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Literature summary for 5.3.4.1 extracted from

  • Koivunen, P.; Pirneskoski, A.; Karvonen, P.; Ljung, J.; Helaakoski, T.; Notbohm, H.; Kivirikko, K.I.
    The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide (1999), EMBO J., 18, 65-74.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression Sf9 insect cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
D439A 119% of wild-type 4-hydroxylase activity Homo sapiens
E454A 76% of wild-type 4-hydroxylase activity Homo sapiens
F449A 63% of wild-type 4-hydroxylase activity Homo sapiens
F449E 9% of wild-type 4-hydroxylase activity Homo sapiens
F449R no 4-hydroxylase activity, 85% and 93% of wild-type isomerase and reductase activity, respectively Homo sapiens
F449W 59%, 133% and 94% of wild-type 4-hydroxylase, isomerase and reductase activity, respectively Homo sapiens
F449Y 79%, 42% and 87% of wild-type 4-hydroxylase, isomerase and reductase activity, respectively Homo sapiens
F452R 115% of wild-type 4-hydroxylase activity Homo sapiens
G448R 43%, 85% and 93% of wild-type 4-hydroxylase, isomerase and reductase activity, respectively Homo sapiens
I438E 79% of wild-type 4-hydroxylase activity Homo sapiens
K450A 113% of wild-type 4-hydroxylase activity Homo sapiens
K451A 74% of wild-type 4-hydroxylase activity Homo sapiens
L446E 107% of wild-type 4-hydroxylase activity Homo sapiens
L453E 13%, 23% and 48% of wild-type 4-hydroxylase, isomerase and reductase activity, respectively Homo sapiens
R444A 43%, 83% and 79% of wild-type 4-hydroxylase, isomerase and reductase activity, respectively Homo sapiens
V437D 102% of wild-type 4-hydroxylase activity Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P07237
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-

Purification (Commentary)

Purification (Comment) Organism
recombinant PDI Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
unfolded RNase PDI is a multifunctional enzyme that acts as a subunit in prolyl 4-hydroxylases and the microsomal triglyceride transfer protein, and as a chaperone that binds various peptides and assists their folding Homo sapiens refolded RNase
-
?

Subunits

Subunits Comment Organism
More PDI is a multifunctional enzyme that acts as beta subunit in prolyl 4-hydroxylases and as a subunit in the microsomal triglyceride transfer protein Homo sapiens

Synonyms

Synonyms Comment Organism
PDI
-
Homo sapiens