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Information on EC 1.8.1.18 - NAD(P)H sulfur oxidoreductase (CoA-dependent)
for references in articles please use BRENDA:EC1.8.1.18
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EC Tree 1 Oxidoreductases
1.8 Acting on a sulfur group of donors
1.8.1 With NAD+ or NADP+ as acceptor
1.8.1.18 NAD(P)H sulfur oxidoreductase (CoA-dependent)
IUBMB Comments
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.
The enzyme appears in viruses and cellular organisms
showSynonyms
pf1186, coenzyme a-dependent nadph sulfur oxidoreductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CoA-dependent NAD(P)H: elemental sulfur (S0) oxidoreductase
-
NSR
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrogen sulfide + NAD(P)+ = sulfur + NAD(P)H + H+
-
-
-
-
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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.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
sulfur + NADH + H+
hydrogen sulfide + NAD+
Substrates: 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)
Products: -
Products: -
?
sulfur + NADPH + H+
hydrogen sulfide + NADP+
Substrates: 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)
Products: -
Products: -
?
polysulfide(n) + NADPH + H+
hydrogen sulfide + polysulfide(n-1) + NADP+
Substrates: -
Products: -
Products: -
?
polysulfide(n) + NADPH + H+
hydrogen sulfide + polysulfide(n-1) + NADP+
B2BSJ7; B2BSJ6; B2BSJ5; B2BSK0
Substrates: NADH can not replace NADPH, the purified recombinant enzyme catalyzes the reduction of polysulfide with NADPH as an electron donor and it also reduces oxygen
Products: -
Products: -
?
polysulfide(n) + NADPH + H+
hydrogen sulfide + polysulfide(n-1) + NADP+
B2BSJ7; B2BSJ6; B2BSJ5; B2BSK0
Substrates: NADH can not replace NADPH, the purified recombinant enzyme catalyzes the reduction of polysulfide with NADPH as an electron donor and it also reduces oxygen
Products: -
Products: -
?
sulfur + NAD(P)H + H+
hydrogen sulfide + NAD(P)+
Substrates: the rate of sulfide production from colloidal sulfur is linear (up to 10 min) suggesting that this is the true substrate for the enzyme. A lag phase in sulfide production would be expected if polysulfide, which is generated by the reaction of sulfide with elemental sulfur, is the natural substrate. A less-than-twofold increase in activity is observed, both at pH 7.0 and at pH 9.0, when polysulfide (11 mM) is used as the substrate compared to when elemental sulfur (6.4 g/liter) is used. Polysulfide is stable at pH 8 and readily dissociates to colloidal sulfur and sulfide at neutral pH. A much greater stimulation of activity would be observed if polysulfide is the preferred substrate, particularly at the higher pH
Products: -
Products: -
?
sulfur + NAD(P)H + H+
hydrogen sulfide + NAD(P)+
Substrates: -
Products: -
Products: -
?
sulfur + NAD(P)H + H+
hydrogen sulfide + NAD(P)+
Substrates: a catalytic cycle of TK1299 is proposed suggesting that CoA-SH acts to solubilize S(0) by forming CoA persulfides, followed by reduction of an enzyme-S-S-CoA intermediate produced after both enzymatic and non-enzymatic evolution of H2S from the CoA persulfide, with NADPH as an electron donor
Products: -
Products: -
?
additional information
?
-
Substrates: PF1186 is formerly proposed to function as a NAD(P)H-dependent CoA-S-S-CoA reductase (CoADR) gene (EC 1.8.1.14). The specific activity for CoA-S-S-CoA reduction (0.006 mol CoA-S-S-CoA reduced/min/mg) is about 20fold lower than the activity that this enzyme exhibits in the S(0) reduction assay. The formeryly reported CoADR activity represents only a partial reaction of its true physiological function, which is now proposed to be CoA-dependent S(0) reduction
Products: -
Products: -
?
additional information
?
-
-
Substrates: PF1186 is formerly proposed to function as a NAD(P)H-dependent CoA-S-S-CoA reductase (CoADR) gene (EC 1.8.1.14). The specific activity for CoA-S-S-CoA reduction (0.006 mol CoA-S-S-CoA reduced/min/mg) is about 20fold lower than the activity that this enzyme exhibits in the S(0) reduction assay. The formeryly reported CoADR activity represents only a partial reaction of its true physiological function, which is now proposed to be CoA-dependent S(0) reduction
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
sulfur + NAD(P)H + H+
hydrogen sulfide + NAD(P)+
Substrates: the rate of sulfide production from colloidal sulfur is linear (up to 10 min) suggesting that this is the true substrate for the enzyme. A lag phase in sulfide production would be expected if polysulfide, which is generated by the reaction of sulfide with elemental sulfur, is the natural substrate. A less-than-twofold increase in activity is observed, both at pH 7.0 and at pH 9.0, when polysulfide (11 mM) is used as the substrate compared to when elemental sulfur (6.4 g/liter) is used. Polysulfide is stable at pH 8 and readily dissociates to colloidal sulfur and sulfide at neutral pH. A much greater stimulation of activity would be observed if polysulfide is the preferred substrate, particularly at the higher pH
Products: -
Products: -
?
sulfur + NAD(P)H + H+
hydrogen sulfide + NAD(P)+
Substrates: a catalytic cycle of TK1299 is proposed suggesting that CoA-SH acts to solubilize S(0) by forming CoA persulfides, followed by reduction of an enzyme-S-S-CoA intermediate produced after both enzymatic and non-enzymatic evolution of H2S from the CoA persulfide, with NADPH as an electron donor
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
activity with NADH is 50% compared to the activity with NADPH
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
FAD
PF1186 is a member of a large family of flavin adenine dinucleotide (FAD)-dependent pyridine nucleotide-disulfide oxidoreductase genes
FAD
addition of FAD increases the activity, potentially reflecting the promoted formation of the active holoenzyme
FAD
B2BSJ7; B2BSJ6; B2BSJ5; B2BSK0
the purified recombinant NsoC contains one FAD cofactor per protein molecule
NADPH
activity with NADH is 50% compared to the activity with NADPH
NADPH
the enzyme exhibits activity with preference to NADPH as an electron donor, as indicated by higher specific activity with NADPH (14.0 U/mg) than with NADH (0.75 U/mg) NADH
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.35
B2BSJ7; B2BSJ6; B2BSJ5; B2BSK0
pH 8.9, 65°C, purified recombinant subunit NsoC, oxidation of NADPH in the presence of polysulfide
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65
B2BSJ7; B2BSJ6; B2BSJ5; B2BSK0
assay at, the temperature optimum of the enzyme can not be determined due to the significant thermolability of NADPH above 80°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
B2BSJ7: alpha subunit, B2BSJ6: beta subunit, B2BSJ5: gamma subunit, B2BSK0: delta subunit
B2BSJ7; B2BSJ6; B2BSJ5; B2BSK0
SwissProt
brenda
B2BSJ7: alpha subunit, B2BSJ6: beta subunit, B2BSJ5: gamma subunit, B2BSK0: delta subunit
B2BSJ7; B2BSJ6; B2BSJ5; B2BSK0
SwissProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NSR_PYRAB
Pyrococcus abyssi (strain GE5 / Orsay)
446
0
49181
Swiss-Prot
-
NSR_PYRFU
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
442
0
48720
Swiss-Prot
-
NSR_THEKO
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
442
0
48610
Swiss-Prot
-
Q5JGF8_THEKO
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
391
0
43984
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
50000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
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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 23°C
722519
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schut, G.J.; Bridger, S.L.; Adams, M.W.
Insights into the metabolism of elemental sulfur by the hyperthermophilic archaeon Pyrococcus furiosus: characterization of a coenzyme A-dependent NAD(P)H sulfur oxidoreductase
J. Bacteriol.
189
4431-4441
2007
Pyrococcus furiosus (Q8U1M0), Pyrococcus furiosus
brenda
Bridger, S.L.; Clarkson, S.M.; Stirrett, K.; DeBarry, M.B.; Lipscomb, G.L.; Schut, G.J.; Westpheling, J.; Scott, R.A.; Adams, M.W.
Deletion strains reveal metabolic roles for key elemental sulfur-responsive proteins in Pyrococcus furiosus
J. Bacteriol.
193
6498-6504
2011
Pyrococcus furiosus (Q8U1M0), Pyrococcus furiosus
brenda
Lipscomb, G.L.; Keese, A.M.; Cowart, D.M.; Schut, G.J.; Thomm, M.; Adams, M.W.; Scott, R.A.
SurR: a transcriptional activator and repressor controlling hydrogen and elemental sulphur metabolism in Pyrococcus furiosus
Mol. Microbiol.
71
332-349
2009
Pyrococcus furiosus (Q8U1M0)
brenda
Harnvoravongchai, P.; Kobori, H.; Orita, I.; Nakamura, S.; Imanaka, T.; Fukui, T.
Characterization and gene deletion analysis of four homologues of group 3 pyridine nucleotide disulfide oxidoreductases from Thermococcus kodakarensis
Extremophiles
18
603-616
2014
Thermococcus kodakarensis (Q5JGF8), Thermococcus kodakarensis (Q5JGP4), Thermococcus kodakarensis
brenda
Toth, A.; Takacs, M.; Groma, G.; Rakhely, G.; Kovacs, K.L.
A novel NADPH-dependent oxidoreductase with a unique domain structure in the hyperthermophilic Archaeon, Thermococcus litoralis
FEMS Microbiol. Lett.
282
8-14
2008
Thermococcus litoralis (B2BSJ7 and B2BSJ6 and B2BSJ5 and B2BSK0), Thermococcus litoralis DSM 5473 (B2BSJ7 and B2BSJ6 and B2BSJ5 and B2BSK0)
brenda
EXTERNAL LINKS (specific for EC-Number 1.8.1.18)
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Release 2023.1 (January 2023)
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