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Literature summary for 3.1.3.11 extracted from
- Molecular cloning, expression and purification of muscle fructose-1,6-bisphosphatase from Zaocys dhumnades: the role of the N-terminal sequence in AMP activation at alkaline pH (2000), Biol. Chem., 381, 561-566.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| AMP | 20% activation at 0.001-0.002 mM of AMP at alkaline pH, KM value of 0.00018 mM at pH 7.5, 30°C, recombinant enzyme | Homo sapiens |  |
| AMP | 4fold activation at pH 9.2 | Ptyas dhumnades | |
| K+ | - |
Homo sapiens | |
| K+ | - |
Ptyas dhumnades | |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| commentary | Ptyas dhumnades |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| AMP | - |
Homo sapiens | |
| AMP | the AMP binding is mainly located in the N-terminal region | Ptyas dhumnades | |
| additional information | not: AMP | Rattus norvegicus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0001 | - |
D-fructose 1,6-bisphosphate | pH 7.5, 30°C, wild-type enzyme | Ptyas dhumnades | |
| 0.00011 | - |
D-fructose 1,6-bisphosphate | pH 7.5, 30°C, recombinant enzyme | Ptyas dhumnades | |
| 0.00014 | - |
D-fructose 1,6-bisphosphate | pH 7.5, 30°C, chimeric enzyme | Ptyas dhumnades | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 36000 | - |
x * 36000, SDS-PAGE | Ptyas dhumnades |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-fructose 1,6-bisphosphate + H2O | Ptyas dhumnades | enzyme is usually regarded as a regulatory enzyme of gluconeogenesis | D-fructose 6-phosphate + phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
| Ptyas dhumnades | - |
snake | - |
| Rattus norvegicus | - |
- |
- |
| Sus scrofa | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| side-chain modification | a chimeric enzyme is constructed where the amino terminal residues, 1-60, are derived from the rat liver enzyme | Ptyas dhumnades |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme | Ptyas dhumnades |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| kidney | - |
Sus scrofa | - |
| liver | - |
Homo sapiens | - |
| liver | - |
Rattus norvegicus | - |
| muscle | - |
Homo sapiens | - |
| muscle | - |
Ptyas dhumnades | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-fructose 1,6-bisphosphate + H2O | - |
Ptyas dhumnades | D-fructose 6-phosphate + phosphate | - |
? | |
| D-fructose 1,6-bisphosphate + H2O | enzyme is usually regarded as a regulatory enzyme of gluconeogenesis | Ptyas dhumnades | D-fructose 6-phosphate + phosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 36000, SDS-PAGE | Ptyas dhumnades |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0006 | - |
AMP | pH 7.5, 30°C, recombinant enzyme | Homo sapiens | |
| 0.0006 | - |
AMP | pH 7.5, 30°C, wild-type enzyme | Ptyas dhumnades | |
| 0.00085 | - |
AMP | pH 7.5, 30°C, recombinant enzyme | Ptyas dhumnades | |
| 1.2 | - |
AMP | pH 7.5, 30°C, chimeric enzyme | Ptyas dhumnades | |
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