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Literature summary for 1.13.11.55 extracted from

  • Sato, Y.; Yabuki, T.; Adachi, N.; Moriya, T.; Arakawa, T.; Kawasaki, M.; Yamada, C.; Senda, T.; Fushinobu, S.; Wakagi, T.
    Crystallographic and cryogenic electron microscopic structures and enzymatic characterization of sulfur oxygenase reductase from Sulfurisphaera tokodaii (2020), J. Struct. Biol., X 4, 100030 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Sulfurisphaera tokodaii

Crystallization (Commentary)

Crystallization (Comment) Organism
structure at 1.73 A resolution. At the catalytic center, iron is ligated to His86, His90, Glu114, and two water molecules. Three conserved cysteines in the cavity are located 9.5-13 A from the iron and are observed as free thiol forms. The iron and Cys31 are essential Sulfurisphaera tokodaii

Protein Variants

Protein Variants Comment Organism
C101A about 10% residual activtiy for both oxygenase and reductase activity Sulfurisphaera tokodaii
C104A about 10% residual activtiy for both oxygenase and reductase activity Sulfurisphaera tokodaii
C31A complete loss of activity Sulfurisphaera tokodaii
E114A complete loss of activity Sulfurisphaera tokodaii
H86A complete loss of activity Sulfurisphaera tokodaii
H90A complete loss of activity Sulfurisphaera tokodaii

Inhibitors

Inhibitors Comment Organism Structure
Cu2+
-
Sulfurisphaera tokodaii
cyanide 1 mM, 71% inhibition Sulfurisphaera tokodaii
dithiothreitol inhibits both reactions Sulfurisphaera tokodaii
Fe2+ inhibits oxygenase reaction Sulfurisphaera tokodaii
Fe3+ inhibits oxygenase reaction Sulfurisphaera tokodaii
Hg2+
-
Sulfurisphaera tokodaii
iodoacetic acid inhibits both reactions Sulfurisphaera tokodaii
additional information not inhibitory: sodium azide Sulfurisphaera tokodaii
N-ethylmaleimide inhibits both reactions Sulfurisphaera tokodaii
PCMB inhibits both reactions Sulfurisphaera tokodaii

Metals/Ions

Metals/Ions Comment Organism Structure
Iron at the catalytic center, iron is ligated to His86, His90, Glu114, and two water molecules Sulfurisphaera tokodaii
Zn2+ activating Sulfurisphaera tokodaii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
539000
-
gel filtration Sulfurisphaera tokodaii

Organism

Organism UniProt Comment Textmining
Sulfurisphaera tokodaii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant protein, by heat treatment and chromatography steps with four different columns Sulfurisphaera tokodaii

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.95
-
80°C, pH 6, production of hydrogen sulfite Sulfurisphaera tokodaii
10.5
-
80°C, pH 6, oxygenase reaction Sulfurisphaera tokodaii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3S + 3H2O
-
Sulfurisphaera tokodaii HSO3- + 2HS- + 3H+
-
?
4 sulfur + 4 H2O + O2
-
Sulfurisphaera tokodaii 2 hydrogen sulfide + 2 sulfite
-
?

Subunits

Subunits Comment Organism
multimer 15-16 * 38000, SDS-PAGE, 15-16 * 35700, calculated from sequence Sulfurisphaera tokodaii

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
80
-
30 min, the remaining oxygenase and reductase activities are approximately 40% and 90%, respectively Sulfurisphaera tokodaii