Title : Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin.

Pub. Date : 1985 Sep 19-25

PMID : 3840230






3 Functional Relationships(s)
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Sentence
Compound Name
Protein Name
Organism
1 The enzyme involved, protein disulphide isomerase (PDI; EC 5.3.4.1), may be the in vivo catalyst of disulphide bond formation. disulphide prolyl 4-hydroxylase subunit beta Rattus norvegicus
2 Each of these regions contains the presumed active site sequence Trp-Cys-Gly-His-Cys-Lys, suggesting that PDI, similar in action to thioredoxin, catalyses disulphide bond interchange via an internal disulphide-sulphydryl interchange. disulphide prolyl 4-hydroxylase subunit beta Rattus norvegicus
3 Each of these regions contains the presumed active site sequence Trp-Cys-Gly-His-Cys-Lys, suggesting that PDI, similar in action to thioredoxin, catalyses disulphide bond interchange via an internal disulphide-sulphydryl interchange. disulphide prolyl 4-hydroxylase subunit beta Rattus norvegicus