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Literature summary for 3.1.3.11 extracted from
- Identification and characterization of cytosolic fructose-1,6-bisphosphatase in Euglena gracilis (2015), Biosci. Biotechnol. Biochem., 79, 1957-1964 .
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| AMP | slight activation at 1 mM | Euglena gracilis |  |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli strain BL21 Star (DE3) pLysS cells | Euglena gracilis |
| gene EgFBPaseIII, semi-quantitative RT-PCR enzyme expression analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 Star (DE3)pLysS | Euglena gracilis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | silencing of EgFBPaseIII by RNAi | Euglena gracilis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| D-fructose 2,6-bisphosphate | the Lys residue, which is known to be essential for inhibiting Fru 2,6-P2 in gluconeogenic FBPases, is also conserved in EgFBPaseIII at Lys408 | Euglena gracilis | |
| H2O2 | the activity of EgFBPaseIII is partially inhibited by the H2O2 treatment, but is not reactivated when incubated with DTT, indicating that EgFBPaseIII is nonspecifically oxidized at amino acid residues, but not specifically at Cys residues | Euglena gracilis | |
| additional information | no inhibition but slight activation by AMP | Euglena gracilis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0165 | - |
D-fructose 1,6-bisphosphate | pH and temperature not specified in the publication | Euglena gracilis | |
| 0.0165 | - |
D-fructose 1,6-bisphosphate | pH 8.0, temperature not specified in the publication, recombinant enzyme | Euglena gracilis | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytosol | - |
Euglena gracilis | 5829 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Euglena gracilis | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 52000 | - |
SDS-PAGE | Euglena gracilis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-fructose 1,6-bisphosphate + H2O | Euglena gracilis | - |
D-fructose 6-phosphate + phosphate | - |
? | |
| D-fructose 1,6-bisphosphate + H2O | Euglena gracilis Z | - |
D-fructose 6-phosphate + phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Euglena gracilis | A0A0U4MTX7 | - |
- |
| Euglena gracilis Z | A0A0U4MTX7 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Euglena gracilis |
| recombinant His-tagged enzyme from Escherichia coli strain BL21 Star (DE3)pLysS by metal affinity chromatography | Euglena gracilis |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 30.4 | - |
pH and temperature not specified in the publication | Euglena gracilis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-fructose 1,6-bisphosphate + H2O | - |
Euglena gracilis | D-fructose 6-phosphate + phosphate | - |
? | |
| D-fructose 1,6-bisphosphate + H2O | - |
Euglena gracilis Z | D-fructose 6-phosphate + phosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 52000, SDS-PAGE | Euglena gracilis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| cytosolic FBPase | - |
Euglena gracilis |
| EgFBPaseIII | - |
Euglena gracilis |
| FBPase | - |
Euglena gracilis |
| fructose-1,6-bisphosphatase | - |
Euglena gracilis |
| neutral FBPase | - |
Euglena gracilis |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 26.4 | - |
D-fructose 1,6-bisphosphate | pH and temperature not specified in the publication | Euglena gracilis | |
| 26.4 | - |
D-fructose 1,6-bisphosphate | pH 8.0, temperature not specified in the publication, recombinant enzyme | Euglena gracilis | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
- |
Euglena gracilis |
| 7.5 | - |
recombinant enzyme | Euglena gracilis |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 9 | activity range, profile overview, recombinant enzyme | Euglena gracilis |
| 6.5 | 8.5 | pH 6.5: about 50% of maximal activity, pH 8.5: about 45% of maximal activity | Euglena gracilis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the amino acid sequence of EgFBPaseIII shows low identity (35%) with EgFBPaseI and II, while it shows higher identity of 51-52% with other cytosolic FBPases from plants. EgFBPaseIII has an additional sequence at the N-terminus that other cytosolic FBPases do not possess, this N-terminal region contains no signal peptide or known domain architecture | Euglena gracilis |
| malfunction | no significant differences are observed in the production of paramylon in transiently suppressed EgFBPaseIII gene expression cells by RNAi (KD-EgFBPaseIII), but FBPase activity is markedly decreased in KD-EgFBPaseIII cells. Growth of KD-EgFBPaseIII cells is slightly increased compared to control cells | Euglena gracilis |
| metabolism | key enzyme in gluconeogenesis and position branch point of carbon partitioning between paramylon and wax ester biosynthesis. The activity of the enzyme (EgFBPaseIII) is not regulated by AMP or reversible redox modulation | Euglena gracilis |
| additional information | cytosolic EgFBPaseIII is identical to the neutral FBPase | Euglena gracilis |
| physiological function | cytosolic fructose-1,6-bisphosphatase (FBPase) appears to be a key enzyme in gluconeogenesis and position branch point of carbon partitioning between paramylon and wax ester biosynthesis. Euglena gracilis accumulates the storage polysaccharide paramylon, a beta-1,3-glucan, under aerobic conditions. Under anaerobic conditions, the cells degrade paramylon and synthesize wax esters. The activity of EgFBPaseIII is not regulated by AMP or reversible redox modulation | Euglena gracilis |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1590 | - |
D-fructose 1,6-bisphosphate | pH and temperature not specified in the publication | Euglena gracilis | |
| 1600 | - |
D-fructose 1,6-bisphosphate | pH 8.0, temperature not specified in the publication, recombinant enzyme | Euglena gracilis | |
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