+ 4 reduced
ferredoxin
Phycocyanobilin:ferredoxin oxidoreductase
| phycocyanobilin:ferredoxin oxidoreductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.3.7.5 | ||||||||
| CAS no. | 347401-12-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, phycocyanobilin:ferredoxin oxidoreductase (PcyA, EC 1.3.7.5) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are biliverdin and reduced ferredoxin. Its products are (2R,3Z)-phycocyanobilin and oxidized ferredoxin.[1][2][3][4]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is (3Z)-phycocyanobilin:ferredoxin oxidoreductase. This enzyme participates in the catabolism of heme.[2]
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2D1E, 2DKE, and 2G18.
References
- ^ Enzyme 1.3.7.5 at KEGG Pathway Database.
- ^ a b Beale, Samuel I. (1993). "Biosynthesis of phycobilins". Chemical Reviews. 93 (2): 785–802. doi:10.1021/cr00018a008.
- ^ Frankenberg N, Mukougawa K, Kohchi T, Lagarias JC (2001). "Functional genomic analysis of the HY2 family of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms". Plant Cell. 13 (4): 965–78. Bibcode:2001PlanC..13..965F. doi:10.1105/tpc.13.4.965. PMC 135530. PMID 11283349.
- ^ Wu SH, McDowell MT, Lagarias JC (1997). "Phycocyanobilin is the natural precursor of the phytochrome chromophore in the green alga Mesotaenium caldariorum". J. Biol. Chem. 272 (41): 25700–5. doi:10.1074/jbc.272.41.25700. PMID 9325294.