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Literature summary for 2.7.9.1 extracted from
- Structural and evolutionary characteristics of pyruvate phosphate dikinase in Giardia lamblia and other amitochondriate protozoa (2014), Chin. Med. Sci., 127, 4097-4103.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene PPDK, phylogenetic analysis of the N- and C-terminal sequences of PPDKs from different species, overview | Zea mays |
| gene PPDK, phylogenetic analysis of the N- and C-terminal sequences of PPDKs from different species, overview | Trypanosoma brucei |
| gene PPDK, phylogenetic analysis of the N- and C-terminal sequences of PPDKs from different species, overview | Giardia intestinalis |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Zea mays |  |
| Mg2+ | required | Trypanosoma brucei | |
| Mg2+ | required | Giardia intestinalis | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + pyruvate + phosphate | Zea mays | - |
AMP + phosphoenolpyruvate + diphosphate | - |
r | |
| ATP + pyruvate + phosphate | Trypanosoma brucei | - |
AMP + phosphoenolpyruvate + diphosphate | - |
r | |
| ATP + pyruvate + phosphate | Giardia intestinalis | - |
AMP + phosphoenolpyruvate + diphosphate | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Giardia intestinalis | P51776 | - |
- |
| Trypanosoma brucei | O76283 | - |
- |
| Zea mays | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + pyruvate + phosphate | - |
Zea mays | AMP + phosphoenolpyruvate + diphosphate | - |
r | |
| ATP + pyruvate + phosphate | - |
Trypanosoma brucei | AMP + phosphoenolpyruvate + diphosphate | - |
r | |
| ATP + pyruvate + phosphate | - |
Giardia intestinalis | AMP + phosphoenolpyruvate + diphosphate | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | role of the N- and C-termini on the orientation of the PPDK central domain, three-dimensional structure analysis | Zea mays |
| More | role of the N- and C-termini on the orientation of the PPDK central domain, three-dimensional structure analysis | Trypanosoma brucei |
| More | role of the N- and C-termini on the orientation of the PPDK central domain, three-dimensional structure analysis | Giardia intestinalis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PPDK | - |
Zea mays |
| PPDK | - |
Trypanosoma brucei |
| PPDK | - |
Giardia intestinalis |
| pyruvate phosphate dikinase | - |
Zea mays |
| pyruvate phosphate dikinase | - |
Trypanosoma brucei |
| pyruvate phosphate dikinase | - |
Giardia intestinalis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Zea mays | |
| ATP | - |
Trypanosoma brucei | |
| ATP | - |
Giardia intestinalis | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | three-dimensional modeling of PPDKs from divergent organisms and comparion of the orientation of the phosphorylatable histidine residue within the central domain of PPDKs. These PPDKs are compared using a maximum-likelihood tree. For PPDK from anaerobic protozoans, the central domain tilt toward the N-terminal nucleotide-binding domain, indicating that this enzyme catalyzes ATP synthesis, phylogenetic analysis of the N- and C-terminal sequences of PPDKs from different species, overview. PPDK in anaerobic organisms is functionally adapted to generate energy more efficiently in an anaerobic environment | Trypanosoma brucei |
| evolution | three-dimensional modeling of PPDKs from divergent organisms and comparion of the orientation of the phosphorylatable histidine residue within the central domain of PPDKs. These PPDKs are compared using a maximum-likelihood tree. For PPDK from Giardia, as well as from other anaerobic protozoans, the central domain tilt toward the N-terminal nucleotide-binding domain, indicating that this enzyme catalyzes ATP synthesis, phylogenetic analysis of the N- and C-terminal sequences of PPDKs from different species, overview. PPDK in anaerobic organisms, e.g. the enzyme from Giardia lamblia, is functionally adapted to generate energy more efficiently in an anaerobic environment | Giardia intestinalis |
| evolution | three-dimensional modeling of PPDKs from divergent organisms and comparion of the orientation of the phosphorylatable histidine residue within the central domain of PPDKs. These PPDKs are compared using a maximum-likelihood tree. Phylogenetic analysis of the N- and C-terminal sequences of PPDKs from different species, overview | Zea mays |
| additional information | role of the N- and C-termini on the orientation of the PPDK central domain, three-dimensional structure analysis | Zea mays |
| additional information | role of the N- and C-termini on the orientation of the PPDK central domain, three-dimensional structure analysis | Trypanosoma brucei |
| additional information | role of the N- and C-termini on the orientation of the PPDK central domain, three-dimensional structure analysis | Giardia intestinalis |
| physiological function | pyruvate phosphate dikinase reversibly catalyzes the interconversion of phosphoenolpyruvate and pyruvic acid, leading to catabolism and adenosine triphosphate (ATP) synthesis or gluconeogenesis and ATP consumption. The orientation of the phosphorylatable histidine residue within the central domain of PPDK determines whether this enzyme promotes catabolism or gluconeogenesis | Zea mays |
| physiological function | pyruvate phosphate dikinase reversibly catalyzes the interconversion of phosphoenolpyruvate and pyruvic acid, leading to catabolism and adenosine triphosphate (ATP) synthesis or gluconeogenesis and ATP consumption. The orientation of the phosphorylatable histidine residue within the central domain of PPDK determines whether this enzyme promotes catabolism or gluconeogenesis | Trypanosoma brucei |
| physiological function | pyruvate phosphate dikinase reversibly catalyzes the interconversion of phosphoenolpyruvate and pyruvic acid, leading to catabolism and adenosine triphosphate (ATP) synthesis or gluconeogenesis and ATP consumption. The orientation of the phosphorylatable histidine residue within the central domain of PPDK determines whether this enzyme promotes catabolism or gluconeogenesis | Giardia intestinalis |
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