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Literature summary extracted from

  • Feng, X.; Yang, C.; Zheng, W.; Wen, J.
    Structural and evolutionary characteristics of pyruvate phosphate dikinase in Giardia lamblia and other amitochondriate protozoa (2014), Chin. Med. Sci., 127, 4097-4103.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.9.1 gene PPDK, phylogenetic analysis of the N- and C-terminal sequences of PPDKs from different species, overview Zea mays
2.7.9.1 gene PPDK, phylogenetic analysis of the N- and C-terminal sequences of PPDKs from different species, overview Trypanosoma brucei
2.7.9.1 gene PPDK, phylogenetic analysis of the N- and C-terminal sequences of PPDKs from different species, overview Giardia intestinalis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.9.1 Mg2+ required Zea mays
2.7.9.1 Mg2+ required Trypanosoma brucei
2.7.9.1 Mg2+ required Giardia intestinalis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.9.1 ATP + pyruvate + phosphate Zea mays
-
 AMP + phosphoenolpyruvate + diphosphate
-
 r
2.7.9.1 ATP + pyruvate + phosphate Trypanosoma brucei
-
 AMP + phosphoenolpyruvate + diphosphate
-
 r
2.7.9.1 ATP + pyruvate + phosphate Giardia intestinalis
-
 AMP + phosphoenolpyruvate + diphosphate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.7.9.1 Giardia intestinalis P51776
-
-
2.7.9.1 Trypanosoma brucei O76283
-
-
2.7.9.1 Zea mays
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.9.1 ATP + pyruvate + phosphate
-
 Zea mays AMP + phosphoenolpyruvate + diphosphate
-
 r
2.7.9.1 ATP + pyruvate + phosphate
-
 Trypanosoma brucei AMP + phosphoenolpyruvate + diphosphate
-
 r
2.7.9.1 ATP + pyruvate + phosphate
-
 Giardia intestinalis AMP + phosphoenolpyruvate + diphosphate
-
 r

Subunits

EC Number Subunits Comment Organism
2.7.9.1 More role of the N- and C-termini on the orientation of the PPDK central domain, three-dimensional structure analysis Zea mays
2.7.9.1 More role of the N- and C-termini on the orientation of the PPDK central domain, three-dimensional structure analysis Trypanosoma brucei
2.7.9.1 More role of the N- and C-termini on the orientation of the PPDK central domain, three-dimensional structure analysis Giardia intestinalis

Synonyms

EC Number Synonyms Comment Organism
2.7.9.1 PPDK
-
 Zea mays
2.7.9.1 PPDK
-
 Trypanosoma brucei
2.7.9.1 PPDK
-
 Giardia intestinalis
2.7.9.1 pyruvate phosphate dikinase
-
 Zea mays
2.7.9.1 pyruvate phosphate dikinase
-
 Trypanosoma brucei
2.7.9.1 pyruvate phosphate dikinase
-
 Giardia intestinalis

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.9.1 ATP
-
 Zea mays
2.7.9.1 ATP
-
 Trypanosoma brucei
2.7.9.1 ATP
-
 Giardia intestinalis

General Information

EC Number General Information Comment Organism
2.7.9.1 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
2.7.9.1 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
2.7.9.1 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
2.7.9.1 additional information role of the N- and C-termini on the orientation of the PPDK central domain, three-dimensional structure analysis Zea mays
2.7.9.1 additional information role of the N- and C-termini on the orientation of the PPDK central domain, three-dimensional structure analysis Trypanosoma brucei
2.7.9.1 additional information role of the N- and C-termini on the orientation of the PPDK central domain, three-dimensional structure analysis Giardia intestinalis
2.7.9.1 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
2.7.9.1 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
2.7.9.1 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