Any feedback?
Literature summary for 3.1.3.11 extracted from
- Fructose 1,6-bisphosphate aldolase/phosphatase may be an ancestral gluconeogenic enzyme (2010), Nature, 464, 1077-1081.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | AMP, ADP or glucose have no effect on enzyme activity | Archaea | |
| additional information | AMP, ADP or glucose have no effect on enzyme activity | Cenarchaeum symbiosum | |
| additional information | AMP, ADP or glucose have no effect on enzyme activity | Ignicoccus hospitalis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | AMP, ADP or glucose have no effect on enzyme activity | Archaea | |
| additional information | AMP, ADP or glucose have no effect on enzyme activity | Cenarchaeum symbiosum | |
| additional information | AMP, ADP or glucose have no effect on enzyme activity | Ignicoccus hospitalis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.04 | - |
D-fructose 1,6-bisphosphate | pH not specified in the publication, 40°C | Cenarchaeum symbiosum |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-fructose 1,6-bisphosphate + H2O | Archaea | - |
D-fructose 6-phosphate + phosphate | - |
? | |
| D-fructose 1,6-bisphosphate + H2O | Cenarchaeum symbiosum | - |
D-fructose 6-phosphate + phosphate | - |
? | |
| D-fructose 1,6-bisphosphate + H2O | Ignicoccus hospitalis | - |
D-fructose 6-phosphate + phosphate | - |
? | |
| additional information | Archaea | bifunctional fructose 1,6-bisphosphate, FBP, aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity | ? | - |
? | |
| additional information | Cenarchaeum symbiosum | bifunctional fructose 1,6-bisphosphate, FBP, aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity | ? | - |
? | |
| additional information | Ignicoccus hospitalis | bifunctional fructose 1,6-bisphosphate, FBP, aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Archaea | - |
- |
- |
| Cenarchaeum symbiosum | - |
- |
- |
| Ignicoccus hospitalis | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-fructose 1,6-bisphosphate + H2O | - |
Archaea | D-fructose 6-phosphate + phosphate | - |
? | |
| D-fructose 1,6-bisphosphate + H2O | - |
Cenarchaeum symbiosum | D-fructose 6-phosphate + phosphate | - |
? | |
| D-fructose 1,6-bisphosphate + H2O | - |
Ignicoccus hospitalis | D-fructose 6-phosphate + phosphate | - |
? | |
| additional information | bifunctional fructose 1,6-bisphosphate, FBP, aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity | Archaea | ? | - |
? | |
| additional information | bifunctional fructose 1,6-bisphosphate, FBP, aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity | Cenarchaeum symbiosum | ? | - |
? | |
| additional information | bifunctional fructose 1,6-bisphosphate, FBP, aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity | Ignicoccus hospitalis | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| archaeal FBP aldolase/phosphatase | - |
Archaea |
| archaeal FBP aldolase/phosphatase | - |
Cenarchaeum symbiosum |
| archaeal FBP aldolase/phosphatase | - |
Ignicoccus hospitalis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
assay at | Cenarchaeum symbiosum |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
the archaeal FBP aldolase/phosphatases are highly thermostable | Archaea |
| 70 | - |
heat-stable for up to 1 h | Cenarchaeum symbiosum |
| 82 | - |
heat-stable, half-life is 20 min | Ignicoccus hospitalis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | virtually all archaeal groups as well as the deeply branching bacterial lineages contain the bifunctional D-fructose 1,6-bisphosphate aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity. This enzyme is missing in most other bacteria and in eukaryota. Phylogenetic analysis, overview | Archaea |
| evolution | virtually all archaeal groups as well as the deeply branching bacterial lineages contain the bifunctional D-fructose 1,6-bisphosphate aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity. This enzyme is missing in most other bacteria and in eukaryota. Phylogenetic analysis, overview | Ignicoccus hospitalis |
| evolution | virtually all archaeal groups as well as the deeply branching bacterial lineages contain the bifunctional D-fructose 1,6-bisphosphate aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity. This enzyme is missing inmost other Bacteria and in Eukaryota. Phylogenetic analysis, overview | Cenarchaeum symbiosum |
| additional information | active site structures, overview | Archaea |
| additional information | active site structures, overview | Cenarchaeum symbiosum |
| physiological function | the enzyme's bifunctionality ensures that heat-labile triosephosphates are quickly removed and trapped in stabie D-fructose 6-phosphate, rendering gluconeogenesis unidirectional | Cenarchaeum symbiosum |
| physiological function | the enzyme's bifunctionality ensures that heat-labile triosephosphates are quickly removed and trapped in stable D-fructose 6-phosphate, rendering gluconeogenesis unidirectional | Archaea |
| physiological function | the enzyme's bifunctionality ensures that heat-labile triosephosphates are quickly removed and trapped in stable D-fructose 6-phosphate, rendering gluconeogenesis unidirectional | Ignicoccus hospitalis |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
