-glutamate Mus musculus
4.4
-
 L-glutamate pH 7.0, 30°C, enzyme from newborn brain, 0.05 mM ATP Mus musculus
5.4
-
 L-glutamate pH 7.0, 30°C, enzyme from adult brain, 0.05 mM ATP Mus musculus
6.7
-
 [beta-tubulin]-L-glutamate pH 7.0, 30°C, enzyme from newborn brain, 0.05 mM L-glutamate Mus musculus
7.5
-
 ATP pH 7.0, 30°C, enzyme from adult brain, 0.006 mM L-glutamate Mus musculus
15.8
-
 [beta-tubulin]-L-glutamate pH 7.0, 30°C, enzyme from newborn brain, 0.05 mM ATP Mus musculus
16
-
 ATP pH 7.0, 30°C, enzyme from newborn brain, 0.05 mM L-glutamate Mus musculus
19.1
-
 ATP pH 7.0, 30°C, enzyme from adult brain, 0.017 mM tubulin Mus musculus
19.6
-
 L-glutamate pH 7.0, 30°C, enzyme from newborn brain, 0.017 mM tubulin Mus musculus
20.2
-
 L-glutamate pH 7.0, 30°C, enzyme from adult brain, 0.017 mM tubulin Mus musculus
21.8
-
 [beta-tubulin]-L-glutamate pH 7.0, 30°C, enzyme from adult brain, 0.05 mM ATP Mus musculus
26.5
-
 ATP pH 7.0, 30°C, enzyme from newborn brain, 0.017 mM tubulin Mus musculus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ 8 mM used in assay conditions Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + [beta-tubulin]-(alpha-L-glutamyl-gamma-L-glutamyl)-L-glutamate + n L-glutamate Mus musculus (1c) [beta-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
-
 ?
ATP + [beta-tubulin]-(gamma-L-glutamyl)-L-glutamate + L-glutamate Mus musculus (1b) [beta-tubulin]-(alpha-L-glutamyl-gamma-L-glutamyl)-L-glutamate + ADP + phosphate
-
 ?
ATP + [beta-tubulin]-L-glutamate + L-glutamate Mus musculus (1a) [beta-tubulin]-(gamma-L-glutamyl)-L-glutamate + ADP + phosphate
-
 ?
n ATP + [beta-tubulin]-L-glutamate + n L-glutamate Mus musculus 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 [beta-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-
Mus musculus A4Q9F0
-
-

Purification (Commentary)

Purification (Comment) Organism
glutathione-Sepharose bead chromatography, and Superdex 200 gel filtration Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
brain adult and newborn Mus musculus
-

Storage Stability

Storage Stability Organism
-80°C, 50 mM Tris-HCl (pH 7.4), 20 mM NaCl, 1 mM EDTA, and 1 mM dithiothreitol, at least 3 months, no loss of activity Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + [beta-tubulin]-(alpha-L-glutamyl-gamma-L-glutamyl)-L-glutamate + n L-glutamate (1c) Mus musculus [beta-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
-
 ?
ATP + [beta-tubulin]-(gamma-L-glutamyl)-L-glutamate + L-glutamate (1b) Mus musculus [beta-tubulin]-(alpha-L-glutamyl-gamma-L-glutamyl)-L-glutamate + ADP + phosphate
-
 ?
ATP + [beta-tubulin]-L-glutamate + L-glutamate (1a) Mus musculus [beta-tubulin]-(gamma-L-glutamyl)-L-glutamate + ADP + phosphate
-
 ?
ATP + [beta-tubulin]-L-glutamate + L-glutamate the enzyme performs both initiation and elongation in the polyglutamylation reaction on beta-tubulin through a random sequential pathway Mus musculus [tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + ADP + phosphate
-
 ?
n ATP + [beta-tubulin]-L-glutamate + n L-glutamate 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 Mus musculus [beta-tubulin]-(gamma-(poly-alpha-L-glutamyl)-L-glutamyl)-L-glutamate + n ADP + n phosphate
-
 ?

Synonyms

Synonyms Comment Organism
beta-tubulin-selective polyglutamylase
-
 Mus musculus
TTLL7
-
 Mus musculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Mus musculus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.02
-
 Adenylyl imidodiphosphate pH 7.0, 30°C, versus ATP Mus musculus
0.12
-
 Adenylyl imidodiphosphate pH 7.0, 30°C, versus L-glutamate Mus musculus
0.23
-
 Adenylyl imidodiphosphate pH 7.0, 30°C, versus beta-tubulin Mus musculus
0.5
-
 C-terminal peptide of class III-tubulin pH 7.0, 30°C, versus beta-tubulin Mus musculus
0.83
-
 C-terminal peptide of class III-tubulin pH 7.0, 30°C, versus ATP Mus musculus
1.06
-
 C-terminal peptide of class III-tubulin pH 7.0, 30°C, versus L-glutamate Mus musculus

General Information

General Information Comment Organism
metabolism the enzyme TTLL7 performs both initiation and elongation in the polyglutamylation reaction on beta-tubulin Mus musculus