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Literature summary extracted from

  • Chastain, C.J.; Failing, C.J.; Manandhar, L.; Zimmerman, M.A.; Lakner, M.M.; Nguyen, T.H.
    Functional evolution of C4 pyruvate, orthophosphate dikinase (2011), J. Exp. Bot., 62, 3083-3091.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.9.1 diphosphate competitive inhibitor Zea mays

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.9.1 0.178
-
 pyruvate at pH 7.0 and 30°C Zea mays
2.7.9.1 0.194
-
 phosphoenolpyruvate at pH 7.0 and 30°C Zea mays

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.9.1 Mg2+ the enzyme requires Mg2+ for oligomerization Zea mays
2.7.9.1 NH4+ the enzyme requires NH4+ as a cofactor for optimal catalysis Zea mays

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.9.1 95000
-
 4 * 95000, the enzyme is maximally active as a homotetramer and is inactive in the dimeric and monomeric forms Zea mays

Organism

EC Number Organism UniProt Comment Textmining
2.7.9.1 Zea mays
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.9.1 phosphoprotein the PPDK regulatory protein catalyses this light-dependent regulation of the enzyme by reversible phosphorylation of the active-site Thr456 residue Zea mays

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.9.1 seed
-
 Zea mays
-

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
2.7.9.1 homotetramer 4 * 95000, the enzyme is maximally active as a homotetramer and is inactive in the dimeric and monomeric forms Zea mays

Synonyms

EC Number Synonyms Comment Organism
2.7.9.1 PPDK
-
 Zea mays
2.7.9.1 pyruvate, orthophosphate dikinase
-
 Zea mays

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.9.1 7
-
 the pyruvate-forming reaction is strongly favoured at pH 7.0 Zea mays
2.7.9.1 8.3
-
 the competency of the enzyme in catalyzing its phosphoenolpyruvate-forming reaction at pH 7.0 is dramatically reduced, having only 6% of the rate at pH 8.3 Zea mays

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.7.9.1 7 8.3 the competency of the enzyme in catalyzing its phosphoenolpyruvate-forming reaction at pH 7.0 is dramatically reduced, having only 6% of the rate at pH 8.3 Zea mays

Expression

EC Number Organism Comment Expression
2.7.9.1 Zea mays in the C4 pathway, enzyme activity is strictly regulated in an up/down manner by the level of incident light up

General Information

EC Number General Information Comment Organism
2.7.9.1 metabolism the enzyme plays a controlling role in the phosphoenolpyruvate-regeneration phase of the C4 photosynthetic pathway Zea mays