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Literature summary for 5.2.1.12 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
Search for more literature for 5.2.1.12

Activating Compound

Activating Compound Comment Organism Structure
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)

Crystallization (Comment) Organism
homology modeling of structure Zea mays

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
 Zea mays 9507
-
membrane integral membrane protein Zea mays 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Iron
-
 Zea mays

Organism

Organism UniProt Comment Textmining
Zea mays B4FHU1
-
-

Purification (Commentary)

Purification (Comment) Organism
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
9,15,9'-tricis-zeta-carotene
-
 Zea mays 9,9'-dicis-zeta-carotene
-
 ?

Synonyms

Synonyms Comment Organism
Z-ISO
-
 Zea mays

Cofactor

Cofactor Comment Organism Structure
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