Information on EC 1.8.1.18 - NAD(P)H sulfur oxidoreductase (CoA-dependent)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.8.1.18
-
RECOMMENDED NAME
GeneOntology No.
NAD(P)H sulfur oxidoreductase (CoA-dependent)
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrogen sulfide + NAD(P)+ = sulfur + NAD(P)H + H+
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
sulfate reduction
-
-
SYSTEMATIC NAME
IUBMB Comments
hydrogen sulfide:NAD(P)+ oxidoreductase (CoA-dependent)
This FAD-dependent enzyme, characterized from the archaeon Pyrococcus furiosus, is responsible for NAD(P)H-linked sulfur reduction. The activity with NADH is about half of that with NADPH. The reaction is dependent on CoA, although the nature of this dependency is not well understood.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
B2BSJ7: alpha subunit, B2BSJ6: beta subunit, B2BSJ5: gamma subunit, B2BSK0: delta subunit
B2BSJ7 and B2BSJ6 and B2BSJ5 and B2BSK0
SwissProt
Manually annotated by BRENDA team
B2BSJ7: alpha subunit, B2BSJ6: beta subunit, B2BSJ5: gamma subunit, B2BSK0: delta subunit
B2BSJ7 and B2BSJ6 and B2BSJ5 and B2BSK0
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
the growth of the NADPH sulfur oxidoreductase deletion strain (NSR1) is unaffected, indicating that NSR is not essential for energy conservation during S(0) reduction. Two sulfide dehydrogenase isoenzymes provide a compensatory NADPH-dependent S(0) reduction system
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
polysulfide(n) + NADPH + H+
hydrogen sulfide + polysulfide(n-1) + NADP+
show the reaction diagram
sulfur + NAD(P)H + H+
hydrogen sulfide + NAD(P)+
show the reaction diagram
sulfur + NADH + H+
hydrogen sulfide + NAD+
show the reaction diagram
colloidal sulfur generated from polysulfide is a better substrate than the elemental sulfur. The sulfur reductase activity requires anaerobic conditions (the product sulfide is oxidized by oxygen)
-
-
?
sulfur + NADPH + H+
hydrogen sulfide + NADP+
show the reaction diagram
colloidal sulfur generated from polysulfide is a better substrate than the elemental sulfur. The sulfur reductase activity requires anaerobic conditions (the product sulfide is oxidized by oxygen)
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
sulfur + NAD(P)H + H+
hydrogen sulfide + NAD(P)+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
-
activity with NADH is 50% compared to the activity with NADPH
NADPH
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CoA
activities in the presence of NADPH or NADH are completely lost in the absence of CoASH, demonstrating strict CoA-dependency of the enzyme for sulfur reduction. Km: 0.26 mM; strict CoA-dependency
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01
NADH
-
pH 7.0, 85C
0.018 - 0.087
NADPH
0.54
polysulfide(n)
B2BSJ7 and B2BSJ6 and B2BSJ5 and B2BSK0
pH 8.9, 65C
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.35
B2BSJ7 and B2BSJ6 and B2BSJ5 and B2BSK0
pH 8.9, 65C, purified recombinant subunit NsoC, oxidation of NADPH in the presence of polysulfide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
sulfide production
8.9
B2BSJ7 and B2BSJ6 and B2BSJ5 and B2BSK0
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
B2BSJ7 and B2BSJ6 and B2BSJ5 and B2BSK0
assay at, the temperature optimum of the enzyme can not be determined due to the significant thermolability of NADPH above 80C
85
-
assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
homohexamer
6 * 50000, SDS-PAGE
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
neither the native nor recombinant enzymes are oxygen sensitive, no loss of activity after exposure to air for 16 h at 23C
-
722519
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
B2BSJ7 and B2BSJ6 and B2BSJ5 and B2BSK0
more than 140fold
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
B2BSJ7 and B2BSJ6 and B2BSJ5 and B2BSK0
expression in Escherichia coli with an N-terminal His-tag
-
expression in Escherichia coli; expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in vitro SurR mediates the primary response to sulfur (S0). It acts as a transcriptional activator of NAD(P)H-dependent sulfur reductase
-
up-regulated within 10 min after the addition of elemental sulfur
-