Enzyme

Download
EC Tree
     1. Oxidoreductases
        1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
            1.14.15 With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor
ID:1.14.15.20
Description:Heme oxygenase (biliverdin-producing, ferredoxin).
Cath: 3.30.70.100; 3.30.70.3430; 1.20.910.10;

3D structure

Click one PDB to see exact 3D structure provided by NGL.

Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.15.20
BRENDA Enzyme Link: BRENDA 1.14.15.20
KEGG Enzyme Link: KEGG1.14.15.20
BioCyc Enzyme Link: BioCyc 1.14.15.20
ExPASy Enzyme Link: ExPASy1.14.15.20
EC2PDB Enzyme Link: EC2PDB 1.14.15.20
ExplorEnz Enzyme Link: ExplorEnz 1.14.15.20
PRIAM enzyme-specific profiles Link: PRIAM 1.14.15.20
IntEnz Enzyme Link: IntEnz 1.14.15.20
MEDLINE Enzyme Link: MEDLINE 1.14.15.20
MSA:

1.14.15.20;

Phylogenetic Tree:

1.14.15.20;

Uniprot:
M-CSA:
RHEA:50232 8 H(+) + heme b + 3 O2 + 6 reduced [2Fe-2S]-[ferredoxin] = biliverdin IXalpha + CO + Fe(2+) + 3 H2O + 6 oxidized [2Fe-2S]-[ferredoxin]
RULE(radius=1)
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Function and distribution of bilin biosynthesis enzymes in photosynthetic organisms.Dammeyer T, Frankenberg-Dinkel N2008 Oct18846276
Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis sp. PCC 6803 in complex with heme.Sugishima M, Migita CT, Zhang X, Yoshida T, Fukuyama K2004 Nov15560792
Phytochrome ancestry: sensors of bilins and light.Montgomery BL, Lagarias JC2002 Aug12167331