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Literature summary for 4.4.1.31 extracted from
- Biliprotein chromophore attachment: Chaperone-like function of the PecE subunit of alpha-phycoerythrocyanin lyase (2007), J. Biol. Chem., 282, 25357-25366.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mastigocladus laminosus | P29729 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| apo-[phycoerythrocyanin alpha-subunit PecA] + phycocyanobilin | substrate PecA and subunit PecE form a weak complex that is stabilized by phycocyanobilin. The first reaction step involves a conformational change and/or protonation of phycocyanobilin, and subunit PecE has a chaperone-like function on the chromoprotein | Mastigocladus laminosus | [phycoerythrocyanin alpha-subunit PecA]-Cys84-phycoviolobilin | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| pecE | - |
Mastigocladus laminosus |
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Release 2023.1 (January 2023)
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