EC Number | General Stability | Organism |
---|---|---|
4.2.1.10 | guanidine hydrochloride, the type II enzyme from Aspergillus nidulans unfolds at concentrations of denaturant 4fold greater than type I enzyme from E. coli and through a series of discrete transitions, while the type I enzyme from E. coli unfolds in a single transition | Escherichia coli |
4.2.1.10 | guanidine hydrochloride, the type II enzyme from Aspergillus nidulans unfolds at concentrations of denaturant 4fold greater than type I enzyme from E. coli and through a series of discrete transitions, while the type I enzyme from E. coli unfolds in a single transition | Aspergillus nidulans |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
4.2.1.10 | diethyl dicarbonate | - |
Aspergillus nidulans | |
4.2.1.10 | diethyl dicarbonate | - |
Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.2.1.10 | 0.015 | - |
3-dehydroquinate | - |
Escherichia coli | |
4.2.1.10 | 0.15 | - |
3-dehydroquinate | - |
Aspergillus nidulans |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
4.2.1.10 | 16505 | - |
12 * 16505 | Aspergillus nidulans |
4.2.1.10 | 27466 | - |
2 * 27466 | Escherichia coli |
4.2.1.10 | 44000 | 53000 | sedimentation velocity determination and equilibrium sedimentation | Escherichia coli |
4.2.1.10 | 190000 | 200000 | determination of sedimentation velocity and equilibrium sedimentation | Aspergillus nidulans |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.2.1.10 | 3-dehydroquinate | Aspergillus nidulans | type II dehydroquinase is involved in the quinate pathway | ? | - |
? | |
4.2.1.10 | 3-dehydroquinate | Escherichia coli | type I dehydroquinase is involved in the biosynthetic shikimate pathway | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.2.1.10 | Aspergillus nidulans | - |
type II dehydroquinase | - |
4.2.1.10 | Escherichia coli | - |
type I dehydroquinase | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.2.1.10 | 3-dehydroquinate | - |
Escherichia coli | 3-dehydroshikimate + H2O | - |
? | |
4.2.1.10 | 3-dehydroquinate | - |
Aspergillus nidulans | 3-dehydroshikimate + H2O | - |
? | |
4.2.1.10 | 3-dehydroquinate | type II dehydroquinase is involved in the quinate pathway | Aspergillus nidulans | ? | - |
? | |
4.2.1.10 | 3-dehydroquinate | type I dehydroquinase is involved in the biosynthetic shikimate pathway | Escherichia coli | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
4.2.1.10 | dimer | 2 * 27466 | Escherichia coli |
4.2.1.10 | dodecamer | 12 * 16505 | Aspergillus nidulans |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
4.2.1.10 | 57 | - |
Tm: 57°C, irreversible thermal denaturation | Escherichia coli |
4.2.1.10 | 70 | - |
10 min, stable | Aspergillus nidulans |
4.2.1.10 | 70 | - |
10 min, not stable | Escherichia coli |
4.2.1.10 | 82 | - |
irreversible thermal denaturation involves at least three transitions. The first is a broad shoulder at approximately 82°C, the second is a shoarp doublet at 86°C and the final transition occurs at 95°C | Aspergillus nidulans |