Information on EC 1.8.99.B1 - protein-disulfide reductase (acceptor)

Substrates: the enzyme is involved in disulfide bond formation
Products: -

protein-dithiol + oxidized acceptor

protein-disulfide + reduced acceptor

Substrates: the enzyme is involved in disulfide bond formation
Products: -

[insulin]-disulfide + reduced dithiothreitol

[insulin]-dithiol + oxidized dithiothreitol

Substrates: -
Products: -

[insulin]-disulfide + reduced dithiothreitol

[insulin]-dithiol + oxidized dithiothreitol

Substrates: -
Products: -

[insulin]-disulfide + reduced dithiothreitol

[insulin]-dithiol + oxidized dithiothreitol

Substrates: -
Products: -

[insulin]-disulfide + reduced dithiothreitol

[insulin]-dithiol + oxidized dithiothreitol

Substrates: -
Products: -

[insulin]-disulfide + reduced dithiothreitol

[insulin]-dithiol + oxidized dithiothreitol

Substrates: the enzyme does not present isomerase activity
Products: -

[insulin]-disulfide + reduced dithiothreitol

[insulin]-dithiol + oxidized dithiothreitol

Substrates: -
Products: -

[insulin]-disulfide + reduced dithiothreitol

[insulin]-dithiol + oxidized dithiothreitol

Substrates: -
Products: -

[insulin]-disulfide + reduced dithiothreitol

[insulin]-dithiol + oxidized dithiothreitol

Substrates: the enzyme does not present isomerase activity
Products: -

[insulin]-disulfide + reduced dithiothreitol

[insulin]-dithiol + oxidized dithiothreitol

Substrates: -
Products: -

[ribonuclease A]-dithiol + oxidized acceptor

[ribonuclease A]-disulfide + reduced acceptor

Substrates: -
Products: -

[ribonuclease A]-dithiol + oxidized acceptor

[ribonuclease A]-disulfide + reduced acceptor

Substrates: -
Products: -

additional information

Substrates: the enzyme reveals an inherent glutathione-dependent thioltransferase activity
Products: -

additional information

Substrates: the enzyme reveals an inherent glutathione-dependent thioltransferase activity
Products: -

additional information

Substrates: the enzyme reveals an inherent glutathione-dependent thioltransferase activity
Products: -

show all columns Go to Natural Substrate Search

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

protein-dithiol + oxidized acceptor

protein-disulfide + reduced acceptor

protein-dithiol + oxidized acceptor

protein-disulfide + reduced acceptor

Substrates: intracellular proteins of certain hyperthermophilic archaea are rich in disulfide bonds. Disulfide bonds stabilize many thermostable proteins
Products: -

protein-dithiol + oxidized acceptor

protein-disulfide + reduced acceptor

Substrates: the enzyme is involved in disulfide bond formation
Products: -

protein-dithiol + oxidized acceptor

protein-disulfide + reduced acceptor

Substrates: the enzyme is involved in disulfide bond formation
Products: -

show all columns Go to pH Optimum Search

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

assay at

assay at

assay at

show all columns Go to Temperature Optimum Search

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TEMPERATURE OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

assay at

assay at

assay at

assay at

679756, 701047

show all columns Go to Pi Value Search

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pI VALUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

4.7

calculated from sequence

5.3

calculated from sequence

show all columns Go to Organism Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks include all textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks + FRENDAco-occurrence of enzyme names and organism names (less precise)

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

UniProt

brenda

UniProt

brenda

661641, 726026

UniProt

brenda

679756, 701047

UniProt

brenda

UniProt

brenda

SwissProt

brenda

679756, 701047

UniProt

brenda

UniProt

brenda

SwissProt

brenda

show all columns Go to Localization Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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LOCALIZATION

ORGANISM

UNIPROT

COMMENTARY

GeneOntology No.

LITERATURE

SOURCE

cytosol

cytosol

brenda

5829

brenda

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Go to AA Sequence and Transmembrane Helices SearchGo to Localization Prediction

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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).

O66753 pBLAST

O66753_AQUAE

Aquifex aeolicus (strain VF5)

229

25641

TrEMBL

Secretory Pathway (Reliability: 4)

P39476 pBLAST

DN7D_SACS2

Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

7280

Swiss-Prot

Q51760 pBLAST

Q51760_9EURY

226

25781

TrEMBL

Q97Z21 pBLAST

Q97Z21_SACS2

Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

171

19931

TrEMBL

Q980T5 pBLAST

Q980T5_SACS2

Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

233

26033

TrEMBL

Secretory Pathway (Reliability: 2)

Q9YDZ4 pBLAST

Q9YDZ4_AERPE

Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)

243

27334

TrEMBL

show all columns Go to Molecular Weight Search

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MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

19930

1 * 19930, calculated from sequence

20995

1 * 20995, light scattering and electrospray mass spectroscopy analyses

21000

light scattering and electrospray mass spectroscopy analyses

25650

wild-type enzyme electrospray mass spectroscopy

26032

x * 26032, calculated from sequence

26700

gel-filtration, electrospray mass spectroscopy

27100

gel filtration, electrospray mass spectrometry

27198

1 * 27198, calculated from sequence, gel filtration, electrospray mass spectroscopy

27200

gel filtration, electrospray mass spectroscopy

6200

x * 6200, reducing SDS-PAGE

show all columns Go to Subunit Search

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SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

4 entries

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

726026

monomer

5 entries

x * 6200, reducing SDS-PAGE

x * 26032, calculated from sequence

x * 6200, reducing SDS-PAGE

x * 26032, calculated from sequence

monomer

1 * 27198, calculated from sequence, gel filtration, electrospray mass spectroscopy

monomer

1 * 20995, light scattering and electrospray mass spectroscopy analyses

monomer

1 * 19930, calculated from sequence

monomer

1 * 20995, light scattering and electrospray mass spectroscopy analyses

monomer

1 * 19930, calculated from sequence

Go to Crystallization (commentary) Search

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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

crystal structure at 2.4 A resolution

the X-ray crystallographic structure is solved at 1.80 A resolution

show all columns Go to Protein Variants Search

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

C148S

mutant enzyme exhibits a lower activity compared to wild-type enzyme

C34S

mutant enzyme retains nearly wild-type activity

C34S/C148S

mutant enzyme shows no activity

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

show all columns Go to Temperature Stability Search

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TEMPERATURE STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

2 h, stable

Tm-value

show all columns Go to Organic Solvent Search

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ORGANIC SOLVENT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

guanidine-HCl

urea

guanidine-HCl

[GuHCl]/2 value is 1.5 M

guanidine-HCl

[GuHCl]/2 value is 1.5 M

urea

resistant to urea presenting a [urea]/2 value of 5 M

urea

resistant to urea presenting a [urea]/2 value of 5 M

Go to Purification (commentary) Search

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PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

5 entries

wild-type enzyme and recombinant mutant enzymes C34S, C148S and C34S/C148S

Go to Cloned (commentary) Search

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CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

expressed in Escherichia coli

expression in Escherichia coli

expression of wild-type and mutant enzymes C35S, C146S and C35S/C146S in Escherichia coli

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

expression in Escherichia coli

expression in Escherichia coli

726026

expression in Escherichia coli

Go to Expression Search

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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

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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)

15291821

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)

17076700

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.

19-26

2009

Saccharolobus solfataricus (Q980T5), Saccharolobus solfataricus P2 (Q980T5)

18988690

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

219-228

2013

Saccharolobus solfataricus (Q97Z21), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97Z21)

24306780

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)

1592111

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

16364362

brenda