Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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

Reaction

hydrogen sulfide
+ 3 NADP+ + 3 H2O =
sulfite
+ 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

     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.1 With NAD+ or NADP+ as acceptor
                1.8.1.2 assimilatory sulfite reductase (NADPH)

Engineering

Engineering on EC 1.8.1.2 - assimilatory sulfite reductase (NADPH)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C427A
-
mutation of the highly conserved cysteine 427, crucial residue for iron-sulfur cluster binding
C433A
-
mutation of the highly conserved cysteine 427, crucial residue for iron-sulfur cluster binding
C472A
-
mutation of the highly conserved cysteine 427, crucial residue for iron-sulfur cluster binding
C476A
-
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
-
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
R83S
mutant is unable to bind flavoprotein SiRFP
V500D
-
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
-
variants of the flavin binding reductase (SiRFP) shows reduced activity compared to that of the wild-type enzyme
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
-
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
-
A979T
-
Met5p mutant
E1356K
-
Met5p mutant
E929K
-
Met10p mutant
G1115D
-
Met5p mutant
L606F
-
Met10p mutant
T990I
-
Met10p mutant
T997I
-
Met10p mutant
W59X
-
Met10p mutant
W841X
-
Met10p mutant
additional information