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Information on EC 2.8.1.5 - thiosulfate-dithiol sulfurtransferase
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2.8.1.5 thiosulfate-dithiol sulfurtransferaseIUBMB Comments
The enzyme from Chlorella shows very little activity towards monothiols such as glutathione and cysteine (cf. EC 2.8.1.3 thiosulfate---thiolsulfurtransferase). The enzyme probably transfers the sulfur atom onto one thiol group to form -S-S-, and sulfide is spontaneously expelled from this by reaction with the other thiol group. May be identical with EC 2.8.1.1 thiosulfate sulfurtransferase.
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Word Map
- 2.8.1.5
- sulfite
- h2s
- tetrathionate
-
dissimilatory
- desulfovibrio
- rhodanese
-
2.8.1.1
-
sulfur-donor
- thiosulfonate
- polysulfide
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
reductase, thiosulfate, Sft, thiosulfate reductase, TSR, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
reductase, thiosulfate
-
-
-
-
thiosulfate reductase
TSR
-
-
-
-
thiosulfate reductase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
thiosulfate + dithioerythritol = sulfite + 4,5-cis-dihydroxy-1,2-dithiacyclohexane (i.e. oxidized dithioerythritol) + sulfide
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sulfur atom transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
thiosulfate:dithioerythritol sulfurtransferase
The enzyme from Chlorella shows very little activity towards monothiols such as glutathione and cysteine (cf. EC 2.8.1.3 thiosulfate---thiolsulfurtransferase). The enzyme probably transfers the sulfur atom onto one thiol group to form -S-S-, and sulfide is spontaneously expelled from this by reaction with the other thiol group. May be identical with EC 2.8.1.1 thiosulfate sulfurtransferase.
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CAS REGISTRY NUMBER
COMMENTARY
9059-49-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
thiosulfate + 2 dithiothreitol
sulfite + dithiothreitol disulfide + sulfide
-
-
-
?
thiosulfate + dithiothreitol
sulfite + oxidized dithiothreitol + sulfide
-
-
-
-
?
thiosulfate + menaquinol
sulfite + oxidized menaquinol + sulfide
-
-
-
-
?
thiosulfate + NAD(P)H
H2S + NAD(P)+ + sulfite
thermophilic iron-oxidizing bacterium strain TI-1
-
-
-
?
thiosulfate + NADH
H2S + NAD+ + sulfite
thermophilic iron-oxidizing bacterium strain TI-1
-
-
-
-
?
thiosulfate + 2 dithioerythritol
sulfite + dithioerythritol disulfide + sulfide
-
-
-
-
?
thiosulfate + 2 dithioerythritol
sulfite + dithioerythritol disulfide + sulfide
-
-
-
-
?
thiosulfate + 2 dithioerythritol
sulfite + dithioerythritol disulfide + sulfide
-
-
-
-
?
thiosulfate + 2 dithioerythritol
sulfite + dithioerythritol disulfide + sulfide
-
-
-
?
thiosulfate + 2 dithioerythritol
sulfite + dithioerythritol disulfide + sulfide
[Chlorella] fusca 211-8b
-
-
-
?
additional information
?
-
enzyme additionally hydrolyzes ATP
-
-
?
additional information
?
-
-
ubiquinone is not an electron donor to thiosulfate reductase
-
-
?
additional information
?
-
-
enzyme also precipitates metals such as zinc, lead and cadmium as metal sulfide complexes
-
-
?
additional information
?
-
-
little activity with: glutathione, L-cysteine, beta-mercaptoethanol
-
-
?
additional information
?
-
[Chlorella] fusca 211-8b
-
little activity with: glutathione, L-cysteine, beta-mercaptoethanol
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
thiosulfate + 2 dithioerythritol
sulfite + dithioerythritol disulfide + sulfide
-
-
-
-
?
thiosulfate + 2 dithioerythritol
sulfite + dithioerythritol disulfide + sulfide
-
-
-
-
?
thiosulfate + 2 dithioerythritol
sulfite + dithioerythritol disulfide + sulfide
-
-
-
-
?
thiosulfate + 2 dithioerythritol
sulfite + dithioerythritol disulfide + sulfide
-
-
-
-
?
thiosulfate + 2 dithioerythritol
sulfite + dithioerythritol disulfide + sulfide
[Chlorella] fusca 211-8b
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3,3',4',5-tetrachlorosalicylanilide
-
sulfide production is nearly completely inhibited (less than 5% residual activity) when low concentrations of 3,3',4',5-tetrachlorosalicylanilide is added
4-chloromercuribenzene sufonic acid
thermophilic iron-oxidizing bacterium strain TI-1
-
strong inhibition at 0.1 mM
carbonyl cyanide-3-chlorophenylhydrazone
-
sulfide production is nearly completely inhibited (less than 5% residual activity) when low concentrations of the protonophore carbonyl cyanide-3-chlorophenylhydrazone is added
carbonyl cyanide-4-trifluoromethoxyphenylhydrazone
-
sulfide production is nearly completely inhibited (less than 5% residual activity) when low concentrations of carbonyl cyanide-4-trifluoromethoxyphenylhydrazone is added
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.54
dithioerythritol
-
pH 9, 37°C, with thiosulfate as second substrate, isoenzyme TSR II
3.1
dithioerythritol
-
pH 9, 37°C, with thiosulfate as second substrate, isoenzyme TSR I
0.156
thiosulfate
-
pH 9, 37°C, with dithioerythritol as second substrate, isoenzyme TSR II
0.164
thiosulfate
-
pH 9, 37°C, with dithioerythritol as second substrate, isoenzyme TSR I
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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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). A0A0H3AAY6_DESVV
Desulfovibrio vulgaris subsp. vulgaris (strain DP4)
698
0
76282
TrEMBL
-
E1SPL6_FERBD
Ferrimonas balearica (strain DSM 9799 / CCM 4581 / KCTC 23876 / PAT)
190
0
20986
TrEMBL
-
K4LBV6_THEPS
Thermacetogenium phaeum (strain ATCC BAA-254 / DSM 26808 / PB)
732
0
82512
TrEMBL
-
L0FBP2_DESDL
Desulfitobacterium dichloroeliminans (strain LMG P-21439 / DCA1)
190
0
20626
TrEMBL
-
M1P6T7_DESSD
Desulfocapsa sulfexigens (strain DSM 10523 / SB164P1)
704
0
79562
TrEMBL
-
K4LE72_THEPS
Thermacetogenium phaeum (strain ATCC BAA-254 / DSM 26808 / PB)
728
0
81569
TrEMBL
-
I3RJK8_PHACH
181
0
20723
TrEMBL
Mitochondrion (Reliability: 1)
E1SPL5_FERBD
Ferrimonas balearica (strain DSM 9799 / CCM 4581 / KCTC 23876 / PAT)
759
0
82517
TrEMBL
-
I3XUI8_SULBS
Sulfurospirillum barnesii (strain ATCC 700032 / DSM 10660 / SES-3)
189
0
21308
TrEMBL
-
I3XUI7_SULBS
Sulfurospirillum barnesii (strain ATCC 700032 / DSM 10660 / SES-3)
757
0
84489
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
thermophilic iron-oxidizing bacterium strain TI-1
-
homotetramer, 4 * 58000, SDS-PAGE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C137A
complete loss of both sulfurtransferase and ATPase activity
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is more stable in phosphate buffer than in Tris, borate or triethanolamine buffer
enzyme is more stable in phosphate buffer than in Tris, borate or triethanolamine buffer
-
enzyme is more stable in phosphate buffer than in Tris, borate or triethanolamine buffer
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schmidt, A.; Erdle, I.; Gamon, B.
Isolation and characterization of thiosulfate reductases from the green alga Chlorella fusca
Planta
162
243-249
1984
[Chlorella] fusca, [Chlorella] fusca 211-8b
brenda
Akagi, J.M.; Drake, H.L.; Kim, J.H.; Gevertz, D.
Thiosulfate and trithionate reductases
Methods Enzymol.
243
260-270
1994
Desulfotomaculum nigrificans, Desulfovibrio vulgaris
-
brenda
Bagchi, D.; Verma, D.
Partial purification and regulation of sulfur metabolizing enzymes in a cyanobacterium Phormidium uncinatum
Indian J. Exp. Biol.
35
876-880
1997
Phormidium uncinatum
-
brenda
Bang, S.W.; Clark, D.S.; Keasling, J.D.
Cadmium, lead, and zinc removal by expression of the thiosulfate reductase gene from Salmonella typhimurium in Escherichia coli
Biotechnol. Lett.
22
1331-1335
2000
Salmonella enterica subsp. enterica serovar Typhimurium
-
brenda
Sugio, T.; Kishimoto, K.; Oda, K.
Thiosulfate reductase from a moderately thermophilic iron-oxidizing bacterium, strain TI-1: purification and characterization
Biosci. Biotechnol. Biochem.
61
470-474
1997
thermophilic iron-oxidizing bacterium strain TI-1
-
brenda
Stoffels, L.; Krehenbrink, M.; Berks, B.C.; Unden, G.
Thiosulfate reduction in Salmonella enterica is driven by the proton motive force
J. Bacteriol.
194
475-485
2012
Salmonella enterica
brenda
Wang, Z.; Wang, G.; Xiang, Q.; Zhang, Y.; Wang, H.
Identification and characterization of a multi-domain sulfurtransferase in Phanerochaete chrysosporium
Biotechnol. Lett.
36
993-999
2014
Phanerochaete chrysosporium (I3RJK8)
brenda
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