Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli Rosetta (DE3) cells | Mus musculus |
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 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 | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | 8 mM used in assay conditions | Mus musculus |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | - |
- |
- |
Mus musculus | A4Q9F0 | - |
- |
Purification (Comment) | Organism |
---|---|
glutathione-Sepharose bead chromatography, and Superdex 200 gel filtration | Mus musculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
brain | adult and newborn | Mus musculus | - |
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 | 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 | Comment | Organism |
---|---|---|
beta-tubulin-selective polyglutamylase | - |
Mus musculus |
TTLL7 | - |
Mus musculus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
- |
Mus musculus |
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 | Comment | Organism |
---|---|---|
metabolism | the enzyme TTLL7 performs both initiation and elongation in the polyglutamylation reaction on beta-tubulin | Mus musculus |