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Information on EC 1.8.99.B1 - protein-disulfide reductase (acceptor)
for references in articles please use BRENDA:EC1.8.99.B1preliminary BRENDA-supplied EC number
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1.8.99.B1 protein-disulfide reductase (acceptor)Specify your search results
Word Map
The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
Reaction Schemes
+
oxidized acceptor
=
+
Synonyms
appdo, sso1120, aapdo, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
disulfide bond-forming enzyme
glutaredoxin related protein
PDO
protein disulfide oxidoreductase
SSO0192
SSO10610
Sso1120
SsPDO
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
protein-dithiol + oxidized acceptor = protein-disulfide + reduced acceptor
-
-
-
-
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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
dithiol peptide NRCSQGSCWN + acceptor
disulfide peptide NRCSQGSCWN + reduced acceptor
-
-
-
?
[ribonuclease A]-dithiol + oxidized acceptor
[ribonuclease A]-disulfide + reduced acceptor
insulin disulfide + reduced thioredoxin
insulin dithiol + oxidized thioredoxin
with NADPH and FAD
-
-
?
insulin disulfide + reduced thioredoxin
insulin dithiol + oxidized thioredoxin
with NADPH and FAD
-
-
?
protein-dithiol + oxidized acceptor
protein-disulfide + reduced acceptor
intracellular proteins of certain hyperthermophilic archaea are rich in disulfide bonds. Disulfide bonds stabilize many thermostable proteins
-
-
?
protein-dithiol + oxidized acceptor
protein-disulfide + reduced acceptor
the enzyme is involved in disulfide bond formation
-
-
?
protein-dithiol + oxidized acceptor
protein-disulfide + reduced acceptor
the enzyme is involved in disulfide bond formation
-
-
?
[insulin]-disulfide + reduced dithiothreitol
[insulin]-dithiol + oxidized dithiothreitol
-
-
-
?
[insulin]-disulfide + reduced dithiothreitol
[insulin]-dithiol + oxidized dithiothreitol
-
-
-
?
[insulin]-disulfide + reduced dithiothreitol
[insulin]-dithiol + oxidized dithiothreitol
-
-
-
?
[insulin]-disulfide + reduced dithiothreitol
[insulin]-dithiol + oxidized dithiothreitol
-
-
-
?
[insulin]-disulfide + reduced dithiothreitol
[insulin]-dithiol + oxidized dithiothreitol
the enzyme does not present isomerase activity
-
-
?
[insulin]-disulfide + reduced dithiothreitol
[insulin]-dithiol + oxidized dithiothreitol
the enzyme does not present isomerase activity
-
-
?
[insulin]-disulfide + reduced dithiothreitol
[insulin]-dithiol + oxidized dithiothreitol
-
-
-
?
[ribonuclease A]-dithiol + oxidized acceptor
[ribonuclease A]-disulfide + reduced acceptor
-
-
-
?
[ribonuclease A]-dithiol + oxidized acceptor
[ribonuclease A]-disulfide + reduced acceptor
-
-
-
?
additional information
?
-
the enzyme reveals an inherent glutathione-dependent thioltransferase activity
-
-
?
additional information
?
-
the enzyme reveals an inherent glutathione-dependent thioltransferase activity
-
-
?
additional information
?
-
-
the enzyme reveals an inherent glutathione-dependent thioltransferase activity
-
-
?
additional information
?
-
5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB) reduction method is used. The enzyme has reductase activity, as tested by insulin assay, but differently from the other PDOs, it does not present isomerase activity. In addition it is able to form a redox couple with the thioredoxin reductase
-
-
?
additional information
?
-
-
5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB) reduction method is used. The enzyme has reductase activity, as tested by insulin assay, but differently from the other PDOs, it does not present isomerase activity. In addition it is able to form a redox couple with the thioredoxin reductase
-
-
?
additional information
?
-
5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB) reduction method is used. The enzyme has reductase activity, as tested by insulin assay, but differently from the other PDOs, it does not present isomerase activity. In addition it is able to form a redox couple with the thioredoxin reductase
-
-
?
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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
protein-dithiol + oxidized acceptor
protein-disulfide + reduced acceptor
intracellular proteins of certain hyperthermophilic archaea are rich in disulfide bonds. Disulfide bonds stabilize many thermostable proteins
-
-
?
protein-dithiol + oxidized acceptor
protein-disulfide + reduced acceptor
the enzyme is involved in disulfide bond formation
-
-
?
protein-dithiol + oxidized acceptor
protein-disulfide + reduced acceptor
the enzyme is involved in disulfide bond formation
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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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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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
evolution
the enzyme belongs to the thioredoxin (Trx) superfamily. Its crystal structure shows differences with respect to other PDOs and an unexpected similarity with the N-terminal domain of the alkyl hydroperoxide reductase F component from Salmonella typhimurium, PDO structure comparisons
evolution
-
the enzyme belongs to the thioredoxin (Trx) superfamily. Its crystal structure shows differences with respect to other PDOs and an unexpected similarity with the N-terminal domain of the alkyl hydroperoxide reductase F component from Salmonella typhimurium, PDO structure comparisons
-
physiological function
PDOs are proteins involved in disulfide bond formation
physiological function
-
PDOs are proteins involved in disulfide bond formation
-
additional information
Sso1120 active site region structure, overview
additional information
-
Sso1120 active site region structure, overview
additional information
-
Sso1120 active site region structure, overview
-
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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). DN7D_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
64
0
7280
Swiss-Prot
-
Q97Z21_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
171
0
19931
TrEMBL
-
Q980T5_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
233
0
26033
TrEMBL
-
Q9YDZ4_AERPE
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
243
0
27334
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20995
1 * 20995, light scattering and electrospray mass spectroscopy analyses
21000
light scattering and electrospray mass spectroscopy analyses
27198
1 * 27198, calculated from sequence, gel filtration, electrospray mass spectroscopy
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
the protein consists of two homologous structural units with low sequence identity. Each unit contains a thioredoxin fold with a distinct CXXC active site motif
monomer
additional information
monomer
1 * 27198, calculated from sequence, gel filtration, electrospray mass spectroscopy
monomer
1 * 20995, light scattering and electrospray mass spectroscopy analyses
monomer
-
1 * 20995, light scattering and electrospray mass spectroscopy analyses
-
additional information
primary structure analysis revealed presence of two Trx units, like in the other PDOs, but only one potential redox site, fitting the sequence of a CXXC motif. Two additional cysteine residues, Cys24 and Cys45, are also present compared to other PDOs
additional information
-
primary structure analysis revealed presence of two Trx units, like in the other PDOs, but only one potential redox site, fitting the sequence of a CXXC motif. Two additional cysteine residues, Cys24 and Cys45, are also present compared to other PDOs
additional information
-
primary structure analysis revealed presence of two Trx units, like in the other PDOs, but only one potential redox site, fitting the sequence of a CXXC motif. Two additional cysteine residues, Cys24 and Cys45, are also present compared to other PDOs
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals are grown in the presence of 2 M ammonium sulfate, 2% (v/v) PEG 400, 0.1 M Hepes (pH 8). X-ray diffraction data are collected to 1.93 A resolution
purified recombinant enzyme, hanging-drop vapor-diffusion method, mixing of 0.001 ml of 5.5 mg/ml protein solution with 0.001 ml of reservoir solution containing 13% PEG 20000, and 0.1 M MES buffer, pH 6.0, method optimization, X-ray diffraction structure determination and analysis at 1.80 A resolution, molecular modelling
the X-ray crystallographic structure is solved at 1.80 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C148S
mutant enzyme exhibits a lower activity compared to wild-type enzyme
C146S
not active in the insulin reductase assay, oxidation of the dithiol peptide NRCSQGSCWN is reduced
C35S
active in the insulin reductase assay, oxidation of the dithiol peptide NRCSQGSCWN is comparable to wild-type enzyme
C35S/C146S
not active in the insulin reductase assay, no oxidation of the dithiol peptide NRCSQGSCWN
C155S/C158S
with insulin as substrate the enzyme is completely inactive
C173S/C178S
with insulin as substrate the enzyme shows lower activity than wild-type enzyme
C41S/C44S
with insulin as substrate the enzyme shows lower activity than wild-type enzyme
C155S/C158S
-
with insulin as substrate the enzyme is completely inactive
-
C173S/C178S
-
with insulin as substrate the enzyme shows lower activity than wild-type enzyme
-
C41S/C44S
-
with insulin as substrate the enzyme shows lower activity than wild-type enzyme
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 90
stable up to 85°C, enzyme melting point, circular dichroism spectroscopy thermal denaturation study
90
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
guanidine-HCl
urea
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His-tagged enzyme from Escherichia coli strain BL21-Codon Plus (DE3)RIL by ultracentrifugation, heat treatment at 70°C for 20 min, metal chelating affinity chromatography, dialysis, anion exchange chromatography, and again dialysis
wild-type enzyme and recombinant mutant enzymes C34S, C148S and C34S/C148S
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of wild-type and mutant enzymes C35S, C146S and C35S/C146S in Escherichia coli
gene Sso1120, recombinant expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21-Codon Plus (DE3)RIL
mutant enzymes C34S, C148S and C34S/C148S, are overexpressed in Escherichia coli
wild-type enzyme and mutant enzymes C155S/C158S, C41S/C44S and C173S/C178S are expressed in Escherichi coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
when Sulfolobus solfataricus cells are incubated with H2O2, paraquat and tert-butyl hydroperoxide, the Sso0192 mRNA level increases. Specifically, a two-fold increase in transcriptional levels is observed within 30 min of the addition of tert-butyl hydroperoxide, while a slight induction is observed 30 min after paraquat and H2O2 treatment
when Sulfolobus solfataricus cells are incubated with H2O2, paraquat and tert-butyl hydroperoxide, the Sso0192 mRNA level increases. Specifically, a two-fold increase in transcriptional levels is observed within 30 min of the addition of tert-butyl hydroperoxide, while a slight induction is observed 30 min after paraquat and H2O2 treatment
when Sulfolobus solfataricus cells are incubated with H2O2, paraquat and tert-butyl hydroperoxide, the Sso0192 mRNA level increases. Specifically, a two-fold increase in transcriptional levels is observed within 30 min of the addition of tert-butyl hydroperoxide, while a slight induction is observed 30 min after paraquat and H2O2 treatment
-
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pedone, E.; Ren, B.; Ladenstein, R.; Rossi, M.; Bartolucci, S.
Functional properties of the protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus: a member of a novel protein family related to protein disulfide-isomerase
Eur. J. Biochem.
271
3437-3448
2004
Pyrococcus furiosus (Q51760)
brenda
Pedone, E.; Limauro, D.; D'Alterio, R.; Rossi, M.; Bartolucci, S.
Characterization of a multifunctional protein disulfide oxidoreductase from Sulfolobus solfataricus
FEBS J.
273
5407-5420
2006
Saccharolobus solfataricus (Q980T5), Saccharolobus solfataricus P2 (Q980T5)
brenda
Limauro, D.; Saviano, M.; Galdi, I.; Rossi, M.; Bartolucci, S.; Pedone, E.
Sulfolobus solfataricus protein disulphide oxidoreductase: insight into the roles of its redox sites
Protein Eng. Des. Sel.
22
19-26
2009
Saccharolobus solfataricus (Q980T5), Saccharolobus solfataricus P2 (Q980T5)
brenda
Limauro, D.; De Simone, G.; Pirone, L.; Bartolucci, S.; D'Ambrosio, K.; Pedone, E.
Sulfolobus solfataricus thiol redox puzzle: characterization of an atypical protein disulfide oxidoreductase
Extremophiles
18
219-228
2013
Saccharolobus solfataricus (Q97Z21), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97Z21)
brenda
Guagliardi, A.; Cerchia, L.; De Rosa, M.; Rossi, M.; Bartolucci, S.
Isolation of a thermostable enzyme catalyzing disulfide bond formation from the archaebacterium Sulfolobus solfataricus
FEBS Lett.
303
27-30
1992
Saccharolobus solfataricus (P39476), Saccharolobus solfataricus P2 (P39476)
brenda
Pedone, E.; D'Ambrosio, K.; De Simone, G.; Rossi, M.; Pedone, C.; Bartolucci, S.
Insights on a new PDI-like family: structural and functional analysis of a protein disulfide oxidoreductase from the bacterium Aquifex aeolicus
J. Mol. Biol.
356
155-164
2005
Aquifex aeolicus (O66753), Aquifex aeolicus
brenda
D'Ambrosio, K.; Pedone, E.; Langella, E.; De Simone, G.; Rossi, M.; Pedone, C.; Bartolucci, S.
A novel member of the protein disulfide oxidoreductase family from Aeropyrum pernix K1: structure, function and electrostatics
J. Mol. Biol.
362
743-752
2006
Aeropyrum pernix (Q9YDZ4)
brenda
Ren, B.; Tibbelin, G.; de Pascale, D.; Rossi, M.; Bartolucci, S.; Ladenstein, R.
A protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus contains two thioredoxin fold units
Nat. Struct. Biol.
5
602-611
1998
Pyrococcus furiosus (Q51760)
brenda
Limauro, D.; De Simone, G.; Pirone, L.; Bartolucci, S.; DAmbrosio, K.; Pedone, E.
Sulfolobus solfataricus thiol redox puzzle characterization of an atypical protein disulfide oxidoreductase
Extremophiles
18
219-228
2014
Saccharolobus solfataricus (Q97Z21), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97Z21)
brenda
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