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Literature summary for 1.8.7.1 extracted from

  • Champier, L.; Sibille, N.; Bersch, B.; Brutscher, B.; Blackledge, M.; Coves, J.
    Reactivity, secondary structure, and molecular topology of the Escherichia coli sulfite reductase flavodoxin-like domain (2002), Biochemistry, 41, 3770-3780.
    View publication on PubMed

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
18000
-
superdex-75 column, SDS-PAGE Escherichia coli
20000
-
native enzime, superdex-75 column Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
sulfite + 3 FMNH2 Escherichia coli sulfate assimilation pathway leading to the biosynthesis of organic sulfur compounds sulfide + 3 FMN + 3 H2O
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
no modification
-
Escherichia coli

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitacion, filtration on a superdex-75 column Escherichia coli

Source Tissue

Source Tissue Comment Organism Textmining
culture supernatant
-
Escherichia coli
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
SO32- + FMNH2
-
Escherichia coli S2- + FMN + H2O
-
?
sulfite + 3 FMNH2 sulfate assimilation pathway leading to the biosynthesis of organic sulfur compounds Escherichia coli sulfide + 3 FMN + 3 H2O
-
?

Subunits

Subunits Comment Organism
homooctamer alpha8 Escherichia coli

Synonyms

Synonyms Comment Organism
sulfite reductase flavoprotein component Escherichia coli

Cofactor

Cofactor Comment Organism Structure
FMN
-
Escherichia coli