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Literature summary for 2.2.1.10 extracted from
- MJ0400 from Methanocaldococcus jannaschii exhibits fructose-1,6-bisphosphate aldolase activity (2008), FEMS Microbiol. Lett., 281, 36-41.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene Mj0400, DNA and amino acid sequence determination and analysis, overexpression of the His6-tagged enzyme in Escherichia coli strain Rosetta2(DE3)pLysS as mainly insoluble protein | Methanocaldococcus jannaschii |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 4-O-phosphonato-D-erythrose | competitive inhibition of aldolase activity | Methanocaldococcus jannaschii |  |
| glycylglycine | slightly inhibiting as buffer at 50 mM | Methanocaldococcus jannaschii | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | MJ0400-His6 exhibits Michaelis-Menten kinetics in the aldolase reaction | Methanocaldococcus jannaschii |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-aspartate semialdehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate | Methanocaldococcus jannaschii | - |
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + 2,3-dioxopropyl phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methanocaldococcus jannaschii | Q57843 | gene mj0400 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| soluble fraction of recombinant His6-tagged MJ0400 from Escherichia coli strain Rosetta(DE3) by nickel affinity chromatography to over 97% purity | Methanocaldococcus jannaschii |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| cell culture | optimal growth temperature is 85°C | Methanocaldococcus jannaschii | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.033 | - |
purified recombinant enzyme, pH 7.5, 50°C, buffer Tris-HCl, HEPES/NaOH, or Na-phosphate | Methanocaldococcus jannaschii |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-aspartate semialdehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate | - |
Methanocaldococcus jannaschii | 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + 2,3-dioxopropyl phosphate | - |
? | |
| additional information | MJ0400 acts as an 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid synthase, catalyzing the reaction of L-aspartate semialdehyde and 6-deoxy-5-ketofructose-1-phosphate to 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid, but the recombinant His6-tagged MJ0400 also catalyzes the cleavage of fructose-1,6-bisphosphate to glyceraldehyde-3-phosphate and dihydroxyacetone phosphate, exhibiting fructose-1,6-bisphosphate aldolase, FBP aldolase, activity, EC 4.1.2.13, or the transaldolase reaction with D-fructose-6-phosphate and D-erythose-4-phosphate as substrates. The enzyme shows high substrate specificity for fructose-6-phosphate | Methanocaldococcus jannaschii | ? | - |
? | |
| pyruvate + D-erythrose 4-phosphate | - |
Methanocaldococcus jannaschii | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid synthase | - |
Methanocaldococcus jannaschii |
| MJ0400 | - |
Methanocaldococcus jannaschii |
| More | cf. EC 4.1.2.13 | Methanocaldococcus jannaschii |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
assay at | Methanocaldococcus jannaschii |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | 85 | 10% activity at 25°C, higher activity at 50°C, optimal activity probably at or above the optimal growth temperature of 85°C | Methanocaldococcus jannaschii |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 80 | - |
10 mg/ml purified recombinant His6-tagged enzyme, 50 mM Tris-HCl, pH 7.5, 1 mM DTT, half-life is 37 h | Methanocaldococcus jannaschii |
| 100 | - |
10 mg/ml purified recombinant His6-tagged enzyme, 50 mM Tris-HCl, pH 7.5, 1 mM DTT, half-life is 1 h | Methanocaldococcus jannaschii |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Methanocaldococcus jannaschii |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.38 | - |
4-O-phosphonato-D-erythrose | recombinant enzyme, pH 7.5, 50°C | Methanocaldococcus jannaschii | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | the enzyme is involved in both carbon metabolism and amino acid biosynthesis, it catalyzes as transaldolase a step leading to biosynthesis of 3-dehydroquinate, which enters the shikimate pathway, and also shows activity as fructose 1,6-bisphosphate aldolase in carbon metabolism, overview | Methanocaldococcus jannaschii |
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