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Literature summary extracted from

  • Kobayashi, K.; Yoshimoto, A.
    Studies on yeast sulfite reductase. IV. Structure and steady-state kinetics (1982), Biochim. Biophys. Acta, 705, 348-356.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.8.1.2 NADP+ competitive to NADPH, noncompetitive to sulfite Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.1.2 0.01
-
NADPH
-
Saccharomyces cerevisiae
1.8.1.2 0.012 0.017 sulfite
-
Saccharomyces cerevisiae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.8.1.2 116000
-
alpha2,beta2, 2 * 116000 + 2 * 167000, SDS-PAGE Saccharomyces cerevisiae
1.8.1.2 167000
-
alpha2,beta2, 2 * 116000 + 2 * 167000, SDS-PAGE Saccharomyces cerevisiae
1.8.1.2 604000
-
gel filtration Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.2 Saccharomyces cerevisiae
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.8.1.2 hydrogen sulfide + 3 NADP+ + 3 H2O = sulfite + 3 NADPH + 3 H+ ping-pong mechanism Saccharomyces cerevisiae

Subunits

EC Number Subunits Comment Organism
1.8.1.2 tetramer alpha2,beta2, 2 * 116000 + 2 * 167000, SDS-PAGE Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.2 flavin 2 FAD and 2 FMN per mol of enzyme Saccharomyces cerevisiae
1.8.1.2 heme
-
Saccharomyces cerevisiae