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Literature summary for 4.1.2.13 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.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| cysteine | highest activity at 1 mM cysteine | Haloferax volcanii |  |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| EDTA | 2 mM, complete inhibition of activity, which could be reversed by the addition of Mn2+ (3 mM) | Haloferax volcanii | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.24 | - |
D-fructose 1,6-bisphosphate | pH 7.5, 42°C | Haloferax volcanii | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| FeSO4 | the enzyme requires divalent cation for activity. The highest activity is obtained with MnCl2 (100%, 50 U/mg), which can be partially replaced by FeSO4 (40% residual activity) | Haloferax volcanii | |
| KCl | highest activity at 1 mM KCl | Haloferax volcanii | |
| MnCl2 | the enzyme requires divalent cation for activity. The highest activity is obtained with MnCl2 (100%, 50 U/mg), which can be partially replaced by FeSO4 (40% residual activity) | Haloferax volcanii | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 42000 | - |
2 * 42000, SDS-PAGE | Haloferax volcanii |
| 80000 | - |
- |
Haloferax volcanii |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-fructose 1,6-bisphosphate | Haloferax volcanii | the enzyme has an anabolic function catalyzing fructose-1,6-bisphosphate formation in the course of gluconeogenesis | glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
r | |
| D-fructose 1,6-bisphosphate | Haloferax volcanii DSM 3757 | the enzyme has an anabolic function catalyzing fructose-1,6-bisphosphate formation in the course of gluconeogenesis | glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Haloferax volcanii | D4GYE0 | - |
- |
| Haloferax volcanii DSM 3757 | D4GYE0 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-fructose 1,6-bisphosphate | - |
Haloferax volcanii | glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
r | |
| D-fructose 1,6-bisphosphate | the enzyme has an anabolic function catalyzing fructose-1,6-bisphosphate formation in the course of gluconeogenesis | Haloferax volcanii | glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
r | |
| D-fructose 1,6-bisphosphate | - |
Haloferax volcanii DSM 3757 | glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
r | |
| D-fructose 1,6-bisphosphate | the enzyme has an anabolic function catalyzing fructose-1,6-bisphosphate formation in the course of gluconeogenesis | Haloferax volcanii DSM 3757 | glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | 2 * 42000, SDS-PAGE | Haloferax volcanii |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| FBA | - |
Haloferax volcanii |
| fructose-1,6-bisphosphate aldolase | - |
Haloferax volcanii |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 42 | - |
assay at | Haloferax volcanii |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
- |
Haloferax volcanii |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Haloferax volcanii | highly increased transcript levels of fba in fructose-grown cells compared to those in glucose-grown cells, indicating fructosespecific upregulation | up |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | deletion mutant loses the ability to grow on fructose, but growth on glucose is not inhibited and is even slightly stimulated | Haloferax volcanii |
| physiological function | the enzyme has an anabolic function catalyzing fructose-1,6-bisphosphate formation in the course of gluconeogenesis. The enzyme is essential for growth on fructose | Haloferax volcanii |
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