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Literature summary for 1.2.99.7 extracted from

  • Marangon, J.; Correia, H.D.; Brondino, C.D.; Moura, J.J.; Romao, M.J.; Gonzalez, P.J.; Santos-Silva, T.
    Kinetic and structural studies of aldehyde oxidoreductase from Desulfovibrio gigas reveal a dithiolene-based chemistry for enzyme activation and inhibition by H(2)O(2) (2013), PLoS ONE, 8, e83234.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
kinetic and X-ray crystallographic study, structures of inactive and activated enzyme. Activation/inactivation is governed by the oxidation state of the dithiolene moiety of the pyranopterin cofactor. Incubation with dithionite plus sulfide in the presence of dioxygen produces hydrogen peroxide not associated with the enzyme activation. The peroxide molecule coordinates to molybdenum in a ny2 fashion inhibiting the enzyme activity Megalodesulfovibrio gigas

Metals/Ions

Metals/Ions Comment Organism Structure
Molybdenum
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Megalodesulfovibrio gigas

Organism

Organism UniProt Comment Textmining
Megalodesulfovibrio gigas Q46509
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