EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
5.2.1.12 | Dithionite | catalytic activity of the as-purified enzyme requires pretreatment with dithionite to a final concentration of 10 mM to create reducing conditions | Zea mays |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
5.2.1.12 | homology modeling of structure | Zea mays |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
5.2.1.12 | chloroplast | - |
Zea mays | 9507 | - |
5.2.1.12 | membrane | integral membrane protein | Zea mays | 16020 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
5.2.1.12 | Iron | - |
Zea mays |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
5.2.1.12 | Zea mays | B4FHU1 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
5.2.1.12 | the as-purified enzyme (considered to be oxidized), as well as heat denatured Z-ISO, are not functional. Catalytic activity requires pretreatment with dithionite to a final concentration of 10 mM to create reducing conditions | Zea mays |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.2.1.12 | 9,15,9'-tricis-zeta-carotene | - |
Zea mays | 9,9'-dicis-zeta-carotene | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
5.2.1.12 | Z-ISO | - |
Zea mays |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
5.2.1.12 | heme | isomerization depends upon a ferrous heme b cofactor that undergoes redox-regulated ligand-switching between the heme iron and alternate Z-ISO amino acid residues. Presence of a high-spin ferric heme and multiple low-spin hemes with broad EPR signals | Zea mays |