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Literature summary for 2.7.1.56 extracted from
- Fructose degradation in the haloarchaeon Haloferax volcanii involves a bacterial type phosphoenolpyruvate-dependent phosphotransferase system, fructose-1-phosphate kinase, and class II fructose-1,6-bisphosphate aldolase (2012), J. Bacteriol., 194, 3088-3097.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.08 | - |
ATP | in 100 mM Tris-HCl, pH 7.5, 7 mM MgCl2, 0.5 M KCl, at 42°C | Haloferax volcanii |  |
| 0.31 | - |
D-Fructose 1-phosphate | in 100 mM Tris-HCl, pH 7.5, 7 mM MgCl2, 0.5 M KCl, at 42°C | Haloferax volcanii | |
| 1.12 | - |
D-fructose 6-phosphate | in 100 mM Tris-HCl, pH 7.5, 7 mM MgCl2, 0.5 M KCl, at 42°C | Haloferax volcanii | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| K+ | the enzyme shows the highest activity at about 0.5M KCl | Haloferax volcanii | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 38000 | - |
2 * 38000, SDS-PAGE | Haloferax volcanii |
| 70000 | - |
gel filtration | Haloferax volcanii |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + D-fructose 1-phosphate | Haloferax volcanii | physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate | ADP + D-fructose 1,6-bisphosphate | - |
? | |
| ATP + D-fructose 1-phosphate | Haloferax volcanii H1209 | physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate | ADP + D-fructose 1,6-bisphosphate | - |
? | |
| ATP + D-fructose 6-phosphate | Haloferax volcanii | physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate | ADP + ? | - |
? | |
| ATP + D-fructose 6-phosphate | Haloferax volcanii H1209 | physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate | ADP + ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Haloferax volcanii | D4GYE6 | - |
- |
| Haloferax volcanii H1209 | D4GYE6 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| Ni-NTA column chromatography and Superdex 200 gel filtration | Haloferax volcanii |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + D-fructose 1-phosphate | physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate | Haloferax volcanii | ADP + D-fructose 1,6-bisphosphate | - |
? | |
| ATP + D-fructose 1-phosphate | physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate | Haloferax volcanii H1209 | ADP + D-fructose 1,6-bisphosphate | - |
? | |
| ATP + D-fructose 6-phosphate | physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate | Haloferax volcanii | ADP + ? | - |
? | |
| ATP + D-fructose 6-phosphate | physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate | Haloferax volcanii H1209 | ADP + ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | 2 * 38000, SDS-PAGE | Haloferax volcanii |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 1-PFK | - |
Haloferax volcanii |
| fructose-1-phosphate kinase | - |
Haloferax volcanii |
| pfkB | - |
Haloferax volcanii |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | 9 | - |
Haloferax volcanii |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Haloferax volcanii | enzyme expression is specifically upregulated in fructose-grown cells | up |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | the enzyme is involved in fructose catabolism | Haloferax volcanii |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 34 | - |
D-fructose 6-phosphate | in 100 mM Tris-HCl, pH 7.5, 7 mM MgCl2, 0.5 M KCl, at 42°C | Haloferax volcanii | |
| 1200 | - |
D-Fructose 1-phosphate | in 100 mM Tris-HCl, pH 7.5, 7 mM MgCl2, 0.5 M KCl, at 42°C | Haloferax volcanii | |
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