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

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:
UNIPROT: Q96DN0
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
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
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
-
-
-
-
additional information
the enzyme belongs to the family of protein disulfide isomerases
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
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glutathione
reduced and oxidized
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ERp27
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
expression of ERp27
Manually annotated by BRENDA team
expression of ERp27
Manually annotated by BRENDA team
expression of ERp27
Manually annotated by BRENDA team
high expression of ERp27
Manually annotated by BRENDA team
expression of ERp27
Manually annotated by BRENDA team
expression of ERp27
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
ERp27 contains a putative secretory pathway signal sequence and a putative endoplasmic reticulum-retention signal, overview
Manually annotated by BRENDA team
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ERP27_HUMAN
273
0
30480
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27700
x * 27700, ERp27, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 27700, ERp27, SDS-PAGE
additional information
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E231A/W232A/D233G
site-directed mutagenesis, the ERp27 mutant shows a similar structure as wild-type ERp57, but highly reduced binding to ERp57 compared to the wild-type enzyme
E231K
site-directed mutagenesis, the ERp27 mutant shows a similar structure as wild-type ERp57, but highly reduced binding to ERp57 compared to the wild-type enzyme
I196W
site-directed mutagenesis, the ERp27 mutant shows a structure and ERp57 binding similar to the wild-type enzyme
R280A
site-directed mutagenesis, the mutant shows a structure reduced binding of ERp27, wild-type and mutants, as compared to the wild-type ERp57
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant proteins from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the gene encoding ERp27 is located at 14,958,241–14,982,750 bp on chromosome 12 and has 7 exons, DNA and amino acid sequence determination and anaylsis, sequence comparison, expression of GFP-fusion ERp27 in COS-7 cell endoplasmic reticulum, expression of N-terminally His-tagged wild-type and mutant ERp57, and of PDI a, b, and b' domains, in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Alanen, H.I.; Williamson, R.A.; Howard, M.J.; Hatahet, F.S.; Salo, K.E.; Kauppila, A.; Kellokumpu, S.; Ruddock, L.W.
ERp27, a new non-catalytic endoplasmic reticulum-located human protein disulfide isomerase family member, interacts with ERp57
J. Biol. Chem.
281
33727-33738
2006
Homo sapiens (Q96DN0), Homo sapiens
Manually annotated by BRENDA team