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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 identity check is positive. P21685 is the bacterial gene product CrtI from Pantoea ananatis (historically Erwinia uredovora), not an unrelated protein sharing the symbol crtI. A 2024 study explicitly identifies P21685 as PaCrtI, while the foundational E. uredovora genetics and later P. ananatis biochemical work converge on the same function: a lycopene-forming, four-step phytoene desaturase. Its experimentally determined amino-oxidase-like flavoprotein structure also agrees with the supplied InterPro/Pfam assignments. (misawa1990elucidationofthe pages 1-2, castanocerezo2024combiningsystemsand pages 4-5)
PaCrtI is a peripheral membrane-associated, FAD-dependent oxidase/isomerase. It converts membrane-embedded 15-cis-phytoene through phytofluene, ζ-carotene, and neurosporene into all-trans-lycopene, introducing four additional conjugated double bonds and accomplishing the necessary cis–trans isomerization. Oxygen is the principal terminal electron acceptor in the purified aerobic assay; suitable quinones can replace oxygen anaerobically. (schaub2012onthestructure pages 2-3, schaub2012onthestructure pages 3-5, schaub2012onthestructure pages 1-2, misawa1990elucidationofthe pages 1-2)
| Annotation aspect | Best-supported conclusion | Evidence type | Key quantitative datum |
|---|---|---|---|
| Exact identity | P21685 is PaCrtI, the lycopene-forming phytoene desaturase from Pantoea ananatis (historically Erwinia uredovora); this is not evidence about similarly named CrtI homologs. (misawa1990elucidationofthe pages 1-2, castanocerezo2024combiningsystemsand pages 4-5) | Direct accession identification plus historical functional genetics | Recombinant monomer reported at approximately 56.04 kDa. (schaub2012onthestructure pages 2-3) |
| Primary reaction and intermediates | One CrtI polypeptide performs four sequential desaturations of 15-cis-phytoene through phytofluene, ζ-carotene, and neurosporene to all-trans-lycopene, coupled to cis–trans isomerization. (schaub2012onthestructure pages 1-2, misawa1990elucidationofthe pages 1-2) | Direct biochemical; heterologous pathway genetics | Four desaturation steps; intermediates do not appreciably accumulate in the purified liposome assay. (schaub2012onthestructure pages 2-3) |
| Substrate specificity and kinetics | The physiological hydrophobic substrate is membrane-embedded 15-cis-phytoene; reduced enzyme can additionally isomerize cis-carotenes anaerobically. (schaub2012onthestructure pages 2-3, schaub2012onthestructure pages 3-5) | Direct biochemical | Apparent phytoene Kₘ <16.7 ± 1.9 µM; reported Vmax <226 ± 19 pmol·min⁻¹ under the assay conditions. (schaub2012onthestructure pages 2-3) |
| FAD, oxygen, and quinones | FAD is the sole identified redox cofactor and also supports formation of active membrane-associated enzyme. Electrons flow from phytoene through FAD to O₂; quinones can substitute anaerobically. (schaub2012onthestructure pages 1-2, schaub2012onthestructure pages 6-8) | Direct biochemical | Apparent FAD Kₘ = 50.5 ± 2.9 µM; duroquinone and O₂ supported approximately 2.2 versus 2.4 pmol lycopene·mg⁻¹·min⁻¹. (schaub2012onthestructure pages 2-3, schaub2012onthestructure pages 3-5) |
| Cellular localization | CrtI is a peripheral membrane-associated, rather than integral transmembrane, oxidoreductase; association with a carotenoid-containing lipid bilayer provides access to its highly hydrophobic substrate. (schaub2012onthestructure pages 2-3, schaub2012onthestructure pages 1-2) | Direct biochemical and membrane-reconstitution evidence | High activity was reconstituted with phytoene embedded in phosphatidylcholine liposomes; no subcellular fraction percentage was reported. (schaub2012onthestructure pages 1-2) |
| Structure and domains | PDB 4DGK exhibits an amino-oxidase-like flavoprotein architecture with FAD-binding, substrate-binding, and helical/membrane-interaction regions, consistent with the annotated Amino_oxidase, carotenoid/retinoid oxidoreductase, and FAD/NAD-binding-superfamily domains. (schaub2012onthestructure pages 8-9, schaub2012onthestructure pages 5-6) | Direct crystallography plus domain inference | Apo structure refined to 2.35 Å; 19 β-strands, 12 α-helices, and three 3₁₀-helices. (schaub2012onthestructure pages 5-6, schaub2012onthestructure pages 13-14) |
| Native pathway and gene cluster | CrtI supplies lycopene to downstream CrtY-mediated β-cyclization in the carotenoid pathway. In strain PA13, crtI occurs in a plasmid-borne crtE–X–Y–I–B–Z cluster; cluster-level carotenoid expression is controlled through quorum sensing/Hfq/RpoS circuitry. (choi2021pantoeaananatiscarotenoid pages 2-4, choi2021pantoeaananatiscarotenoid pages 8-9) | Native cluster/regulatory evidence; effects are pathway-level, not P21685-specific biochemistry | Reassembled crtE-B, crtE-B-I, and crtE-B-I-Y modules produced phytoene, lycopene, and β-carotene, respectively, in E. coli. (choi2021pantoeaananatiscarotenoid pages 8-9) |
| 2024 in-vivo enzymology | A 2024 study explicitly examined P21685/PaCrtI in engineered Saccharomyces cerevisiae, demonstrating a systems-biology strategy for measuring difficult membrane-associated carotenoid enzymes under intracellular conditions. (castanocerezo2024combiningsystemsand pages 4-5) | Direct accession-specific heterologous in-vivo study | Engineered strains spanned 4–1,641 µM phytoene, a 430-fold concentration range; the available excerpt does not report a PaCrtI-specific in-vivo Kₘ or kcat. (castanocerezo2024combiningsystemsand pages 4-5) |
| Plant biofortification | Plastid-targeted bacterial CrtI has been used to bypass the multi-enzyme plant desaturation/isomerization sequence, including in Golden Rice. Reported crop outcomes reflect the entire engineered pathway, particularly combined PSY and crtI expression, not CrtI alone. (schaub2012onthestructure pages 1-2, naik2024biofortificationasa pages 4-5) | Whole-pathway application | Golden Rice 2 reportedly achieved a 23-fold increase in total carotenoids relative to the original Golden Rice through maize PSY plus bacterial CrtI. (naik2024biofortificationasa pages 4-5) |
| Transient lycopene production | A viral vector expressing P. ananatis crtE, crtB, and crtI rewired tobacco-leaf metabolism to produce lycopene; the yield cannot be attributed specifically to CrtI. (majer2017rewiringcarotenoidbiosynthesis pages 6-6) | Whole-pathway plant application | Approximately 150 µg lycopene·g⁻¹ dry weight. (majer2017rewiringcarotenoidbiosynthesis pages 6-6) |
Table: Evidence-graded functional annotation of PaCrtI, separating accession-specific biochemical and structural findings from native-pathway observations and whole-pathway engineering outcomes.
The symbol crtI matches the supplied protein description: bacterial/fungal-type, lycopene-forming phytoene desaturase, also called phytoene dehydrogenase or four-step phytoene desaturase. The original functional-genetics study analyzed crtI in Erwinia uredovora strain 20D3/ATCC 19321. Later biochemical and structural work identifies the organism under its accepted name, Pantoea ananatis, and the 2024 in-vivo enzymology study explicitly identifies P21685 as PaCrtI. (misawa1990elucidationofthe pages 1-2, castanocerezo2024combiningsystemsand pages 4-5)
This distinction matters because crtI is a generic pathway-gene symbol used for many bacterial and fungal phytoene desaturases. Results concerning Pantoea agglomerans, Rhodobacter, Rubrivivax, fungi, or other CrtI homologs should not automatically be assigned to P21685. For example, heterologous studies show that CrtI homologs can stop at neurosporene, extend desaturation beyond lycopene, or change product distributions with pathway context. Those findings illustrate family diversity but do not redefine P21685. (song2013heterologouscarotenoidbiosyntheticenzymes pages 1-2, song2013heterologouscarotenoidbiosyntheticenzymes pages 3-4)
The supplied Amino_oxidase/PF01593, carotenoid-retinoid oxidoreductase, and FAD/NAD-binding-superfamily annotations agree with crystallography. Apo-PaCrtI has an amino-oxidase-like flavoprotein fold organized into an FAD-binding region, a substrate-binding region, and a predominantly helical region implicated in membrane interaction. The structure contains 19 β-strands, 12 α-helices, and three 3₁₀-helices; PDB 4DGK was refined to 2.35 Å in the reported structural analysis. (schaub2012onthestructure pages 8-9, schaub2012onthestructure pages 5-6, schaub2012onthestructure pages 13-14)
Thus, the domain evidence supports—not merely predicts—the supplied functional annotation.
PaCrtI converts the colorless C40 carotene 15-cis-phytoene to red all-trans-lycopene. Functional reconstruction in E. coli originally showed that one CrtI gene product conducts four sequential desaturations through:
15-cis-phytoene → phytofluene → ζ-carotene → neurosporene → all-trans-lycopene. (misawa1990elucidationofthe pages 1-2)
Purified-protein assays subsequently confirmed production of all-trans-lycopene from 15-cis-phytoene in phosphatidylcholine liposomes. Appreciable quantities of the intermediates did not accumulate in that assay, consistent with efficient repeated processing by the same enzyme. The overall transformation includes four dehydrogenations and a cis–trans isomerization. (schaub2012onthestructure pages 2-3, schaub2012onthestructure pages 1-2)
The best-supported physiological substrate is 15-cis-phytoene embedded in a lipid bilayer. The requirement for a membrane-like presentation is biologically sensible because phytoene and later carotene intermediates are extremely hydrophobic. Purified soluble enzyme became highly active when presented with phytoene-containing phosphatidylcholine liposomes. (schaub2012onthestructure pages 2-3, schaub2012onthestructure pages 1-2)
PaCrtI also has a conditional isomerase activity. Under anaerobic, reducing conditions, reduced-FAD enzyme isomerized tetra-cis-lycopene/prolycopene to tri-cis- and smaller amounts of other cis-lycopene species. It did not comparably isomerize 15-cis-phytoene under the tested CRTISO-like conditions. This is secondary mechanistic activity rather than evidence that cis-lycopene is its principal physiological substrate. (schaub2012onthestructure pages 3-5, schaub2012onthestructure pages 8-9)
Reported apparent parameters in the liposome assay were a phytoene Kₘ below 16.7 ± 1.9 µM, FAD Kₘ of 50.5 ± 2.9 µM, and Vmax below 226 ± 19 pmol·min⁻¹ under the specified experimental conditions. The “below” qualification should be retained because substrate availability in a two-phase membrane system limits interpretation as conventional solution kinetics. (schaub2012onthestructure pages 2-3)
FAD is the sole demonstrated redox-active cofactor; no additional metal or cofactor was required. Electrons removed during carotene desaturation pass to enzyme-associated FAD and then to a terminal acceptor. FAD is also required during productive membrane association: enzyme associated with membranes without FAD was inactive and could not simply be rescued later by adding FAD. This led the structural investigators to characterize FAD as both catalytic and architectural. (schaub2012onthestructure pages 1-2, schaub2012onthestructure pages 6-8)
Under aerobic assay conditions, molecular oxygen serves as the terminal acceptor, making PaCrtI operationally a phytoene:oxygen oxidoreductase/oxidase. Under anaerobic conditions, quinones can substitute. Benzoquinones generally performed better than naphthoquinones, with optimal midpoint potentials around 0–100 mV. Duroquinone and oxygen supported similar reported activity—approximately 2.2 versus 2.4 pmol lycopene·mg⁻¹·min⁻¹ in the cited comparison. (schaub2012onthestructure pages 3-5, schaub2012onthestructure pages 8-9, schaub2012onthestructure pages 6-8)
Whether oxygen or a membrane quinone is the dominant acceptor in native P. ananatis cells has not been established as firmly as the purified-enzyme result. The defensible annotation is therefore: oxygen is directly demonstrated in vitro, and quinones are competent alternatives under oxygen limitation.
Structural docking places FAD’s isoalloxazine ring and the carotene chain within a shared tunnel-like cavity. Conserved residues including Asp149 and nearby arginines have been proposed to participate in base-assisted dehydrogenation or substrate polarization, while reduced FAD may stabilize a carbocation during isomerization. Histidine substitutions changed the extent/product specificity of desaturation without abolishing all activity. These residue-level mechanisms remain a combination of structural modeling and mutagenic inference rather than a fully resolved catalytic sequence. (schaub2012onthestructure pages 6-8, schaub2012onthestructure pages 13-14)
PaCrtI is best annotated as a cytoplasmic-side peripheral membrane protein, not an integral transmembrane transporter or secreted enzyme. Purified CrtI is soluble and approximately 56.04 kDa as a monomer, but catalysis requires association with a lipid bilayer carrying its hydrophobic carotene substrate. Liposome reconstitution, membrane washing, FAD-dependent holoenzyme formation, and the structure’s helical membrane-interaction region collectively support this assignment. (schaub2012onthestructure pages 2-3, schaub2012onthestructure pages 1-2, schaub2012onthestructure pages 5-6)
The precise native bacterial membrane leaflet and quantitative partitioning between soluble and membrane-associated pools have not been resolved in the retrieved studies. “Peripheral inner-membrane associated” is therefore a biologically likely interpretation, while “membrane-peripheral” is the directly demonstrated statement.
CrtB first condenses geranylgeranyl diphosphate-derived precursors to phytoene. CrtI then creates lycopene’s extended conjugated system; CrtY can cyclize lycopene to β-carotene, after which hydroxylation and glycosylation generate downstream xanthophylls. Reconstruction experiments support this ordering: crtE-B produced phytoene, crtE-B-I produced lycopene, and crtE-B-I-Y produced β-carotene. (misawa1990elucidationofthe pages 1-2, choi2021pantoeaananatiscarotenoid pages 8-9)
In P. ananatis PA13, carotenoid genes occur in a plasmid-borne crtE–X–Y–I–B–Z region. Cluster-level carotenoid synthesis is governed by an Hfq/quorum-sensing/RpoS network: AHL signaling relieves EanR repression, Hfq supports quorum signaling, and RpoS promotes carotenoid production. These are pathway-regulatory findings, not evidence that CrtI itself acts as a signaling protein. (choi2021pantoeaananatiscarotenoid pages 2-4, choi2021pantoeaananatiscarotenoid pages 8-9)
Native P. ananatis carotenoid production confers tolerance to UV radiation and toxoflavin, consistent with carotenoids functioning as membrane-associated antioxidant and photoprotective pigments. However, those phenotypes were established at the carotenoid-pathway level; they should not be interpreted as isolated, CrtI-specific pleiotropic activities. CrtI’s precise contribution is catalytic: without phytoene desaturation, the conjugated colored carotenoids required for these protective effects cannot be formed. (choi2021pantoeaananatiscarotenoid pages 2-4, choi2021pantoeaananatiscarotenoid pages 8-9)
The most important accession-specific recent development is Castaño-Cerezo et al., published in September 2024 in The EMBO Journal. The investigators explicitly studied P21685/PaCrtI in engineered Saccharomyces cerevisiae, alongside fungal desaturases, using strains spanning intracellular phytoene concentrations of 4–1,641 µM, a 430-fold range. The work demonstrates a systems/synthetic-biology route to characterize hydrophobic, membrane-associated enzymes under intracellular conditions where conventional purified-enzyme parameters may not reflect physiology. (castanocerezo2024combiningsystemsand pages 4-5)
The accessible evidence does not supply a PaCrtI-specific in-vivo Kₘ, Vmax, or kcat from that paper, so such values should not be inferred. Its major current contribution is methodological: it places P21685 in a quantitative cellular context and highlights the importance of substrate availability, expression burden, membrane storage, and product toxicity when interpreting carotenoid-enzyme performance. (castanocerezo2024combiningsystemsand pages 4-5)
A May 2024 biofortification review confirms continued importance of bacterial CrtI in Golden Rice. Golden Rice 2, combining bacterial CrtI with maize PSY, reportedly achieved a 23-fold increase in total carotenoids relative to the original Golden Rice. This is a combined-pathway outcome and cannot be attributed to CrtI alone. DOI: 10.1016/j.heliyon.2024.e30595. (naik2024biofortificationasa pages 4-5)
Recent carotenoid-production research increasingly treats membrane capacity as an engineering variable. A 2024 E. coli study reported that chromosomal installation of an upstream isopentenol-utilization pathway increased specific lycopene yield approximately 2.0–2.1-fold, while membrane-lipid engineering raised lipid content by 31–33% but had context-dependent effects on lycopene. These data are relevant to PaCrtI deployment because its substrate, enzyme complex, and product are membrane-associated, but that study is production-system evidence rather than direct characterization of P21685.
Plastid-targeted bacterial CrtI replaces the plant requirement for separate PDS, ZDS, Z-ISO, and CRTISO activities between phytoene and lycopene. This compact function has enabled provitamin-A engineering in rice and has also been deployed experimentally in maize, tomato, potato, and tobacco. Its best-known implementation is Golden Rice, where CrtI operates with phytoene synthase and endogenous downstream cyclization to produce β-carotene in endosperm. (schaub2012onthestructure pages 1-2, naik2024biofortificationasa pages 4-5)
A January 2017 viral-vector study expressed the P. ananatis crtE, crtB, and crtI pathway in tobacco leaves and obtained approximately 150 µg lycopene·g⁻¹ dry weight. This demonstrates rapid, transient rewiring of plant metabolism, although the yield is attributable to the three-enzyme pathway rather than CrtI in isolation. DOI: 10.1038/srep41645. (majer2017rewiringcarotenoidbiosynthesis pages 6-6)
PaCrtI is widely useful as a synthetic-biology module because one enzyme supplies all four phytoene desaturation steps. In engineered bacteria and yeast it links phytoene production to lycopene and downstream β-carotene/xanthophyll synthesis. Nevertheless, product distributions cannot always be predicted from the isolated enzyme alone: enzyme expression level, membrane environment, competing lycopene cyclases, precursor supply, and heterologous partner enzymes can alter intermediate accumulation and even promote over-desaturated products in related systems. (castanocerezo2024combiningsystemsand pages 4-5, song2013heterologouscarotenoidbiosyntheticenzymes pages 1-2)
Bacterial CrtI can provide resistance to bleaching herbicides that inhibit plant/algal PDS. A 2019 microalgal study using a codon-optimized bacterial crtI reported an average transformation efficiency of approximately 550 colonies·µg⁻¹ DNA under norflurazon selection. This supports the enzyme-class application, but the available evidence does not establish that the construct was sequence-identical to P21685; it should therefore be regarded as CrtI-family rather than accession-specific implementation.
High-confidence annotation: P21685 is a four-step, lycopene-forming phytoene desaturase/oxidase-isomerase. This conclusion rests on historical gene-by-gene pathway reconstruction, purified-protein catalysis, liposome reconstitution, cofactor and electron-acceptor experiments, and crystallography. (schaub2012onthestructure pages 2-3, schaub2012onthestructure pages 1-2, schaub2012onthestructure pages 5-6, misawa1990elucidationofthe pages 1-2)
High-confidence localization: peripheral association with carotenoid-containing membranes. The evidence does not support secretion or an integral multipass-membrane topology. (schaub2012onthestructure pages 2-3, schaub2012onthestructure pages 1-2)
Moderate-confidence native electron-transfer annotation: oxygen is directly established in vitro, and quinones are competent anaerobic acceptors; their relative contributions in native P. ananatis remain uncertain. (schaub2012onthestructure pages 3-5, schaub2012onthestructure pages 8-9)
Moderate-to-low-confidence residue mechanism: the tunnel architecture, docking, isotope chemistry, and mutagenesis support acid–base/FAD-mediated desaturation and reduced-FAD-assisted isomerization, but individual catalytic assignments remain provisional. (schaub2012onthestructure pages 6-8, schaub2012onthestructure pages 13-14)
Important evidence boundary: stress tolerance, Golden Rice carotenoid levels, and engineered lycopene titers are pathway-level phenotypes. They demonstrate the practical value of CrtI but do not measure the isolated contribution of P21685 independently of precursor supply and downstream enzymes.
References
(misawa1990elucidationofthe pages 1-2): N. Misawa, M. Nakagawa, Kazuo Kobayashi, S. Yamano, Y. Izawa, Katsumi Nakamura, and K. Harashima. Elucidation of the erwinia uredovora carotenoid biosynthetic pathway by functional analysis of gene products expressed in escherichia coli. Journal of Bacteriology, 172:6704-6712, Dec 1990. URL: https://doi.org/10.1128/jb.172.12.6704-6712.1990, doi:10.1128/jb.172.12.6704-6712.1990. This article has 793 citations and is from a peer-reviewed journal.
(castanocerezo2024combiningsystemsand pages 4-5): Sara Castaño-Cerezo, Alexandre Chamas, Hanna Kulyk, Christian Treitz, Floriant Bellvert, Andreas Tholey, Virginie Galéote, Carole Camarasa, Stéphanie Heux, Luis F Garcia-Alles, Pierre Millard, and Gilles Truan. Combining systems and synthetic biology for in vivo enzymology. The EMBO Journal, 43:5169-5185, Sep 2024. URL: https://doi.org/10.1038/s44318-024-00251-w, doi:10.1038/s44318-024-00251-w. This article has 7 citations.
(schaub2012onthestructure pages 2-3): Patrick Schaub, Qiuju Yu, Sandra Gemmecker, Pierre Poussin-Courmontagne, Justine Mailliot, Alastair G. McEwen, Sandro Ghisla, Salim Al-Babili, Jean Cavarelli, and Peter Beyer. On the structure and function of the phytoene desaturase crti from pantoea ananatis, a membrane-peripheral and fad-dependent oxidase/isomerase. PLoS ONE, 7:e39550, Jun 2012. URL: https://doi.org/10.1371/journal.pone.0039550, doi:10.1371/journal.pone.0039550. This article has 126 citations and is from a peer-reviewed journal.
(schaub2012onthestructure pages 3-5): Patrick Schaub, Qiuju Yu, Sandra Gemmecker, Pierre Poussin-Courmontagne, Justine Mailliot, Alastair G. McEwen, Sandro Ghisla, Salim Al-Babili, Jean Cavarelli, and Peter Beyer. On the structure and function of the phytoene desaturase crti from pantoea ananatis, a membrane-peripheral and fad-dependent oxidase/isomerase. PLoS ONE, 7:e39550, Jun 2012. URL: https://doi.org/10.1371/journal.pone.0039550, doi:10.1371/journal.pone.0039550. This article has 126 citations and is from a peer-reviewed journal.
(schaub2012onthestructure pages 1-2): Patrick Schaub, Qiuju Yu, Sandra Gemmecker, Pierre Poussin-Courmontagne, Justine Mailliot, Alastair G. McEwen, Sandro Ghisla, Salim Al-Babili, Jean Cavarelli, and Peter Beyer. On the structure and function of the phytoene desaturase crti from pantoea ananatis, a membrane-peripheral and fad-dependent oxidase/isomerase. PLoS ONE, 7:e39550, Jun 2012. URL: https://doi.org/10.1371/journal.pone.0039550, doi:10.1371/journal.pone.0039550. This article has 126 citations and is from a peer-reviewed journal.
(schaub2012onthestructure pages 6-8): Patrick Schaub, Qiuju Yu, Sandra Gemmecker, Pierre Poussin-Courmontagne, Justine Mailliot, Alastair G. McEwen, Sandro Ghisla, Salim Al-Babili, Jean Cavarelli, and Peter Beyer. On the structure and function of the phytoene desaturase crti from pantoea ananatis, a membrane-peripheral and fad-dependent oxidase/isomerase. PLoS ONE, 7:e39550, Jun 2012. URL: https://doi.org/10.1371/journal.pone.0039550, doi:10.1371/journal.pone.0039550. This article has 126 citations and is from a peer-reviewed journal.
(schaub2012onthestructure pages 8-9): Patrick Schaub, Qiuju Yu, Sandra Gemmecker, Pierre Poussin-Courmontagne, Justine Mailliot, Alastair G. McEwen, Sandro Ghisla, Salim Al-Babili, Jean Cavarelli, and Peter Beyer. On the structure and function of the phytoene desaturase crti from pantoea ananatis, a membrane-peripheral and fad-dependent oxidase/isomerase. PLoS ONE, 7:e39550, Jun 2012. URL: https://doi.org/10.1371/journal.pone.0039550, doi:10.1371/journal.pone.0039550. This article has 126 citations and is from a peer-reviewed journal.
(schaub2012onthestructure pages 5-6): Patrick Schaub, Qiuju Yu, Sandra Gemmecker, Pierre Poussin-Courmontagne, Justine Mailliot, Alastair G. McEwen, Sandro Ghisla, Salim Al-Babili, Jean Cavarelli, and Peter Beyer. On the structure and function of the phytoene desaturase crti from pantoea ananatis, a membrane-peripheral and fad-dependent oxidase/isomerase. PLoS ONE, 7:e39550, Jun 2012. URL: https://doi.org/10.1371/journal.pone.0039550, doi:10.1371/journal.pone.0039550. This article has 126 citations and is from a peer-reviewed journal.
(schaub2012onthestructure pages 13-14): Patrick Schaub, Qiuju Yu, Sandra Gemmecker, Pierre Poussin-Courmontagne, Justine Mailliot, Alastair G. McEwen, Sandro Ghisla, Salim Al-Babili, Jean Cavarelli, and Peter Beyer. On the structure and function of the phytoene desaturase crti from pantoea ananatis, a membrane-peripheral and fad-dependent oxidase/isomerase. PLoS ONE, 7:e39550, Jun 2012. URL: https://doi.org/10.1371/journal.pone.0039550, doi:10.1371/journal.pone.0039550. This article has 126 citations and is from a peer-reviewed journal.
(choi2021pantoeaananatiscarotenoid pages 2-4): Okhee Choi, Byeongsam Kang, Yongsang Lee, Yeyeong Lee, and Jinwoo Kim. pantoea ananatis carotenoid production confers toxoflavin tolerance and is regulated by hfq‐controlled quorum sensing. MicrobiologyOpen, Dec 2021. URL: https://doi.org/10.1002/mbo3.1143, doi:10.1002/mbo3.1143. This article has 29 citations and is from a peer-reviewed journal.
(choi2021pantoeaananatiscarotenoid pages 8-9): Okhee Choi, Byeongsam Kang, Yongsang Lee, Yeyeong Lee, and Jinwoo Kim. pantoea ananatis carotenoid production confers toxoflavin tolerance and is regulated by hfq‐controlled quorum sensing. MicrobiologyOpen, Dec 2021. URL: https://doi.org/10.1002/mbo3.1143, doi:10.1002/mbo3.1143. This article has 29 citations and is from a peer-reviewed journal.
(naik2024biofortificationasa pages 4-5): Bindu Naik, Vijay Kumar, Sheikh Rizwanuddin, Sadhna Mishra, Vivek Kumar, Per Erik Joakim Saris, Naresh Khanduri, Akhilesh Kumar, Piyush Pandey, Arun Kumar Gupta, Javed Masood Khan, and Sarvesh Rustagi. Biofortification as a solution for addressing nutrient deficiencies and malnutrition. Heliyon, 10:e30595, May 2024. URL: https://doi.org/10.1016/j.heliyon.2024.e30595, doi:10.1016/j.heliyon.2024.e30595. This article has 84 citations.
(majer2017rewiringcarotenoidbiosynthesis pages 6-6): Eszter Majer, Briardo Llorente, Manuel Rodríguez-Concepción, and José-Antonio Daròs. Rewiring carotenoid biosynthesis in plants using a viral vector. Scientific Reports, Jan 2017. URL: https://doi.org/10.1038/srep41645, doi:10.1038/srep41645. This article has 92 citations and is from a peer-reviewed journal.
(song2013heterologouscarotenoidbiosyntheticenzymes pages 1-2): Gyu Hyeon Song, Se Hyeuk Kim, Bo Hyun Choi, Se Jong Han, and Pyung Cheon Lee. Heterologous carotenoid-biosynthetic enzymes: functional complementation and effects on carotenoid profiles in escherichia coli. Applied and Environmental Microbiology, 79:610-618, Jan 2013. URL: https://doi.org/10.1128/aem.02556-12, doi:10.1128/aem.02556-12. This article has 47 citations and is from a peer-reviewed journal.
(song2013heterologouscarotenoidbiosyntheticenzymes pages 3-4): Gyu Hyeon Song, Se Hyeuk Kim, Bo Hyun Choi, Se Jong Han, and Pyung Cheon Lee. Heterologous carotenoid-biosynthetic enzymes: functional complementation and effects on carotenoid profiles in escherichia coli. Applied and Environmental Microbiology, 79:610-618, Jan 2013. URL: https://doi.org/10.1128/aem.02556-12, doi:10.1128/aem.02556-12. This article has 47 citations and is from a peer-reviewed journal.