The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The requested identity is verified. Z-ISO (At1g10830; Q9SAC0) in Arabidopsis thaliana is the chloroplast-targeted, multipass membrane enzyme 15-cis-ζ-carotene isomerase (EC 5.2.1.12), not a similarly named protein from another organism. Its primary function is the stereospecific conversion of 9,15,9′-tri-cis-ζ-carotene into 9,9′-di-cis-ζ-carotene by isomerizing the central 15–15′ double bond from cis to trans. This reaction lies between phytoene desaturase (PDS) and ζ-carotene desaturase (ZDS) in plastidial carotenoid biosynthesis and is especially important when light cannot perform the equivalent photoisomerization. Genetic, metabolite, heterologous-expression, biochemical, and cross-species complementation evidence all support this annotation. (chen2010isolationandcharacterization pages 11-12, chen2010isolationandcharacterization pages 1-2, beltran2015controlofcarotenoid pages 1-2, proctor2022zetacaroteneisomerase(ziso) pages 10-12)
| Aspect | Best-supported conclusion | Evidence type | Confidence / caveat |
|---|---|---|---|
| Identity | Arabidopsis thaliana At1g10830 encodes Z-ISO, corresponding to UniProt Q9SAC0, a chloroplast-targeted 15-cis-ζ-carotene isomerase. | Mutant mapping, functional expression, proteomics, and cross-species complementation | High. The symbol, locus, organism, accession, and biochemical activity are concordant; no similarly named protein was substituted. |
| Catalytic reaction | Z-ISO isomerizes the central 15–15′ double bond of 9,15,9′-tri-cis-ζ-carotene to form 9,9′-di-cis-ζ-carotene. | Carotenoid profiling in mutants and engineered E. coli; biochemical reconstitution | High. The stereospecific substrate and product are directly supported. |
| Pathway position | Z-ISO acts after phytoene desaturase (PDS) and before ζ-carotene desaturase (ZDS) during the plastidial conversion of 15-cis-phytoene toward all-trans-lycopene. Its product supplies the 15-trans configuration required by ZDS. | Pathway genetics, metabolite accumulation, and heterologous pathway reconstruction | High. This is its primary physiological function. |
| Localization and topology | The precursor is imported into chloroplasts and functions as a multipass integral membrane protein in plastids. A transit-peptide cleavage near residue 58 and five to seven transmembrane helices have been predicted; the precise plastid membrane and experimentally resolved topology remain uncertain. | Chloroplast proteomics and sequence/topology prediction | High for plastid integral-membrane localization; moderate for cleavage position, helix count, and exact membrane compartment. |
| Cofactor and redox chemistry | Plant Z-ISO is a heme-b-dependent isomerase whose active state requires reduced, ferrous heme; redox-regulated axial-ligand switching has been proposed. | Purified maize Z-ISO in membrane/liposome systems, spectroscopy, mutagenesis, and comparative modeling | High for the plant-enzyme heme-b and ferrous dependence; moderate when transferred specifically to Arabidopsis because the decisive biochemical work used maize protein. |
| Structural mechanism | AlphaFold-guided models place the carotenoid and heme within a transmembrane cavity. H266 and H354 are leading candidate heme ligands, while H150 may participate near the substrate’s 15-cis bond rather than bind heme directly. | Computational docking plus comparative mutagenesis | Provisional. No experimentally determined Z-ISO structure is available, and residue-level assignments remain hypotheses. |
| Domain and evolution | Q9SAC0 contains the NnrU domain represented by InterPro IPR009915/Pfam PF07298. Plant Z-ISO likely evolved from an NnrU-like bacterial membrane protein, but ordinary denitrification-associated NnrU proteins do not necessarily possess carotenoid-isomerase activity. | Domain annotation, phylogenetics, gene-neighborhood analysis, and functional comparison | High for homology/domain membership; high that domain identity alone is insufficient to infer Z-ISO activity. |
| Loss-of-function evidence | Arabidopsis and maize loss-of-function mutants accumulate the tri-cis substrate, have impaired carotenoid synthesis, appear pale in darkness, and green slowly after illumination. Light can photochemically bypass part of the block but does not fully replace the enzyme. | Forward genetics, mutant metabolite profiling, and de-etiolation phenotyping | High. Phenotypes directly connect the gene to light-independent and efficient light-exposed carotenoid synthesis. |
| E. coli functional evidence | Full-length functional Arabidopsis Z-ISO converts most accumulated 9,15,9′-tri-cis-ζ-carotene to the di-cis product in engineered E. coli; a shortened alternative product and C-terminal mutant lack detectable activity. | Heterologous functional assay | High. Demonstrates catalytic sufficiency and the importance of the C-terminal region. |
| 2022 cross-species rescue | Arabidopsis At1g10830 lacking its predicted 58-residue transit peptide restored β-carotene synthesis in a Synechocystis Δslr1599 Z-ISO mutant under light-activated heterotrophic conditions. | In-vivo trans-complementation | High for conserved light-independent Z-ISO activity; the study did not report a quantitative Arabidopsis rescue efficiency. |
| Plastid-development signaling | In a carotenoid-isomerase-defective ccr2 background, ziso-155 prevents downstream cis-carotene formation and restores prolamellar bodies in more than 94% of etioplasts, supporting a cis-carotene-derived apocarotenoid signal that regulates etioplast/chloroplast development. | Arabidopsis epistasis, carotenoid profiling, microscopy, and de-etiolation measurements | High for the genetic interaction and altered metabolite requirement; the precise signaling molecule remains unidentified. This is a downstream consequence, not Z-ISO’s primary enzymatic reaction. |
| 2023–2024 research status | No major 2023–2024 Arabidopsis-specific study located in the reviewed literature materially revised At1g10830’s catalytic annotation. Recent crop and algal studies mainly treat Z-ISO ortholog expression as a carotenoid-pathway marker or engineering candidate. | Targeted recent-literature search | Moderate. This is a search-based absence statement, not proof that no relevant publication exists; ortholog findings should not be presented as direct At1g10830 evidence. |
Table: A concise evidence matrix distinguishing well-established annotation of Arabidopsis Z-ISO from topology, mechanistic, signaling, and recent-literature conclusions that retain important caveats.
The foundational 2010 study mapped the relevant Arabidopsis activity to At1g10830 and showed that its functional transcript, termed AtZ-ISO1.1, encodes an enzyme equivalent to maize Z-ISO. Expression in engineered Escherichia coli directly demonstrated the expected carotenoid-isomerase activity. The Arabidopsis protein represented by UniProt Q9SAC0 was subsequently used explicitly in AlphaFold-based comparative structural analysis. These observations establish agreement among locus, accession, organism, and biochemical function. (chen2010isolationandcharacterization pages 7-9, proctor2022zetacaroteneisomerase(ziso) pages 12-14, proctor2022zetacaroteneisomerase(ziso) pages 6-7)
The supplied InterPro/Pfam assignments—NnrU_dom, IPR009915; NnrU, PF07298—are consistent with the literature. Phylogenetic analysis places plant, algal, diatom, and cyanobacterial Z-ISO proteins in an NnrU-related lineage, probably recruited from an ancestral bacterial membrane protein. However, ordinary denitrification-associated bacterial NnrU proteins do not automatically possess Z-ISO activity: a bacterial NnrU tested alongside plant proteins lacked detectable carotenoid-isomerase activity. Thus, the domain supports ancestry and membrane architecture but is not alone sufficient for functional annotation. (chen2010isolationandcharacterization pages 1-2, chen2010isolationandcharacterization pages 7-9, chen2010isolationandcharacterization pages 6-7)
Arabidopsis also produces an alternatively processed transcript, AtZ-ISO1.2, containing retained intronic sequence, omission of the fourth exon, and a premature stop. Its altered C terminus has one fewer predicted membrane span and lacks detectable activity in the heterologous assay. The biologically supported catalytic product is therefore the full-length AtZ-ISO1.1 form. (chen2010isolationandcharacterization pages 6-7, chen2010isolationandcharacterization pages 9-11, chen2010isolationandcharacterization pages 7-9)
The reaction is:
9,15,9′-tri-cis-ζ-carotene → 9,9′-di-cis-ζ-carotene
Z-ISO changes the configuration of the central 15–15′ C=C bond from cis to trans without changing the carotenoid’s degree of desaturation. Its specificity is therefore both substrate- and double-bond-selective. In engineered E. coli accumulating the tri-cis substrate, full-length Arabidopsis Z-ISO converted most of it to the di-cis product, whereas the shortened splice product and a C-terminally truncated mutant protein did not. (chen2010isolationandcharacterization pages 1-2, chen2010isolationandcharacterization pages 9-11, chen2010isolationandcharacterization pages 7-9)
This step resolves an obligatory stereochemical mismatch in the plant poly-cis desaturation pathway. PDS produces 9,15,9′-tri-cis-ζ-carotene, whereas the next desaturase, ZDS, requires a carotenoid with the central bond in the 15-trans configuration. Z-ISO consequently acts after PDS and before ZDS, permitting continued desaturation and subsequent isomerization toward all-trans-lycopene, the branch-point precursor for α- and β-carotene and downstream xanthophylls. (chen2010isolationandcharacterization pages 11-12, beltran2015controlofcarotenoid pages 1-2, rosassaavedra2016biosynthesisofcarotenoids pages 11-14)
Biochemical reconstitution established plant Z-ISO as an unusual heme-b-dependent integral-membrane isomerase. Activity depends on reduced, ferrous heme, and spectroscopy supports redox-regulated switching of axial ligands to the heme iron. This is an unusual use of heme chemistry because the substrate is a large hydrophobic carotenoid embedded in a membrane rather than a conventional small redox substrate. The decisive purification and spectroscopy were performed primarily with maize Z-ISO; the strong sequence, structural, and functional conservation supports application of the general mechanism to Arabidopsis, but Arabidopsis Q9SAC0 itself has not been characterized to the same biochemical depth. (beltran2015controlofcarotenoid pages 1-2)
A 2022 AlphaFold and docking analysis predicted seven transmembrane helices in plant Z-ISO and highly similar Arabidopsis and maize folds, with backbone RMSD values of approximately 0.4–0.9 Å after transit-peptide removal. Arabidopsis docking produced candidate heme sites with estimated binding energies near −9 kcal mol⁻¹. Current models favor H266 and H354 as possible axial heme ligands, while H150 may instead lie near the substrate’s 15-cis bond and have a catalytic or structural role. These residue-level assignments remain provisional because no experimental Z-ISO structure has yet resolved the heme and carotenoid sites. (proctor2022zetacaroteneisomerase(ziso) pages 14-15, proctor2022zetacaroteneisomerase(ziso) pages 15-17, proctor2022zetacaroteneisomerase(ziso) pages 6-7)
At1g10830 encodes a precursor with a predicted chloroplast transit-peptide cleavage near residue 58. Chloroplast proteomics, targeting predictions, and the known plastid localization of carotenoid synthesis support import into chloroplasts and other carotenoid-producing plastids. The mature protein is a multipass integral membrane protein. Early sequence analysis predicted five membrane-spanning segments; newer AlphaFold-guided topology predicts seven. This difference reflects method-dependent prediction rather than disagreement over its fundamental membrane localization. (chen2010isolationandcharacterization pages 6-7, chen2010isolationandcharacterization pages 9-11, proctor2022zetacaroteneisomerase(ziso) pages 14-15)
The exact plastid membrane—envelope versus thylakoid—and experimentally validated orientation remain less certain. Reviews describe the specific membrane assignment as unresolved, although Z-ISO has also been detected in an approximately 480-kDa complex. The most defensible annotation is therefore chloroplast/plastid integral membrane, without assigning a unique membrane compartment. (rosassaavedra2016biosynthesisofcarotenoids pages 11-14)
Arabidopsis loss-of-function alleles accumulate 9,15,9′-tri-cis-ζ-carotene, exactly the predicted substrate, and exhibit impaired carotenoid synthesis. Dark-grown mutant tissues are pale or light yellow, and seedlings show delayed greening after illumination. Carotenoid and chlorophyll levels can remain reduced even in light, demonstrating that environmental photoisomerization only partially bypasses the enzymatic step. (chen2010isolationandcharacterization pages 11-12)
Two molecular alleles illustrate the importance of intact protein architecture. zic1-1 contains a 10-bp deletion in exon 4 that alters the C terminus and introduces a new stop codon; zic1-2 contains a 20-bp intronic deletion that causes aberrant splicing, although trace wild-type transcript remains. The inactive zic1-1 product and inactive shortened alternative transcript support a requirement for the normal C-terminal membrane region. (chen2010isolationandcharacterization pages 6-7, chen2010isolationandcharacterization pages 7-9)
Full-length AtZ-ISO1.1 was sufficient to perform the reaction in a reconstructed bacterial carotenoid pathway, separating catalytic activity from broader plant developmental effects. In 2022, Arabidopsis At1g10830 with its predicted 58-residue transit peptide removed also rescued β-carotene formation in a Synechocystis Δslr1599 Z-ISO mutant under light-activated heterotrophic growth. This in-vivo complementation demonstrates conservation of the light-independent reaction across oxygenic phototrophs. The study did not report a quantitative Arabidopsis rescue efficiency. (chen2010isolationandcharacterization pages 9-11, proctor2022zetacaroteneisomerase(ziso) pages 10-12)
At1g10830 transcript is most abundant in green leaves; Arabidopsis root expression was reported to be approximately fourfold lower. Seedling expression increases with light and falls when the night is extended. This pattern is consistent with demand for carotenoid synthesis in photosynthetic organs but does not imply that the enzyme is dispensable in darkness—indeed, the absence of photochemical rescue makes its catalytic role especially evident in dark or non-green tissues. (chen2010isolationandcharacterization pages 6-7)
Z-ISO is part of the plastidial pathway converting phytoene to lycopene. Its direct contribution is to maintain flux through the PDS–Z-ISO–ZDS sequence; downstream carotenoids then support photosystem assembly, light harvesting, quenching of reactive excited states, photoprotection, coloration, and production of apocarotenoid hormones such as abscisic acid and strigolactones. These downstream roles explain broad mutant phenotypes, but they should not be mistaken for additional catalytic activities of Z-ISO. (moise2014mechanisticaspectsof pages 15-16, rosassaavedra2016biosynthesisofcarotenoids pages 11-14)
Light can directly photoisomerize the labile 15-cis bond, explaining why early pathway schemes considered an enzyme unnecessary. Mutant studies showed, however, that photochemistry is incomplete and unavailable in endosperm, roots, etiolated seedlings, internal fruit tissue, and other poorly illuminated plastids. Z-ISO is therefore indispensable for light-independent carotenoid production and improves pathway efficiency even in illuminated tissues. (chen2010isolationandcharacterization pages 11-12, beltran2015controlofcarotenoid pages 1-2)
A 2020 Arabidopsis epistasis study used ziso-155, a G→A mutation in exon 3 of At1g10830 producing a 212-amino-acid protein rather than the 367-amino-acid full-length protein. In the crtiso/ccr2 background, loss of Z-ISO prevented production of downstream cis-carotenes: the double mutant accumulated a Z-ISO-like mixture dominated by 9,15,9′-tri-cis-ζ-carotene, phytofluene, and phytoene, while neurosporene isomers, tetra-cis-lycopene, and di-cis-ζ-carotene were absent. (cazzonelli2020aciscarotenederived pages 8-9, cazzonelli2020aciscarotenederived pages 9-10)
Remarkably, this metabolic block restored prolamellar-body formation in more than 94% of ccr2 ziso etioplasts and brought chlorophyll toward wild-type levels after 48–72 hours of de-etiolation. The genetic interpretation is that a downstream cis-carotene, or a cleavage-derived apocarotenoid, acts as a retrograde signal regulating etioplast and chloroplast development in parallel with DET1 and affecting POR, PIF3, and HY5 protein regulation. The exact signaling molecule remains unidentified. This is important biology revealed using Z-ISO, but it is a consequence of changing pathway intermediates rather than evidence that Z-ISO itself is a signaling protein. (cazzonelli2020aciscarotenederived pages 8-9, cazzonelli2020aciscarotenederived pages 21-22)
A targeted search did not identify a 2023–2024 primary study that materially changes the catalytic annotation of Arabidopsis At1g10830. The latest substantial mechanistic development recovered was the 2022 study combining cyanobacterial genetics, Arabidopsis complementation, and AlphaFold-guided analysis. It strengthened cross-lineage functional conservation and proposed revised heme-ligand and substrate-site models, but explicitly did not replace the need for an experimentally determined structure. (proctor2022zetacaroteneisomerase(ziso) pages 14-15, proctor2022zetacaroteneisomerase(ziso) pages 15-17, proctor2022zetacaroteneisomerase(ziso) pages 10-12)
Recent crop and algal omics papers frequently identify Z-ISO/ZCIS ortholog expression as part of carotenoid accumulation, fruit coloration, stress response, or β-carotene production. Such studies establish applied relevance of the conserved reaction but are not direct evidence about Arabidopsis Q9SAC0. Accordingly, ortholog-based 2023–2024 findings should not be used to revise At1g10830 substrate specificity, localization, or mechanism without direct validation.
Nutritional biofortification. Z-ISO must be considered when engineering β-carotene and provitamin-A pathways into poorly illuminated tissues such as cereal endosperm. Adding upstream phytoene synthesis and desaturation without adequate Z-ISO activity can create a stereochemical bottleneck at tri-cis-ζ-carotene. This application was a major rationale for identifying the missing enzyme. (chen2010isolationandcharacterization pages 1-2, beltran2015controlofcarotenoid pages 1-2)
Crop color and carotenoid content. Because Z-ISO supplies the ZDS substrate, altered expression or activity can change pathway flux, pigmentation, and availability of downstream carotenoids. Arabidopsis provides the mechanistic reference, while translation to fruit or grain requires direct testing of the relevant crop ortholog.
Synthetic biology and microbial production. AtZ-ISO functions in engineered E. coli and in a cyanobacterial deletion strain, demonstrating portability into heterologous carotenoid pathways. Its membrane integration, heme requirement, transit-peptide removal, and cellular redox environment are practical design constraints. (chen2010isolationandcharacterization pages 9-11, proctor2022zetacaroteneisomerase(ziso) pages 10-12)
Pathway and signaling research. Z-ISO mutants provide a precise means of stopping carotenoid flux before di-cis-ζ-carotene. This has enabled causal tests of cis-carotene-derived retrograde signaling during plastid development. (cazzonelli2020aciscarotenederived pages 8-9, cazzonelli2020aciscarotenederived pages 21-22)
The following conclusions are strongly established: At1g10830/Q9SAC0 identity; chloroplast/plastid targeting; integral-membrane character; conversion of 9,15,9′-tri-cis-ζ-carotene to 9,9′-di-cis-ζ-carotene; placement between PDS and ZDS; NnrU-domain ancestry; and importance for light-independent carotenoid biosynthesis. (chen2010isolationandcharacterization pages 11-12, chen2010isolationandcharacterization pages 6-7, chen2010isolationandcharacterization pages 7-9)
The principal uncertainties are the exact plastid membrane, definitive topology, atomic structure, identities and dynamics of Arabidopsis heme ligands, detailed catalytic proton/electron movements, and the chemical identity of the downstream cis-carotene-derived developmental signal. Quantitative steady-state kinetic constants for purified Arabidopsis Q9SAC0 were not found in the retrieved evidence. Thus, the correct functional annotation is precise at the reaction and pathway levels but still incomplete at atomic-mechanistic resolution.
References
(chen2010isolationandcharacterization pages 11-12): Yu Chen, Faqiang Li, and Eleanore T. Wurtzel. Isolation and characterization of the z-iso gene encoding a missing component of carotenoid biosynthesis in plants. Plant Physiology, 153:66-79, Mar 2010. URL: https://doi.org/10.1104/pp.110.153916, doi:10.1104/pp.110.153916. This article has 301 citations and is from a highest quality peer-reviewed journal.
(chen2010isolationandcharacterization pages 1-2): Yu Chen, Faqiang Li, and Eleanore T. Wurtzel. Isolation and characterization of the z-iso gene encoding a missing component of carotenoid biosynthesis in plants. Plant Physiology, 153:66-79, Mar 2010. URL: https://doi.org/10.1104/pp.110.153916, doi:10.1104/pp.110.153916. This article has 301 citations and is from a highest quality peer-reviewed journal.
(beltran2015controlofcarotenoid pages 1-2): Jesús Beltrán, Brian Kloss, Jonathan P Hosler, Jiafeng Geng, Aimin Liu, Anuja Modi, John H Dawson, Masanori Sono, Maria Shumskaya, Charles Ampomah-Dwamena, James D Love, and Eleanore T Wurtzel. Control of carotenoid biosynthesis through a heme-based cis-trans isomerase. Jun 2015. URL: https://doi.org/10.1038/nchembio.1840, doi:10.1038/nchembio.1840. This article has 102 citations and is from a highest quality peer-reviewed journal.
(proctor2022zetacaroteneisomerase(ziso) pages 10-12): Matthew S. Proctor, Felix S. Morey-Burrows, Daniel P. Canniffe, Elizabeth C. Martin, David J. K. Swainsbury, Matthew P. Johnson, C. Neil Hunter, George A. Sutherland, and Andrew Hitchcock. Zeta-carotene isomerase (z-iso) is required for light-independent carotenoid biosynthesis in the cyanobacterium synechocystis sp. pcc 6803. Microorganisms, 10:1730, Aug 2022. URL: https://doi.org/10.3390/microorganisms10091730, doi:10.3390/microorganisms10091730. This article has 12 citations.
(chen2010isolationandcharacterization pages 7-9): Yu Chen, Faqiang Li, and Eleanore T. Wurtzel. Isolation and characterization of the z-iso gene encoding a missing component of carotenoid biosynthesis in plants. Plant Physiology, 153:66-79, Mar 2010. URL: https://doi.org/10.1104/pp.110.153916, doi:10.1104/pp.110.153916. This article has 301 citations and is from a highest quality peer-reviewed journal.
(proctor2022zetacaroteneisomerase(ziso) pages 12-14): Matthew S. Proctor, Felix S. Morey-Burrows, Daniel P. Canniffe, Elizabeth C. Martin, David J. K. Swainsbury, Matthew P. Johnson, C. Neil Hunter, George A. Sutherland, and Andrew Hitchcock. Zeta-carotene isomerase (z-iso) is required for light-independent carotenoid biosynthesis in the cyanobacterium synechocystis sp. pcc 6803. Microorganisms, 10:1730, Aug 2022. URL: https://doi.org/10.3390/microorganisms10091730, doi:10.3390/microorganisms10091730. This article has 12 citations.
(proctor2022zetacaroteneisomerase(ziso) pages 6-7): Matthew S. Proctor, Felix S. Morey-Burrows, Daniel P. Canniffe, Elizabeth C. Martin, David J. K. Swainsbury, Matthew P. Johnson, C. Neil Hunter, George A. Sutherland, and Andrew Hitchcock. Zeta-carotene isomerase (z-iso) is required for light-independent carotenoid biosynthesis in the cyanobacterium synechocystis sp. pcc 6803. Microorganisms, 10:1730, Aug 2022. URL: https://doi.org/10.3390/microorganisms10091730, doi:10.3390/microorganisms10091730. This article has 12 citations.
(chen2010isolationandcharacterization pages 6-7): Yu Chen, Faqiang Li, and Eleanore T. Wurtzel. Isolation and characterization of the z-iso gene encoding a missing component of carotenoid biosynthesis in plants. Plant Physiology, 153:66-79, Mar 2010. URL: https://doi.org/10.1104/pp.110.153916, doi:10.1104/pp.110.153916. This article has 301 citations and is from a highest quality peer-reviewed journal.
(chen2010isolationandcharacterization pages 9-11): Yu Chen, Faqiang Li, and Eleanore T. Wurtzel. Isolation and characterization of the z-iso gene encoding a missing component of carotenoid biosynthesis in plants. Plant Physiology, 153:66-79, Mar 2010. URL: https://doi.org/10.1104/pp.110.153916, doi:10.1104/pp.110.153916. This article has 301 citations and is from a highest quality peer-reviewed journal.
(rosassaavedra2016biosynthesisofcarotenoids pages 11-14): Carolina Rosas-Saavedra and Claudia Stange. Biosynthesis of carotenoids in plants: enzymes and color. Sub-cellular biochemistry, 79:35-69, Jan 2016. URL: https://doi.org/10.1007/978-3-319-39126-7_2, doi:10.1007/978-3-319-39126-7_2. This article has 136 citations.
(proctor2022zetacaroteneisomerase(ziso) pages 14-15): Matthew S. Proctor, Felix S. Morey-Burrows, Daniel P. Canniffe, Elizabeth C. Martin, David J. K. Swainsbury, Matthew P. Johnson, C. Neil Hunter, George A. Sutherland, and Andrew Hitchcock. Zeta-carotene isomerase (z-iso) is required for light-independent carotenoid biosynthesis in the cyanobacterium synechocystis sp. pcc 6803. Microorganisms, 10:1730, Aug 2022. URL: https://doi.org/10.3390/microorganisms10091730, doi:10.3390/microorganisms10091730. This article has 12 citations.
(proctor2022zetacaroteneisomerase(ziso) pages 15-17): Matthew S. Proctor, Felix S. Morey-Burrows, Daniel P. Canniffe, Elizabeth C. Martin, David J. K. Swainsbury, Matthew P. Johnson, C. Neil Hunter, George A. Sutherland, and Andrew Hitchcock. Zeta-carotene isomerase (z-iso) is required for light-independent carotenoid biosynthesis in the cyanobacterium synechocystis sp. pcc 6803. Microorganisms, 10:1730, Aug 2022. URL: https://doi.org/10.3390/microorganisms10091730, doi:10.3390/microorganisms10091730. This article has 12 citations.
(moise2014mechanisticaspectsof pages 15-16): Alexander R. Moise, Salim Al-Babili, and Eleanore T. Wurtzel. Mechanistic aspects of carotenoid biosynthesis. Chemical reviews, 114 1:164-93, Jan 2014. URL: https://doi.org/10.1021/cr400106y, doi:10.1021/cr400106y. This article has 396 citations and is from a highest quality peer-reviewed journal.
(cazzonelli2020aciscarotenederived pages 8-9): Christopher I Cazzonelli, Xin Hou, Yagiz Alagoz, John Rivers, Namraj Dhami, Jiwon Lee, Shashikanth Marri, and Barry J Pogson. A cis-carotene derived apocarotenoid regulates etioplast and chloroplast development. Jan 2020. URL: https://doi.org/10.7554/elife.45310, doi:10.7554/elife.45310. This article has 92 citations and is from a domain leading peer-reviewed journal.
(cazzonelli2020aciscarotenederived pages 9-10): Christopher I Cazzonelli, Xin Hou, Yagiz Alagoz, John Rivers, Namraj Dhami, Jiwon Lee, Shashikanth Marri, and Barry J Pogson. A cis-carotene derived apocarotenoid regulates etioplast and chloroplast development. Jan 2020. URL: https://doi.org/10.7554/elife.45310, doi:10.7554/elife.45310. This article has 92 citations and is from a domain leading peer-reviewed journal.
(cazzonelli2020aciscarotenederived pages 21-22): Christopher I Cazzonelli, Xin Hou, Yagiz Alagoz, John Rivers, Namraj Dhami, Jiwon Lee, Shashikanth Marri, and Barry J Pogson. A cis-carotene derived apocarotenoid regulates etioplast and chloroplast development. Jan 2020. URL: https://doi.org/10.7554/elife.45310, doi:10.7554/elife.45310. This article has 92 citations and is from a domain leading peer-reviewed journal.