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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.8.1.18 - NAD(P)H sulfur oxidoreductase (CoA-dependent) and Organism(s) Thermococcus kodakarensis and UniProt Accession Q5JGP4

for references in articles please use BRENDA:EC1.8.1.18
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Thermococcus kodakarensis
UNIPROT: Q5JGP4
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
The taxonomic range for the selected organisms is: Thermococcus kodakarensis
The enzyme appears in selected viruses and cellular organisms
Synonyms
pf1186, coenzyme a-dependent nadph sulfur oxidoreductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CoA-dependent NAD(P)H: elemental sulfur (S0) oxidoreductase
-
NAD(P)H: S0 oxidoreductase
-
CoA-dependent NAD(P)H: elemental sulfur (S0) oxidoreductase
-
NAD(P)H: S0 oxidoreductase
-
PATHWAY SOURCE
PATHWAYS
-
-
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.
SUBSTRATE
PRODUCT                       
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
sulfur + NAD(P)H + H+
hydrogen sulfide + NAD(P)+
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
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
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CoA
activities in the presence of NADPH or NADH are completely lost in the absence of CoA–SH, demonstrating strict CoA-dependency of the enzyme for sulfur reduction. KM: 0.26 mM
FAD
addition of FAD increases the activity, potentially reflecting the promoted formation of the active holoenzyme
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
CoA
strict CoA-dependency
NADPH
preference for NADPH as an electron donor
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CoA
activities in the presence of NADPH or NADH are completely lost in the absence of CoA–SH, demonstrating strict CoA-dependency of the enzyme for sulfur reduction. Km: 0.26 mM
CoA
strict CoA-dependency
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
6 * 50000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homohexamer
6 * 50000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team