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Literature summary for 2.7.9.1 extracted from

  • Appanna, V.P.; Alhasawi, A.A.; Auger, C.; Thomas, S.C.; Appanna, V.D.
    Phospho-transfer networks and ATP homeostasis in response to an ineffective electron transport chain in Pseudomonas fluorescens (2016), Arch. Biochem. Biophys., 606, 26-33.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
AMP + phosphoenolpyruvate + diphosphate Pseudomonas fluorescens the enzyme is dependent on AMP in the phosphotransfer networks ATP + pyruvate + phosphate
-
r
AMP + phosphoenolpyruvate + diphosphate Pseudomonas fluorescens ATCC 13525 the enzyme is dependent on AMP in the phosphotransfer networks ATP + pyruvate + phosphate
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r

Organism

Organism UniProt Comment Textmining
Pseudomonas fluorescens
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Pseudomonas fluorescens ATCC 13525
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
AMP + phosphoenolpyruvate + diphosphate
-
Pseudomonas fluorescens ATP + pyruvate + phosphate
-
r
AMP + phosphoenolpyruvate + diphosphate the enzyme is dependent on AMP in the phosphotransfer networks Pseudomonas fluorescens ATP + pyruvate + phosphate
-
r
AMP + phosphoenolpyruvate + diphosphate
-
Pseudomonas fluorescens ATCC 13525 ATP + pyruvate + phosphate
-
r
AMP + phosphoenolpyruvate + diphosphate the enzyme is dependent on AMP in the phosphotransfer networks Pseudomonas fluorescens ATCC 13525 ATP + pyruvate + phosphate
-
r

Synonyms

Synonyms Comment Organism
PPDK
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Pseudomonas fluorescens
pyruvate orthophosphate dikinase
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Pseudomonas fluorescens

Cofactor

Cofactor Comment Organism Structure
AMP
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Pseudomonas fluorescens
ATP
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Pseudomonas fluorescens

Expression

Organism Comment Expression
Pseudomonas fluorescens enzyme PPDK is upregulated in Pseudomonas fluorescens cells exposed to H2O2 or nitrosative stress up

General Information

General Information Comment Organism
metabolism despite the diminished activities of enzymes involved in the TCA cycle and in the electron transport chain, the ATP levels do not appear to be significantly affected in cells stressed by the presence of hydrogen peroxide and nitrosative stress. A phospho-transfer networks mediated by acetate kinase, adenylate kinase, and nucleoside diphosphate kinase are involved in maintaining ATP homeostasis in the oxidatively challenged cells. This phospho-relay machinery orchestrated by substrate-level phosphorylation is aided by the upregulation in the activities of such enzymes like phosphoenolpyruvate carboxylase, pyruvate orthophosphate dikinase, and phosphoenolpyruvate synthase. The enhanced production of phosphoenolpyruvate and pyruvate further fuel the synthesis of ATP. The phospho-transfer system enables the organism to generate ATP irrespective of the carbon source utilized, and this metabolic reconfiguration enables the organism to fulfill its ATP need in an O2-independent manner by utilizing an intricate phospho-wire module aimed at maximizing the energy potential of PEP with the participation of AMP. While PPDK helps synthesize ATP from of phosphoenolpyruvate in the presence of AMP and diphosphate, phosphoenolpyruvate synthase produces the high energy triphosphate with the participation of AMP and phosphate. These two enzymes are markedly increased in activity in the bacteria grown in the stressed conditions. The two AMP-utilizing enzymes provide a more effective route to ATP than the traditional ADP-dependent pyruvate kinase Pseudomonas fluorescens
physiological function enzyme PPDK is involved in ATP homeostasis in Pseudomonas fluorescens, overview Pseudomonas fluorescens