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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.B1
preliminary BRENDA-supplied EC number
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UNIPROT: Q97Z21
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Word Map
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Synonyms
appdo, sso1120, aapdo, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glutaredoxin related protein
UniProt
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
insulin disulfide + reduced thioredoxin
insulin dithiol + oxidized thioredoxin
show the reaction diagram
with NADPH and FAD
-
-
?
protein-dithiol + oxidized acceptor
protein-disulfide + reduced acceptor
show the reaction diagram
the enzyme is involved in disulfide bond formation
-
-
?
[insulin]-disulfide + reduced dithiothreitol
[insulin]-dithiol + oxidized dithiothreitol
show the reaction diagram
the enzyme does not present isomerase activity
-
-
?
additional information
?
-
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
protein-dithiol + oxidized acceptor
protein-disulfide + reduced acceptor
show the reaction diagram
the enzyme is involved in disulfide bond formation
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3
calculated from sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q97Z21_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
171
0
19931
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 90
stable up to 85°C, enzyme melting point, circular dichroism spectroscopy thermal denaturation study
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
guanidine-HCl
[GuHCl]/2 value is 1.5 M
urea
resistant to urea presenting a [urea]/2 value of 5 M
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
gene Sso1120, recombinant expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21-Codon Plus (DE3)RIL
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team