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

BRENDA support

Literature summary for 1.15.1.2 extracted from

  • Emerson, J.P.; Cabelli, D.E.; Kurtz, D.M., Jr.
    An engineered two-iron superoxide reductase lacking the [Fe(SCys)4] site retains its catalytic properties in vitro and in vivo (2003), Proc. Natl. Acad. Sci. USA, 100, 3802-3807.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.15.1.2

Protein Variants

Protein Variants Comment Organism
C13S destruction of native Fe(SCys)4 site with complete loss of its iron, no enzymic activity. Fe(NHis)4(SCys) site and protein homodimer remain intact Desulfovibrio vulgaris

Metals/Ions

Metals/Ions Comment Organism Structure
Iron
-
 Desulfovibrio vulgaris

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Desulfovibrio vulgaris in times of oxidative stress, enzyme efficiently diverts intracellular reducing equivalents to superoxide ?
-
 ?

Organism

Organism UniProt Comment Textmining
Desulfovibrio vulgaris
-
-
-

Reaction

Reaction Comment Organism Reaction ID
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin presence of Fe(NHis)4(SCys) site is sufficient to catalyze reduction of the intracellular superoxide to nonlethal levels Desulfovibrio vulgaris
a
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin steady state kinetics, diffusion-controlled reaction of reduced enzyme with superoxide is the slowest process during turnover, neither ligation nor deligation of the active site carboxylate limits turnover rate Desulfovibrio vulgaris
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information in times of oxidative stress, enzyme efficiently diverts intracellular reducing equivalents to superoxide Desulfovibrio vulgaris ?
-
 ?