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Catalog Number | orb1961071 |
---|---|
Category | Proteins |
Description | Phosphopantothenoylcysteine Decarboxylase (PPC-DC) is an essential enzyme in the biosynthesis ofCoenzyme A and catalyzes the decarboxylation of PPC to Phosphopantetheine. PPC-DC catalyzes the decarboxylation of the Cysteine moiety of 4-Phosphopantothenoylcysteine (PPC) to form 4-Phosphopantetheine (PPantSH), this reaction forms part of the biosynthesis of Coenzyme A. The enzyme is a member of the larger family of Cysteine Decarboxylases including the Lantibiotic-Biosynthesizing enzymes EpiD and MrsD, all of which use a tightly bound Flavin cofactor to oxidize the Thiol moiety of the substrate to a Thioaldehyde. |
Tag | N-6xHis |
Purity | 98.00% |
MW | 27 KDa (reducing condition) |
UniProt ID | Q96CD2 |
Protein Sequence | Met1-Ser204 |
Expression System | E. coli |
Biological Origin | Human |
Biological Activity | Phosphopantothenoylcysteine Decarboxylase (PPC-DC) is an essential enzyme in the biosynthesis ofCoenzyme A and catalyzes the decarboxylation of PPC to Phosphopantetheine. PPC-DC catalyzes the decarboxylation of the Cysteine moiety of 4-Phosphopantothenoylcysteine (PPC) to form 4-Phosphopantetheine (PPantSH), this reaction forms part of the biosynthesis of Coenzyme A. The enzyme is a member of the larger family of Cysteine Decarboxylases including the Lantibiotic-Biosynthesizing enzymes EpiD and MrsD, all of which use a tightly bound Flavin cofactor to oxidize the Thiol moiety of the substrate to a Thioaldehyde. |
Expression Region | Met1-Ser204 |
Storage | -20°C |
Note | For research use only |
Expiration Date | 6 months from date of receipt. |