Control of carotenoid biosynthesis through a heme-based cis-trans isomerase
| Autor: | Eleanore T. Wurtzel, Maria Shumskaya, Masanori Sono, Jiafeng Geng, Anuja Modi, Jonathan P. Hosler, Aimin Liu, Brian Kloss, Jesús Beltrán, Charles Ampomah-Dwamena, John H. Dawson, J. Love |
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| Rok vydání: | 2015 |
| Předmět: |
Models
Molecular cis-trans-Isomerases 0106 biological sciences Chloroplasts Stereochemistry Iron Arabidopsis Gene Expression Heme Isomerase zeta Carotene Zea mays 01 natural sciences Article Cofactor 03 medical and health sciences chemistry.chemical_compound Isomerism Escherichia coli Molecular Biology Integral membrane protein Plant Proteins 030304 developmental biology chemistry.chemical_classification 0303 health sciences biology Arabidopsis Proteins Membrane Proteins food and beverages Cell Biology Recombinant Proteins Isoenzymes Heme B Enzyme chemistry Biochemistry Cis-trans-Isomerases biology.protein Hydrophobic and Hydrophilic Interactions Oxidation-Reduction Isomerization 010606 plant biology & botany |
| Zdroj: | Nature chemical biology |
| ISSN: | 1552-4469 1552-4450 |
| Popis: | Plants synthesize carotenoids, which are essential for plant development and survival. These metabolites also serve as essential nutrients for human health. The biosynthetic pathway for all plant carotenoids occurs in chloroplasts and other plastids and requires 15-cis-ζ-carotene isomerase (Z-ISO). It was not known whether Z-ISO catalyzes isomerization alone or in combination with other enzymes. Here we show that Z-ISO is a bona fide enzyme and integral membrane protein. Z-ISO independently catalyzes the cis-trans isomerization of the 15-15' carbon-carbon double bond in 9,15,9'-cis-ζ-carotene to produce the substrate required by the subsequent biosynthetic-pathway enzyme. We discovered that 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. Heme b-dependent isomerization of a large hydrophobic compound in a membrane was previously undescribed. As an isomerase, Z-ISO represents a new prototype for heme b proteins and potentially uses a new chemical mechanism. |
| Databáze: | OpenAIRE |
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