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BRENDA support

Literature summary for 2.7.9.2 extracted from

  • Harauz, G.
    Symmetry in the 2.25 MDa homomultimeric phosphoenolpyruvate synthase from Staphylothermus marinus: analyses of negatively stained preparations (1998), Micron, 29, 161-173.
No PubMed abstract available

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + pyruvate + H2O Staphylothermus marinus involved in gluconeogenesis AMP + phosphoenolpyruvate + phosphate
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r

Organism

Organism UniProt Comment Textmining
Staphylothermus marinus
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hyperthermophilic archaeon
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + pyruvate + H2O
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Staphylothermus marinus AMP + phosphoenolpyruvate + phosphate
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r
ATP + pyruvate + H2O involved in gluconeogenesis Staphylothermus marinus AMP + phosphoenolpyruvate + phosphate
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r

Subunits

Subunits Comment Organism
multimer enzyme forms an unusually large tetraeisosameric complex of 2494 kDa, structure analysis by cryoelectron micrography Staphylothermus marinus