Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.8.99.5 extracted from

  • Lui, S.M.; Cowan, J.A.
    Conformational gating of the dissimilatory sulfite reductase from Desulfovibrio vulgaris (Hildenborough). Synthesis, characterization, and stopped-flow kinetics studies of 1,5-IAEDANS-labeled desulfoviridin (1994), Biochemistry, 33, 11209-11216.
    View publication on PubMed
Search for more literature for 1.8.99.5

Organism

Organism UniProt Comment Textmining
Desulfovibrio vulgaris
-
-
-
Desulfovibrio vulgaris Hildenborough
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information two-state hypothesis for enzyme activity: an active form (DVa) binds and catalyzes substrate reduction, and an inactive form (DVi) exists for the resting enzyme. Only the active form of the enzyme need be considered during steady-state turnover. Determination of the rate constants defining these structural perturbations, from oxidized to reduced and reduced to oxidized states Desulfovibrio vulgaris ?
-
 ?
additional information two-state hypothesis for enzyme activity: an active form (DVa) binds and catalyzes substrate reduction, and an inactive form (DVi) exists for the resting enzyme. Only the active form of the enzyme need be considered during steady-state turnover. Determination of the rate constants defining these structural perturbations, from oxidized to reduced and reduced to oxidized states Desulfovibrio vulgaris Hildenborough ?
-
 ?