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Literature summary for 2.7.9.1 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

Inhibitors Comment Organism Structure
diphosphate competitive inhibitor Zea mays

KM Value [mM]

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

Metals/Ions

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Zea mays
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
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

Source Tissue Comment Organism Textmining
seed
-
Zea mays
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
PPDK
-
Zea mays
pyruvate, orthophosphate dikinase
-
Zea mays

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
the pyruvate-forming reaction is strongly favoured at pH 7.0 Zea mays
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

pH Minimum pH Maximum Comment Organism
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

Organism Comment Expression
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

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