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Information on EC 2.7.11.33 - [pyruvate, water dikinase] kinase for references in articles please use BRENDA:EC2.7.11.33Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The expected taxonomic range for this enzyme is: Escherichia coli
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[pyruvate, water dikinase] kinase
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ADP + [pyruvate, water dikinase] = AMP + [pyruvate, water dikinase] phosphate
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ADP:[pyruvate, water dikinase] phosphotransferase
The enzyme from the bacterium Escherichia coli is bifunctional and catalyses both the phosphorylation and dephosphorylation of EC 2.7.9.2, pyruvate, water dikinase. cf. EC 2.7.4.28, ([pyruvate, water dikinase] phosphate) phosphotransferase [1]. The enzyme is specific for a reaction intermediate form of EC 2.7.9.2, where it phosphorylates an active site histidine [1]. It has no activity toward EC 2.7.9.1 pyruvate, phosphate dikinase (cf. EC 2.7.11.32, [pyruvate, phosphate dikinase] kinase).
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bifunctional ADP-dependent kinase - Pi-dependent pyrophosphorylase
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PEP synthetase regulatory protein
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brenda
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phosphoenolpyruvate synthase + ADP
[phosphoenolpyruvate synthase]phosphate + AMP
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His residue phosphorylated (active)
His and Thr residues phosphorylated (inactive)
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25000
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4 * 25000, gel filtration, SDS-PAGE
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homotetramer
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4 * 25000, gel filtration, SDS-PAGE
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purified protein stable for at least a week when stored on ice
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immobilized metal ion affinity chromatography (Ni2+)
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His-tagged protein expressed in Escherichia coli NM522
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Burnell, J.
Cloning and characterization of Escherichia coli DUF299: A bifunctional ADP-dependent kinase - Pi-dependent pyrophosphorylase from bacteria
BMC Biochem.
11
0000
2010
Escherichia coli
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