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Literature summary for 1.8.1.2 extracted from

  • Murray, D.T.; Weiss, K.L.; Stanley, C.B.; Nagy, G.; Stroupe, M.E.
    Small-angle neutron scattering solution structures of NADPH-dependent sulfite reductase (2021), J. Struct. Biol., 213, 107724 .
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
sulfite + 3 NADPH + 3 H+ Escherichia coli
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hydrogen sulfide + 3 NADP+ + 3 H2O
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli W8SX42 AND P17846 W8SX42: SiRFP, sulfite reductase [NADPH] flavoprotein alpha-component (cysJ), P17846: SiRHP, sulfite reductase [NADPH] hemoprotein beta-component (cysI)
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sulfite + 3 NADPH + 3 H+
-
Escherichia coli hydrogen sulfide + 3 NADP+ + 3 H2O
-
?

Subunits

Subunits Comment Organism
dodecamer the dodecameric complex of flavoprotein reductase subunits (SiRFP) and hemoprotein oxidase subunits (SiRHP). Small-angle neutron scattering solution structures of the interaction of SiRFP show, how both SiRHP binding to, and reduction of, SiRFP positions SiRFP for electron transfer between the subunits Escherichia coli

Synonyms

Synonyms Comment Organism
NADPH-dependent sulfite reductase
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Escherichia coli
SIR
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Escherichia coli