1.8.1.2: assimilatory sulfite reductase (NADPH)
This is an abbreviated version!
For detailed information about assimilatory sulfite reductase (NADPH), go to the full flat file.
Word Map on EC 1.8.1.2
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1.8.1.2
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sulfur
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siroheme
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dissimilatory
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hemoprotein
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desulfovibrio
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sulfate-reducing
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thiosulfate
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six-electron
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desulfoviridin
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o-acetylserine
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sulfhydrylase
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dsrab
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sulfurylase
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5'-phosphosulfate
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hildenborough
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ferredoxin-dependent
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o-acetyl-l-serine
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exchange-coupled
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desulfotomaculum
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brewing
-
nutrition
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medicine
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synthesis
- 1.8.1.2
- sulfur
- siroheme
-
dissimilatory
- hemoprotein
- desulfovibrio
-
sulfate-reducing
- thiosulfate
-
six-electron
-
desulfoviridin
- o-acetylserine
-
sulfhydrylase
- dsrab
-
sulfurylase
- 5'-phosphosulfate
- hildenborough
-
ferredoxin-dependent
- o-acetyl-l-serine
-
exchange-coupled
- desulfotomaculum
- brewing
- nutrition
- medicine
- synthesis
Reaction
+ 3 NADP+ + 3 H2O = + 3 NADPH + 3 H+
Synonyms
CNG03990, coenzyme F420-dependent sulfite reductase, CysI, CysIJ, desulforubidin, EC 1.8.99.1, Fsr, H2S-NADP oxidoreductase, MET10, NADPH-dependent assimilatory sulfite reductase, NADPH-dependent sulfite reductase, NADPH-sulfite reductase, reductase, sulfite (reduced nicotinamide adenine dinucleotide phosphate), SIR, SIR-FP, SIR-HP, SiR/SiRHP, SIRHP, sulfite reductase, sulfite reductase hemo-subunit
ECTree
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Cofactor
Cofactor on EC 1.8.1.2 - assimilatory sulfite reductase (NADPH)
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FAD
flavoprotein. The electron transfer occurs via multiple pathways, bypassing the need for electrons to move intra-molecularly from the NADH to the FAD to the FMN and then in cis to SiRHP. In this way, SiR effectively raises the local concentration of electrons relative to SiRHP active sites to facilitate the full six electron reduction of SO32- to S2-
flavin
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treatment with ammonium sulfate causes dissociation of FMN but retetion of FAD and heme
flavin
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4 FAD and 4 FMN per mol of enzyme
flavin
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treatment with p-chloromercuriphenylsulfonate causes dissociation of FMN but retetion of FAD and heme
heme
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tetrahydroporphyrin of isobacteriochlorin type with eight carboxylic side chains
heme
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2 fully metallated sirohemes per mol of enzyme, S=9/2 EPR iron-sulfur cluster
heme
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hemoprotein subunit contains one siroheme and one Fe4S4 center per polypeptide
siroheme
siroheme-containing subunit of the multimeric hemoflavoprotein NADPH-dependent sulfite reductase. Siroheme is an iron-containing isobacteriochlorin, that does not work alone but is covalently coupled to a Fe4S4 cluster through one of the cluster's ligands