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Literature summary for 3.5.4.16 extracted from
- Biochemical characterization of oligomerization of Escherichia coli GTP cyclohydrolase I (2002), J. Biochem. Mol. Biol., 35, 255-261.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| overexpression of wild-type and mutant enzymes from plasmids in strain DH5alpha | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C110G | site-directed mutagenesis, 0.22% activity compared to the wild-type enzyme, increased temperature optimum | Escherichia coli |
| C181S | site-directed mutagenesis, 0.29% activity compared to the wild-type enzyme, highly increased temperature optimum | Escherichia coli |
| E111K | site-directed mutagenesis, 3.1% activity compared to the wild-type enzyme, increased temperature optimum | Escherichia coli |
| E152K | site-directed mutagenesis, 0.06% activity compared to the wild-type enzyme, increased pH optimum, decreased temperature optimum | Escherichia coli |
| H112D | site-directed mutagenesis, 0.23% activity compared to the wild-type enzyme, decreased pH optimum, increased temperature optimum | Escherichia coli |
| H113N | site-directed mutagenesis, 67% activity compared to the wild-type enzyme, decreased pH optimum, increased temperature optimum | Escherichia coli |
| H179Q | site-directed mutagenesis, 0.8% activity compared to the wild-type enzyme, increased temperature optimum | Escherichia coli |
| K136E | site-directed mutagenesis, 0.25% activity compared to the wild-type enzyme, increased temperature optimum | Escherichia coli |
| L134Q | site-directed mutagenesis, 1.85% activity compared to the wild-type enzyme, increased temperature optimum | Escherichia coli |
| R139C | site-directed mutagenesis, 29.3% activity compared to the wild-type enzyme, decreased pH optimum | Escherichia coli |
| R185G | site-directed mutagenesis, 2.9% activity compared to the wild-type enzyme, decreased temperature optimum | Escherichia coli |
| R56L | site-directed mutagenesis, 14% activity compared to the wild-type enzyme, increased temperature optimum | Escherichia coli |
| S135C | site-directed mutagenesis, 0.7% activity compared to the wild-type enzyme, decreased pH and temperature optimum | Escherichia coli |
| V150E | site-directed mutagenesis, 3.2% activity compared to the wild-type enzyme, slightly decreased pH optimum, increased temperature optimum | Escherichia coli |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | association and dissociation constants of wild-type and mutant enzymes in oligomerization | Escherichia coli |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| additional information | - |
MW of mutant E152K is very high in gel filtration approximately corresponding to a didecameric form | Escherichia coli |
| 25000 | - |
10 * 25000, about, composed of a pentamers of 5 dimers, the active site is located at the interface between dimers, Lys136, Arg139, and Glu152 are especially important for the oligomerization | Escherichia coli |
| 50000 | - |
dimeric mutants K136E and R139C, gel filtration | Escherichia coli |
| 120000 | - |
wild-type enzyme in presence of 0.3 M KCl, mutants C110G, E111K, H112D, and C181S, gel filtration | Escherichia coli |
| 250000 | - |
decameric wild-type enzyme, gel filtration | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| GTP + H2O | Escherichia coli | first step in the biosynthesis of pteridine coenzymes, such as folic acid and tetrahydrobiopterin | dihydroneopterin triphosphate + formate | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant wild-type and mutant enzymes | Escherichia coli |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| reconstitution of dissociated mutant enzyme subunits to chimeric dimers from 2 monomers A and B derived from 2 different mutants, overview | Escherichia coli |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
reconstituted chimeric mutant dimers, overview | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| GTP + H2O | - |
Escherichia coli | dihydroneopterin triphosphate + formate | - |
? | |
| GTP + H2O | first step in the biosynthesis of pteridine coenzymes, such as folic acid and tetrahydrobiopterin | Escherichia coli | dihydroneopterin triphosphate + formate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| decamer | 10 * 25000, about, composed of a pentamers of 5 dimers, the active site is located at the interface between dimers, Lys136, Arg139, and Glu152 are especially important for the oligomerization | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GTP CHase I | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 45 | - |
mutant E152K | Escherichia coli |
| 55 | - |
mutants S135C and R185G | Escherichia coli |
| 60 | - |
wild-type enzyme and mutant R139C | Escherichia coli |
| 65 | - |
mutants H112D, K136E, and H179Q | Escherichia coli |
| 70 | - |
mutant H113 N | Escherichia coli |
| 72 | - |
mutant R56L | Escherichia coli |
| 75 | - |
mutants C110G and L134Q | Escherichia coli |
| 85 | - |
mutants E111K and V150E | Escherichia coli |
| 90 | - |
mutant C181S | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
mutant S135C | Escherichia coli |
| 7 | 8.5 | mutant V150E | Escherichia coli |
| 7.5 | - |
mutant H112D | Escherichia coli |
| 8 | - |
mutants H113N and R139C | Escherichia coli |
| 8.5 | - |
wild-type enzyme and mutants R56L, C110G, E111K, L134Q, K136E, H179Q, C181S, and R185G | Escherichia coli |
| 9 | - |
mutant E152K | Escherichia coli |
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