Species: Ye
Applications: WB, ICC/IF, IP
Host: Mouse Monoclonal
Description
One of the important aspects of secretory protein's folding process is the formation of native disulfide bonds which is catalyzed by enzyme protein disulfide isomerase (PDI) and yeast Saccharomyces cerevisiae has about 5 protein disulfide isomerase (PDI) family members (EUG1, MPD1, MPD2, EPS1 and PDI1/PDI1p). Pdi1p is a typical member of its family which is an essential gene and is considered homologus to human PDI with no significant differences; however, the two proteins are only 29% identical. It is a major ER protein with chaperon/co-chaperon activity and is involved in the retention of resident ER proteins as well as in recognizing proteins targeted for ER-associated degradation (ERAD). Yeast Pdi1p is a folding catalyst which introduces disulfide bonds into its substrates and rearranges or reduces pre-existing ones, and besides its oxidoreductase activity, Pdi1p acts as a molecular chaperone that also facilitates folding of proteins which do not contain disulfide bonds.
Bioinformatics
| Alternate Names |
- MFP 1
- MFP1
- PDI 1
- PDI
- PDI1
- Protein disulfide isomerase
- Thioredoxin related glycoprotein 1
- TRG 1
- TRG1
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