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Literature summary extracted from

  • Beltran, J.; Kloss, B.; Hosler, J.P.; Geng, J.; Liu, A.; Modi, A.; Dawson, J.H.; Sono, M.; Shumskaya, M.; Ampomah-Dwamena, C.; Love, J.D.; Wurtzel, E.T.
    Control of carotenoid biosynthesis through a heme-based cis-trans isomerase (2015), Nat. Chem. Biol., 11, 598-605 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.2.1.12 homology modeling of structure Zea mays

Localization

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
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.2.1.12 Iron
-
Zea mays

Organism

EC Number Organism UniProt Comment Textmining
5.2.1.12 Zea mays B4FHU1
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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
-
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Synonyms

EC Number Synonyms Comment Organism
5.2.1.12 Z-ISO
-
Zea mays

Cofactor

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