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Literature summary extracted from

  • Mullins, L.S.; Hong, S.B.; Gibson, G.E.; Walker, H.; Stadtman, T.C.; Raushel, F.M.
    Identification of a phosphorylated enzyme intermediate in the catalytic mechanism for selenophosphate synthetase (1997), J. Am. Chem. Soc., 119, 6684-6685.
No PubMed abstract available

Organism

EC Number Organism UniProt Comment Textmining
2.7.9.3 Escherichia coli
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Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.9.3 ATP + selenide + H2O = AMP + selenophosphate + phosphate mechanism Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.9.3 ATP + selenide + H2O the gamma-phosphoryl group of the substrate ATP is cleaved in a kinetically competent reaction to form a phosphoryl-enzyme intermediate in the absence of the second substrate, selenide Escherichia coli AMP + selenophosphate + phosphate
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