Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 5.3.4.1 - protein disulfide-isomerase and Organism(s) Sus scrofa and UniProt Accession E1CAJ6

for references in articles please use BRENDA:EC5.3.4.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     5 Isomerases
         5.3 Intramolecular oxidoreductases
             5.3.4 Transposing S-S bonds
                5.3.4.1 protein disulfide-isomerase
IUBMB Comments
Needs reducing agents or partly reduced enzyme; the reaction depends on sulfhydryl-disulfide interchange.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Sus scrofa
UNIPROT: E1CAJ6
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Sus scrofa
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
hide
catalyses the rearrangement of -S-S- bonds in proteins
Synonyms
fibronectin, pdi, protein disulfide isomerase, erp57, pdia3, protein disulphide isomerase, cabp1, erp44, disulfide isomerase, erp72, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
protein disulfide isomerase-P5
-
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
-
-
-
-
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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
37318-49-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
unfolded acidic phospholipase A2
refolded acidic phospholipase A2
show the reaction diagram
-
PDI at a molar ratio to acidic phospholipase A2 of 0.1 increases the reactivation of reduced and denatured acidic phospholipase A2 from 4% to 15%
-
?
unfolded insulin
refolded insulin
show the reaction diagram
-
-
-
?
unfolded mitochondrial malate dehydrogenase
refolded mitochondrial malate dehydrogenase
show the reaction diagram
-
maximum refolding when the PDI concentration is 20fold higher than the malate dehydrogenase concentration
-
?
unfolded RNase A
refolded RNase
show the reaction diagram
-
-
-
?
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
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.6
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDI-P5; isozymes PDIA3 and PDI-P5
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
epididymal caput, corpus, and cauda sperm, isozymes PDIA3 and PDI-P5. PDI-P5 is downregulated from the epididymal corpus to cauda sperm, while PDIA3 is constitutively expressed
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
physiological roles of PDIA3 and PDI-P5 in sperm maturation and fertilization, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
E1CAJ6_PIG
440
0
48074
TrEMBL
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48074
x * 48074, PDI-P5, sequence calculation, x * 56859, PDIA3, sequence calculation
56859
x * 48074, PDI-P5, sequence calculation, x * 56859, PDIA3, sequence calculation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 48074, PDI-P5, sequence calculation, x * 56859, PDIA3, sequence calculation
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
autophosphorylation in the central domain
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged mature isozymes PDIA3 and PDI-P5 from Escherichia coli strain HMS174 (DE3) by nickel affinity chromatography and anion exchange chromatography, the His-tag of PDI-P5 is cleaved off
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
isozymes PDIA3 and PDI-P5 precursors, DNA and amino acid sequence determination and analysis, expression of His-tagged mature isozymes in Escherichia coli strain HMS174 (DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Churchich, J.E.
Retinol, a probe of conformational changes in protein disulfide isomerase
Biochem. Biophys. Res. Commun.
261
41-45
1999
Sus scrofa
Manually annotated by BRENDA team
Churchich, J.E.; Lee, K.S.
A catalytic site of protein disulfide isomerase probed with adenosine-5'-triphosphate analogs
Biochim. Biophys. Acta
1479
293-302
2000
Sus scrofa
Manually annotated by BRENDA team
Cheung, P.Y.; Churchich, J.E.
Recognition of protein substrates by protein-disulfide isomerase. A sequence of the b' domain responds to substrate binding
J. Biol. Chem.
274
32757-32761
1999
Sus scrofa
Manually annotated by BRENDA team
Wang, C.C.
Protein disulfide isomerase as an enzyme and a chaperone in protein folding
Methods Enzymol.
348
66-75
2002
Sus scrofa
Manually annotated by BRENDA team
Akama, K.; Horikoshi, T.; Sugiyama, A.; Nakahata, S.; Akitsu, A.; Niwa, N.; Intoh, A.; Kakui, Y.; Sugaya, M.; Takei, K.; Imaizumi, N.; Sato, T.; Matsumoto, R.; Iwahashi, H.; Kashiwabara, S.; Baba, T.; Nakamura, M.; Toda, T.
Protein disulfide isomerase-P5, down-regulated in the final stage of boar epididymal sperm maturation, catalyzes disulfide formation to inhibit protein function in oxidative refolding of reduced denatured lysozyme
Biochim. Biophys. Acta
1804
1272-1284
2010
Sus scrofa (E1CAJ6), Sus scrofa
Manually annotated by BRENDA team