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
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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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Engineering
Engineering on EC 1.8.1.2 - assimilatory sulfite reductase (NADPH)
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C427A
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mutation of the highly conserved cysteine 427, crucial residue for iron-sulfur cluster binding
C433A
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mutation of the highly conserved cysteine 427, crucial residue for iron-sulfur cluster binding
C472A
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mutation of the highly conserved cysteine 427, crucial residue for iron-sulfur cluster binding
C476A
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mutation of the highly conserved cysteine 427, crucial residue for iron-sulfur cluster binding
F437A
the variant is more reactive when reduced chemically, likely because the chemical reductant has superior access to the active site, the variant is also more active as part of the dodecamer
F496D
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variants of the flavin binding reductase (SiRFP) shows reduced activity compared to that of the wild-type enzyme
M444A
the variant is more reactive when reduced chemically, likely because the chemical reductant has superior access to the active site, the variant is not more active as part of the dodecamer
V500D
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variant of the flavin binding reductase (SiRFP) binds NADP+ with an affinity similar to that of wild-type enzyme. The variant is reduced by about 60% in its ability to transfer electrons to the iron-containing oxidase (SiRHP).
Y101A
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variants of the flavin binding reductase (SiRFP) shows reduced activity compared to that of the wild-type enzyme
F437A
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the variant is more reactive when reduced chemically, likely because the chemical reductant has superior access to the active site, the variant is also more active as part of the dodecamer
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M444A
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the variant is more reactive when reduced chemically, likely because the chemical reductant has superior access to the active site, the variant is not more active as part of the dodecamer
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additional information
construction of large scale amounts of random T-DNA-inserted mutants, identification of a knockout mutant DELTAMet10
additional information
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construction of large scale amounts of random T-DNA-inserted mutants, identification of a knockout mutant DELTAMet10
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additional information
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construction of large scale amounts of random T-DNA-inserted mutants, identification of a knockout mutant DELTAMet10
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additional information
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4 mutants blocked in sulfite reduction, 3 containing only FMN, 1 lacking both flavins