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Information on EC 5.3.4.1 - protein disulfide-isomerase and Organism(s) Humicola insolens and UniProt Accession P55059
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5.3.4.1 protein disulfide-isomeraseIUBMB Comments
Needs reducing agents or partly reduced enzyme; the reaction depends on sulfhydryl-disulfide interchange.
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Word Map
- 5.3.4.1
- collagen
- laminin
- integrins
- endothelial
- actin
- fibrosis
-
adhesive
-
basement
- mesenchymal
- vessel
- fiber
- metastasis
- proteoglycans
- vitronectin
- fibrinogen
- matrices
- nephropathy
- albumin
- gelatin
-
interstitial
-
mesangial
- platelet
- monolayer
- cytoskeleton
- glomerular
- rgd
- vimentin
- e-cadherin
-
cell-cell
- adhesions
- zeta
- myofibroblasts
- willebrand
-
epithelial-mesenchymal
- factor-beta
- fak
- fibrin
- metalloproteinases
-
preterm
-
dish
-
biomaterials
- procollagens
- heparan
-
alpha-smooth
- dermal
- tgf-beta
- plasminogen
-
fibrillar
- drug development
-
heparin-binding
- synthesis
- thrombospondin
- medicine
- industry
- diagnostics
- pharmacology
- biotechnology
- analysis
The taxonomic range for the selected organisms is: Humicola insolens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
fibronectin, pdi, protein disulfide isomerase, erp57, pdia3, protein disulphide isomerase, cabp1, erp44, disulfide isomerase, erp72, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5'-MD
-
-
-
-
58 kDa glucose regulated protein
-
-
-
-
58 kDa microsomal protein
-
-
-
-
CaBP1
-
-
-
-
CaBP2
-
-
-
-
Cellular thyroid hormone binding protein
-
-
-
-
Disulfide interchange enzyme
-
-
-
-
Disulfide isomerase ER-60
-
-
-
-
DsbA
-
-
-
-
DsbC
-
-
-
-
DsbD
-
-
-
-
endoplasmic reticulum protein EUG1
-
-
-
-
ER58
-
-
-
-
ERp-72 homolog
-
-
-
-
ERp57
-
-
-
-
ERP59
-
-
-
-
ERP60
-
-
-
-
ERp72
-
-
-
-
HIP-70
-
-
-
-
Iodothyronine 5'-monodeiodinase
-
-
-
-
P55
-
-
-
-
P58
-
-
-
-
PDI
PDIp
-
-
-
-
Protein disulfide isomerase P5
-
-
-
-
Protein disulfide isomerase-related protein
-
-
-
-
Protein disulphide isomerase
-
-
-
-
Protein ERp-72
-
-
-
-
R-cognin
-
-
-
-
Rearrangease
-
-
-
-
Reduced ribonuclease reactivating enzyme
-
-
-
-
Retina cognin
-
-
-
-
S-S rearrangase
-
-
-
-
Thyroid hormone-binding protein
-
-
-
-
Thyroxine deiodinase
-
-
-
-
PDI
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
-
-
-
-
intramolecular oxidoreduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
Protein disulfide-isomerase
Needs reducing agents or partly reduced enzyme; the reaction depends on sulfhydryl-disulfide interchange.
CAS REGISTRY NUMBER
COMMENTARY
37318-49-3
-
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
denatured lysozyme
?
-
PDI catalyzes the formation, rearrangement, and breakage of disulfide bonds, oxidative refolding by PDI almost completely restores lysozyme activity, overview
-
-
?
Proteins
Proteins
-
refolding of scrambled ribonuclease
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
refolding of scrambled lysosyme
with correct disulfide bonds
?
additional information
?
-
PDI is a major protein in the endoplasmic reticulum, operating as an essential folding catalyst and molecular chaperone for disulfide-containing proteins by catalyzing the formation, rearrangement, and breakage of their disulfide bridges
-
-
?
additional information
?
-
-
PDI is a major protein in the endoplasmic reticulum, operating as an essential folding catalyst and molecular chaperone for disulfide-containing proteins by catalyzing the formation, rearrangement, and breakage of their disulfide bridges
-
-
?
additional information
?
-
the enzyme has a modular structure with four thioredoxin-like domains, a, b, b', and a', along with a C-terminal extension. The homologous a and a' domains contain one cysteine pair in their active site directly involved in thiol-disulfide exchange reactions, while the b' domain putatively provides a primary binding site for unstructured regions of the substrate polypeptides, mechanistic model of PDI action, overview. The a' domain transfers its own disulfide bond into the unfolded protein accommodated on the hydrophobic surface of the substrate-binding region, which consequently changes into a closed form releasing the oxidized substrate, domain arrangements and redox behaviour, overview
-
-
?
additional information
?
-
-
the enzyme has a modular structure with four thioredoxin-like domains, a, b, b', and a', along with a C-terminal extension. The homologous a and a' domains contain one cysteine pair in their active site directly involved in thiol-disulfide exchange reactions, while the b' domain putatively provides a primary binding site for unstructured regions of the substrate polypeptides, mechanistic model of PDI action, overview. The a' domain transfers its own disulfide bond into the unfolded protein accommodated on the hydrophobic surface of the substrate-binding region, which consequently changes into a closed form releasing the oxidized substrate, domain arrangements and redox behaviour, overview
-
-
?
additional information
?
-
-
PDI also functions as a dehydroascorbate reductase and a molecular chaperone besides its disulfide-isomerizing function
-
-
?
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
additional information
?
-
PDI is a major protein in the endoplasmic reticulum, operating as an essential folding catalyst and molecular chaperone for disulfide-containing proteins by catalyzing the formation, rearrangement, and breakage of their disulfide bridges
-
-
?
additional information
?
-
-
PDI is a major protein in the endoplasmic reticulum, operating as an essential folding catalyst and molecular chaperone for disulfide-containing proteins by catalyzing the formation, rearrangement, and breakage of their disulfide bridges
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
refolding reaction obeys almost first-order kinetics with respect to PDI concentration
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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). PDI_HUMIN
505
1
55114
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme has a modular structure with four thioredoxin-like domains, a, b, b', and a', along with a C-terminal extension. The homologous a and a' domains contain one cysteine pair in their active site directly involved in thiol-disulfide exchange reactions, while the b' domain putatively provides a primary binding site for unstructured regions of the substrate polypeptides, structure determination and analysis by NMR and small-angle X-ray scattering methods, domain arrangements and redox behaviour, overview
additional information
-
the enzyme has a modular structure with four thioredoxin-like domains, a, b, b', and a', along with a C-terminal extension. The homologous a and a' domains contain one cysteine pair in their active site directly involved in thiol-disulfide exchange reactions, while the b' domain putatively provides a primary binding site for unstructured regions of the substrate polypeptides, structure determination and analysis by NMR and small-angle X-ray scattering methods, domain arrangements and redox behaviour, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with alpha-synuclein, using 0.1 M HEPES buffer (pH 7.5) containing 25% (w/v) PEG3350
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
chelating Sepharose column chromatography and Resource Q column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sugiyama, H.; Idekoba, C.; Kajino, T.; Hoshino, F.; Asami, O.; Yamada, Y.; Udaka, S.
Purification of protein disulfide isomerase from a thermophilic fungus
Biosci. Biotechnol. Biochem.
57
1704-1707
1993
Humicola insolens
Kajino, T.; Miyazaki, C.; Asami, O.; Hirai, M.; Yamada, Y.; Udaka, S.
Thermophilic fungal protein disulfide isomerase
Methods Enzymol.
290
50-59
1998
Bos taurus, Humicola insolens
Nohara, D.; Hizikata, H.; Asami, O.
Enhancement of the activity of renatured lysozyme by protein disulfide isomerase
J. Biosci. Bioeng.
104
235-237
2007
Humicola insolens
Serve, O.; Kamiya, Y.; Maeno, A.; Nakano, M.; Murakami, C.; Sasakawa, H.; Yamaguchi, Y.; Harada, T.; Kurimoto, E.; Yagi-Utsumi, M.; Iguchi, T.; Inaba, K.; Kikuchi, J.; Asami, O.; Kajino, T.; Oka, T.; Nakasako, M.; Kato, K.
Redox-dependent domain rearrangement of protein disulfide isomerase coupled with exposure of its substrate-binding hydrophobic surface
J. Mol. Biol.
396
361-374
2010
Humicola insolens (P55059), Humicola insolens
Nakasako, M.; Maeno, A.; Kurimoto, E.; Harada, T.; Yamaguchi, Y.; Oka, T.; Takayama, Y.; Iwata, A.; Kato, K.
Redox-dependent domain rearrangement of protein disulfide isomerase from a thermophilic fungus
Biochemistry
49
6953-6962
2010
Humicola insolens
Inagaki, K.; Satoh, T.; Yagi-Utsumi, M.; Le Gulluche, A.C.; Anzai, T.; Uekusa, Y.; Kamiya, Y.; Kato, K.
Redox-coupled structural changes of the catalytic a' domain of protein disulfide isomerase
FEBS Lett.
589
2690-2694
2015
Humicola insolens (P55059)
EXTERNAL LINKS (specific for EC-Number 5.3.4.1)
Transporter Classification Database (TCDB): 8.A.88.2.3, 8.A.88.2.7
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