BRENDA - Enzyme Database show
show all sequences of 2.7.11.32

Regulation of C4 photosynthesis: Purification and properties of the protein catalyzing ADP-mediated inactivation and Pi-mediated activation of pyruvate,Pi dikinase

Burnell, J.; Hatch, M.; Arch. Biochem. Biophys. 237, 490-503 (1985)

Data extracted from this reference:

General Stability
General Stability
Organism
stabilized at 25°C by phosphate, ATP, Blue Dextran and Cibacron blue
Zea mays
Inhibitors
Inhibitors
Commentary
Organism
Structure
ADP-beta-S
competitive to ADP
Zea mays
pyruvate,Pi dikinase phosphorylated at a Thr residue
competitive to ADP; competitive to substrate pyruvate,Pi dikinase
Zea mays
[pyruvate,Pi dikinase]phosphate
competitive to substrate pyruvate,Pi dikinase; noncompetitive to ADP
Zea mays
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0012
-
pyruvate,Pi dikinase
pyruvate,Pi dikinase phosphorylated at a His residue, pH 8.3, temperature not specified in the publication
Zea mays
0.052
-
ADP
pH 8.3, temperature not specified in the publication
Zea mays
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
-
Zea mays
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
45000
-
x * 45000, SDS-PAGE
Zea mays
90000
-
pH 7.5, gel filtration
Zea mays
180000
-
pH 8.3, gel filtration
Zea mays
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Zea mays
-
cv. Dekalb XL81
-
Purification (Commentary)
Commentary
Organism
ammonium sulfate precipitation, dye ligand chromatography (agarose-Blue Dextran), gel filtration
Zea mays
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
pyruvate,Pi dikinase + ADP
substrate pyruvate,Pi dikinase is phosphorylated at a His residue and active; CDP shows 40% activity, GDP 35% activity and UDP 0% activity in comparison with ADP
721404
Zea mays
[pyruvate,Pi dikinase]phosphate + AMP
phosphorylated at a Thr residue, inactive
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 45000, SDS-PAGE
Zea mays
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.1
-
broad optimum pH 7.8-8.4, 68% activity at pH 7.2
Zea mays
General Stability (protein specific)
General Stability
Organism
stabilized at 25°C by phosphate, ATP, Blue Dextran and Cibacron blue
Zea mays
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
ADP-beta-S
competitive to ADP
Zea mays
pyruvate,Pi dikinase phosphorylated at a Thr residue
competitive to ADP; competitive to substrate pyruvate,Pi dikinase
Zea mays
[pyruvate,Pi dikinase]phosphate
competitive to substrate pyruvate,Pi dikinase; noncompetitive to ADP
Zea mays
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0012
-
pyruvate,Pi dikinase
pyruvate,Pi dikinase phosphorylated at a His residue, pH 8.3, temperature not specified in the publication
Zea mays
0.052
-
ADP
pH 8.3, temperature not specified in the publication
Zea mays
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
-
Zea mays
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
45000
-
x * 45000, SDS-PAGE
Zea mays
90000
-
pH 7.5, gel filtration
Zea mays
180000
-
pH 8.3, gel filtration
Zea mays
Purification (Commentary) (protein specific)
Commentary
Organism
ammonium sulfate precipitation, dye ligand chromatography (agarose-Blue Dextran), gel filtration
Zea mays
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
pyruvate,Pi dikinase + ADP
substrate pyruvate,Pi dikinase is phosphorylated at a His residue and active; CDP shows 40% activity, GDP 35% activity and UDP 0% activity in comparison with ADP
721404
Zea mays
[pyruvate,Pi dikinase]phosphate + AMP
phosphorylated at a Thr residue, inactive
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 45000, SDS-PAGE
Zea mays
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.1
-
broad optimum pH 7.8-8.4, 68% activity at pH 7.2
Zea mays
Other publictions for EC 2.7.11.32
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
739352
Chen
Posttranslational modification ...
Zea mays
Plant Physiol.
165
534-549
2014
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723426
Astley
The pyruvate, orthophosphate d ...
Arabidopsis thaliana
Plant J.
68
1070-1080
2011
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694671
Chastain
The pyruvate, orthophosphate d ...
Arabidopsis thaliana
Plant J.
53
854-863
2008
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671766
Burnell
Cloning and expression of maiz ...
Zea mays
Biochem. Biophys. Res. Commun.
345
675-680
2006
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676721
Chastain
Posttranslational regulation o ...
Oryza sativa
Planta
224
924-934
2006
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645466
Chastain
-
Regulation of pyruvate, orthop ...
Zea mays
Plant Physiol. Biochem.
41
523-532
2003
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645460
Chastain
Further analysis of maize C(4) ...
Zea mays
Arch. Biochem. Biophys.
375
165-170
2000
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723347
Chastain
Maize recombinant C4-pyruvate, ...
Zea mays
Photosyn. Res.
49
83-89
1996
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722587
Roeske
Sequence of the phosphothreony ...
Zea mays
J. Biol. Chem.
263
6683-6687
1988
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721518
Budde
Substrate specificity and regu ...
Zea mays
Biochem. J.
236
579-584
1986
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721404
Burnell
Regulation of C4 photosynthesi ...
Zea mays
Arch. Biochem. Biophys.
237
490-503
1985
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721403
Burnell
Regulation of C4 photosynthesi ...
Zea mays
Arch. Biochem. Biophys.
231
175-182
1984
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