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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 literature evidence reviewed here matches the UniProt target Q9SLD2 from Arabidopsis thaliana, whose gene is DGAT1 (locus At2g19450) and which is also known as TAG1 (triacylglycerol 1). Lu et al. experimentally investigated At2g19450/DGAT1 promoter activity and enzyme activity in Arabidopsis, confirming that this locus encodes diacylglycerol acyltransferase-1 involved in TAG biosynthesis (https://doi.org/10.1023/a:1023935605864; published May 2003) (lu2003expressionpatternof pages 1-3, lu2003expressionpatternof pages 3-4).
DGAT1 (acyl-CoA:diacylglycerol acyltransferase 1) catalyzes the terminal/committed step of the acyl-CoA–dependent (Kennedy) pathway of triacylglycerol (TAG) assembly: transfer of an acyl group from acyl-CoA to diacylglycerol (DAG) (sn-3 position) to form TAG. This role is described directly in Arabidopsis-focused primary literature and is reiterated in reviews of plant TAG biosynthesis (lu2003expressionpatternof pages 1-3, aulakh2018transcriptomicandlipidomic pages 41-45, zhou2024regulationofoil pages 5-7).
Lu et al. provide direct biochemical assay evidence: Arabidopsis microsomal membranes catalyzed incorporation of [14C]oleoyl-CoA into TAG using 1,2-dioleoylglycerol as acyl acceptor (reaction mixture included 200 µM 1,2-dioleoylglycerol and 22.8 µM [14C]oleoyl-CoA), demonstrating the canonical DGAT reaction with defined substrates (https://doi.org/10.1023/a:1023935605864; 2003) (lu2003expressionpatternof pages 3-4).
A consistent theme in Arabidopsis and broader plant literature is that DGAT1 provides a major acyl-CoA–dependent route to TAG, while phospholipid:diacylglycerol acyltransferase (PDAT1) can provide an acyl-CoA–independent route (using phospholipids as acyl donors). Genetic evidence (summarized in a lipidomics/transcriptomics synthesis) indicates functional overlap between DGAT1 and PDAT1; severe TAG depletion and reproductive defects can arise when both routes are impaired (aulakh2018transcriptomicandlipidomic pages 104-109, behera2023acylcoadependentandacylcoaindependent pages 2-3).
DGAT1 catalytic activity is measured in microsomal membrane fractions (Lu et al., 2003), indicating that the enzyme acts in a membrane context (ER-derived microsomes in typical plant preparations) rather than as a soluble cytosolic enzyme (lu2003expressionpatternof pages 3-4, lu2003expressionpatternof pages 7-8). Review synthesis further describes plant DGAT1 as an integral ER membrane enzyme (xu2018propertiesandbiotechnological pages 11-13).
Plant DGAT1 is widely described as a ~500 aa multi-pass membrane protein (commonly ~8–10 transmembrane segments) in the MBOAT (membrane-bound O-acyltransferase) family, with a relatively large N-terminal region that can contribute to regulatory functions (e.g., acyl-CoA/CoA binding, oligomerization). These structural features are summarized in an authoritative Lipids review (Xu et al., 2018; https://doi.org/10.1002/lipd.12081; published July 2018) (xu2018propertiesandbiotechnological pages 11-13, xu2018propertiesandbiotechnological pages 33-36).
Lu et al. (2003) used promoter::GUS and immunoblotting to show DGAT1 expression is prominent in developing seeds/embryos and pollen, consistent with major TAG accumulation in these tissues (https://doi.org/10.1023/a:1023935605864; 2003) (lu2003expressionpatternof pages 1-3, lu2003expressionpatternof pages 3-4). DGAT1 protein during embryo development was detectable by ~5 days after anthesis, peaked around 7–9 days after anthesis, and remained detectable at later stages (lu2003expressionpatternof pages 7-8).
In seedlings, DGAT1 promoter activity is detected in regions associated with rapid growth (shoot/root apical regions), and DGAT1 transcript abundance is responsive to sugar availability; 2% glucose induced DGAT1 expression by ~4-fold in 2-day-old seedlings (lu2003expressionpatternof pages 1-3, lu2003expressionpatternof pages 7-8).
In Arabidopsis, tag1/dgat1 mutants show an extreme reduction in measurable microsomal DGAT activity. Lu et al. report microsomal DGAT activity (nmol·mg−1·min−1) of roughly ~116–201 (Col WT; two experiments) and ~138–260 (Ws WT), compared with ~2–8 in tag1 mutant alleles, consistent with DGAT1 being the major microsomal DGAT activity in their assay conditions (https://doi.org/10.1023/a:1023935605864; 2003) (lu2003expressionpatternof pages 7-8).
Consistently, when labeling 2-day seedlings with [14C]acetate, wild type incorporated ~5–7% of label into TAG, while tag1 mutants incorporated ~2–3%, implying DGAT1 contributes about half of detectable TAG synthesis in that seedling labeling context (lu2003expressionpatternof pages 7-8).
A synthesis of Arabidopsis DGAT1 mutant phenotypes reports that dgat1-1 retains about ~75% of wild-type total seed oil and dgat1-2 retains about ~55% (i.e., ~25% and ~45% reductions). The same source summarizes fatty-acid composition changes including strong decreases in 18:1 and 20:1 and increases in 18:3 (aulakh2018transcriptomicandlipidomic pages 41-45).
Lipidomics-focused summaries also report developing dgat1-1 seeds with ~35% reduced neutral lipid content and that, in genetic backgrounds where PDAT1 compensation is diminished (PDAT1 knockdown in dgat1), seed TAG can fall by ~70–80%, highlighting that DGAT1 and PDAT1 together define much of terminal TAG-assembly capacity (aulakh2018transcriptomicandlipidomic pages 104-109).
A 2023 review in Plant Biotechnology Journal emphasizes that plant lipid biosynthesis is increasingly understood through the lens of protein interactomes and cooperative ER assemblies, rather than isolated enzymes. This review discusses DGAT (including Arabidopsis DGAT1) as an ER-localized acyltransferase for DAG→TAG and reports AlphaFold2-based structural predictions suggesting an interaction between Arabidopsis LPCAT (lysophosphatidylcholine acyltransferase) and DGAT1, consistent with a model where acyl groups are channeled from phosphatidylcholine remodeling toward TAG assembly (https://doi.org/10.1111/pbi.14027; published March 2023) (xu2023proteininteractomesfor pages 4-6).
A 2024 review in Genes describes DGAT1 as a key, often broadly acting enzyme in plant seed oil synthesis and provides a concrete Arabidopsis engineering example: AtDGAT1 overexpression increased DGAT activity by ~10–70% relative to wild type and increased thousand-seed weight and seed oil content (https://doi.org/10.3390/genes15091125; published Aug 2024) (zhou2024regulationofoil pages 7-9, zhou2024regulationofoil pages 5-7). This supports DGAT1 as a current “lever” in oilseed trait improvement.
DGAT1 is widely treated as a high-value engineering target to increase TAG accumulation in seeds (and sometimes vegetative tissues) because it catalyzes the last committed step in the acyl-CoA–dependent TAG pathway (zhou2024regulationofoil pages 5-7). The 2024 review’s reported 10–70% DGAT activity increase and associated improvements in seed mass/oil content exemplify real-world strategy: increase terminal TAG assembly capacity to boost oil traits (zhou2024regulationofoil pages 7-9).
However, Arabidopsis genetic-interaction evidence indicates engineering should account for network redundancy and compensation. PDAT1 can partially compensate for DGAT1 loss, and reducing both activities can cause very large TAG decreases (reported 70–80% TAG reduction when PDAT1 is knocked down in a dgat1 background), as well as reproductive defects such as pollen oil body disruption and sterile pollen in combined-impairment contexts (aulakh2018transcriptomicandlipidomic pages 104-109, behera2023acylcoadependentandacylcoaindependent pages 2-3).
Although not specific to Arabidopsis DGAT1, 2023 primary work on avocado DGAT1 illustrates a modern implementation pattern: expressing DGAT1 orthologs in heterologous systems (yeast, Nicotiana leaves) to increase lipid accumulation and steer fatty-acid composition. Avocado mesocarp naturally accumulates ~70% TAG (dry weight) and PaDGAT1 showed preference for oleic acid over palmitic acid in vitro, consistent with efforts to tailor oil composition by choosing DGAT variants with desired acyl preferences (https://doi.org/10.3389/fpls.2022.1056582; published Jan 2023) (behera2023acylcoadependentandacylcoaindependent pages 1-2).
Authoritative synthesis (Xu et al., 2018, Lipids) frames DGAT1 as a major determinant of carbon flux into seed TAG, typically ER-associated and membrane embedded, explaining why DGAT1 is repeatedly targeted in engineering approaches (https://doi.org/10.1002/lipd.12081; July 2018) (xu2018propertiesandbiotechnological pages 8-11, xu2018propertiesandbiotechnological pages 11-13).
The 2023 interactome review highlights a current research direction: to improve oil traits, it may be insufficient to increase DGAT1 abundance alone; instead, engineering might leverage enzyme assemblies and substrate channeling at the ER (e.g., involving LPCAT–DGAT1 coupling) to more efficiently route acyl flux into TAG (https://doi.org/10.1111/pbi.14027; March 2023) (xu2023proteininteractomesfor pages 4-6).
| Study (first author, year) | Publication (journal) and URL/DOI | What was shown | Key quantitative results | Notes on relevance to functional annotation |
|---|---|---|---|---|
| Lu, 2003 | Plant Molecular Biology; https://doi.org/10.1023/A:1023935605864 | Verified Arabidopsis DGAT1 corresponds to At2g19450/TAG1 and catalyzes the final acylation step in TAG biosynthesis; microsomal assay used 1,2-dioleoylglycerol + [14C]oleoyl-CoA; promoter::GUS and immunoblotting showed expression in developing seeds, pollen, germinating seeds/seedlings, and apical regions. (lu2003expressionpatternof pages 1-3, lu2003expressionpatternof pages 3-4) | In vitro assay used 200 µM 1,2-dioleoylglycerol and 22.8 µM [14C]oleoyl-CoA with 10 µg microsomal protein; DGAT1 protein detected by 5 days after anthesis, peaked at 7–9 DAA, still detectable at 23 DAA. (lu2003expressionpatternof pages 3-4, lu2003expressionpatternof pages 7-8) | Strong primary evidence for core function, biochemical substrates, and tissue/developmental expression of Q9SLD2/AtDGAT1. |
| Lu, 2003 | Plant Molecular Biology; https://doi.org/10.1023/A:1023935605864 | Demonstrated DGAT1 activity is largely microsomal and that tag1 mutants lose most detectable DGAT activity; also linked DGAT1 to seedling TAG synthesis and glucose-responsive expression. (lu2003expressionpatternof pages 7-8) | Microsomal DGAT activity (nmol·mg−1·min−1): Col WT 201 ± 1 and 116 ± 18; Ws WT 260 ± 29 and 138 ± 11; tag1-1 2 ± 3 and 7 ± 4; tag1-2 4 ± 1 and 8 ± 2. [14C]acetate labeling into TAG: WT ~5–7% vs tag1 ~2–3%. DGAT1 transcript upregulated ~4-fold by 2% glucose in 2-day seedlings. (lu2003expressionpatternof pages 7-8) | Provides quantitative loss-of-function evidence that DGAT1 is the major Arabidopsis microsomal DGAT in seedlings and is responsive to carbon status. |
| Aulakh, 2018 (summarizing prior Arabidopsis studies) | Unknown journal/book chapter; no DOI in snippet | Summarized that AtDGAT1 transfers an acyl group from acyl-CoA to the sn-3 position of DAG to form TAG; described AtDGAT1 as ~500 aa with ~10 predicted TM domains and ER-associated activity in developing seeds; transcripts present in siliques, stem, leaves, flowers, germinating seeds, and seedlings. (aulakh2018transcriptomicandlipidomic pages 41-45) | Overexpression in yeast increased microsomal DGAT activity 3.5–4-fold; dgat1-1 showed 40–70% lower DGAT activity during seed development; mature seed oil retained: dgat1-1 ~75% of WT, dgat1-2 ~55% of WT. (aulakh2018transcriptomicandlipidomic pages 41-45) | Useful secondary synthesis aligning UniProt family/domain assignment with plant MBOAT topology and ER localization. |
| Aulakh, 2018 (summarizing prior Arabidopsis studies) | Unknown journal/book chapter; no DOI in snippet | Reported mutant lipid phenotypes and pathway compensation with PDAT1; emphasized that TAG1 is a DGAT1 mutant affecting TAG synthesis in seeds and pollen. (aulakh2018transcriptomicandlipidomic pages 104-109, aulakh2018transcriptomicandlipidomic pages 100-104) | dgat1-1: 25–45% seed oil reduction; developing seeds had 35% lower neutral lipid; ~60% decreases in 18:1 and 20:1 and ~100% increase in 18:3 in mature seed; PDAT1 knockdown in dgat1 background caused 70–80% oil reduction; dgat1-1 pdat1 disrupted pollen oil body formation and caused sterile pollen. (aulakh2018transcriptomicandlipidomic pages 104-109, aulakh2018transcriptomicandlipidomic pages 41-45) | Important for pathway annotation: DGAT1 is primary but not sole TAG-synthesis route; overlaps functionally with PDAT1 and is required for normal pollen/seed development when compensation is removed. |
| Xu, 2018 | Lipids; https://doi.org/10.1002/lipd.12081 | Review described DGAT1 as a membrane-bound acyl-CoA:diacylglycerol acyltransferase in the acyl-CoA-dependent TAG pathway, generally ER-localized and a major determinant of carbon flux into seed TAG. (xu2018propertiesandbiotechnological pages 8-11) | No Arabidopsis-specific kinetic numbers in snippet; reports qualitative evidence that AS11/DGAT1 inactivation dramatically decreases seed oil and that enhanced DGAT1 expression improves freezing tolerance. (xu2018propertiesandbiotechnological pages 8-11, xu2018propertiesandbiotechnological pages 11-13) | Authoritative review supporting current understanding of DGAT1 as a central, often rate-limiting TAG assembly enzyme in plants. |
| Xu, 2018 | Lipids; https://doi.org/10.1002/lipd.12081 | Summarized structural/topological features of plant DGAT1: integral ER membrane enzyme with large hydrophilic N-terminus, ~8–10 TM helices, MBOAT-family catalytic residues, N-terminal acyl-CoA/CoA-binding and oligomerization features, and an ER retrieval motif. (xu2018propertiesandbiotechnological pages 11-13, xu2018propertiesandbiotechnological pages 33-36) | Protein size ~500 aa; topology ~8–10 TMs. (xu2018propertiesandbiotechnological pages 11-13, xu2018propertiesandbiotechnological pages 33-36) | Highly relevant to subcellular localization and mechanism; supports UniProt domain/family assignment for Q9SLD2. |
| Xu, 2018 | Lipids; https://doi.org/10.1002/lipd.12081 | Cited transcriptional regulation leads for DGAT1, including MYB96 activation and ABI4/ABI5 synergistic regulation under stress; also highlighted molecular studies on membrane interactions and substrate binding. (xu2018propertiesandbiotechnological pages 43-45) | No quantitative Arabidopsis values in snippet. (xu2018propertiesandbiotechnological pages 43-45) | Useful for functional annotation of regulatory context, though details should be treated as review-level leads unless checked in primary papers. |
| Xu, 2023 | Plant Biotechnology Journal; https://doi.org/10.1111/pbi.14027 | Positioned DGAT1 within an ER transferase interactome for TAG assembly; AlphaFold2 and prior interaction evidence suggested Arabidopsis LPCAT–DGAT1 interaction and acyl channeling from PC to TAG. (xu2023proteininteractomesfor pages 4-6) | No quantitative effect sizes in snippet. (xu2023proteininteractomesfor pages 4-6) | Relevant to modern understanding that DGAT1 may function within multiprotein ER assemblies rather than as an isolated enzyme. |
| Zhou, 2024 | Genes; https://doi.org/10.3390/genes15091125 | Recent review reaffirmed DGAT1/2/3 catalyze DAG-to-TAG conversion using acyl-CoA and emphasized DGAT1 as broadly important in plant TAG metabolism; highlighted AtDGAT1 overexpression as an engineering strategy. (zhou2024regulationofoil pages 7-9, zhou2024regulationofoil pages 5-7) | AtDGAT1 overexpression increased DGAT activity by 10–70% over WT and increased thousand-seed weight and seed oil content. (zhou2024regulationofoil pages 7-9, zhou2024regulationofoil pages 5-7) | Useful 2024 synthesis connecting Arabidopsis DGAT1 function to current crop-oil engineering strategies. |
| Behera, 2023 | Frontiers in Plant Science; https://doi.org/10.3389/fpls.2022.1056582 | Although focused on avocado DGAT1, this 2023 study/review context reinforced that Arabidopsis DGAT1 loss causes modest total seed-oil reduction but strong fatty-acid composition shifts, and that DGAT1 and PDAT1 are partially redundant in seed TAG synthesis. (behera2023acylcoadependentandacylcoaindependent pages 2-3, behera2023acylcoadependentandacylcoaindependent pages 1-2) | Seed-specific PDAT1 RNAi in a dgat1 background caused 70–80% TAG reduction; avocado mesocarp example accumulated ~70% TAG dry weight and PaDGAT1 preferred oleic acid over palmitate. (behera2023acylcoadependentandacylcoaindependent pages 2-3, behera2023acylcoadependentandacylcoaindependent pages 1-2) | Relevant comparative evidence for substrate preference concepts and for understanding DGAT1/PDAT1 functional redundancy in plants. |
Table: This table compiles evidence-based findings for Arabidopsis thaliana DGAT1/At2g19450/TAG1 from primary and review sources cited in the conversation. It is useful for functional annotation because it links reaction chemistry, localization, expression, mutant phenotypes, regulation, and engineering relevance to specific evidence snippets.
References
(lu2003expressionpatternof pages 1-3): Chaofu Lu, Shen Bayon de Noyer, D. Hobbs, Jinling Kang, Y. Wen, D. Krachtus, and M. Hills. Expression pattern of diacylglycerol acyltransferase-1, an enzyme involved in triacylglycerol biosynthesis, in arabidopsis thaliana. Plant Molecular Biology, 52:31-41, May 2003. URL: https://doi.org/10.1023/a:1023935605864, doi:10.1023/a:1023935605864. This article has 96 citations and is from a peer-reviewed journal.
(lu2003expressionpatternof pages 3-4): Chaofu Lu, Shen Bayon de Noyer, D. Hobbs, Jinling Kang, Y. Wen, D. Krachtus, and M. Hills. Expression pattern of diacylglycerol acyltransferase-1, an enzyme involved in triacylglycerol biosynthesis, in arabidopsis thaliana. Plant Molecular Biology, 52:31-41, May 2003. URL: https://doi.org/10.1023/a:1023935605864, doi:10.1023/a:1023935605864. This article has 96 citations and is from a peer-reviewed journal.
(aulakh2018transcriptomicandlipidomic pages 41-45): KS Aulakh. Transcriptomic and lipidomic profiling in developing seeds of two brassicaceae species to identify key regulators associated with storage oil synthesis. Unknown journal, 2018.
(zhou2024regulationofoil pages 5-7): Lixia Zhou, Qiufei Wu, Yaodong Yang, Qihong Li, Rui Li, and Jianqiu Ye. Regulation of oil biosynthesis and genetic improvement in plants: advances and prospects. Genes, 15:1125, Aug 2024. URL: https://doi.org/10.3390/genes15091125, doi:10.3390/genes15091125. This article has 23 citations.
(aulakh2018transcriptomicandlipidomic pages 104-109): KS Aulakh. Transcriptomic and lipidomic profiling in developing seeds of two brassicaceae species to identify key regulators associated with storage oil synthesis. Unknown journal, 2018.
(behera2023acylcoadependentandacylcoaindependent pages 2-3): Jyoti Behera, Md Mahbubur Rahman, Jay Shockey, and Aruna Kilaru. Acyl-coa-dependent and acyl-coa-independent avocado acyltransferases positively influence oleic acid content in nonseed triacylglycerols. Frontiers in Plant Science, Jan 2023. URL: https://doi.org/10.3389/fpls.2022.1056582, doi:10.3389/fpls.2022.1056582. This article has 17 citations.
(lu2003expressionpatternof pages 7-8): Chaofu Lu, Shen Bayon de Noyer, D. Hobbs, Jinling Kang, Y. Wen, D. Krachtus, and M. Hills. Expression pattern of diacylglycerol acyltransferase-1, an enzyme involved in triacylglycerol biosynthesis, in arabidopsis thaliana. Plant Molecular Biology, 52:31-41, May 2003. URL: https://doi.org/10.1023/a:1023935605864, doi:10.1023/a:1023935605864. This article has 96 citations and is from a peer-reviewed journal.
(xu2018propertiesandbiotechnological pages 11-13): Yang Xu, Kristian Mark P. Caldo, Dipasmita Pal‐Nath, Jocelyn Ozga, M. Joanne Lemieux, Randall J. Weselake, and Guanqun Chen. Properties and biotechnological applications of acyl-coa:diacylglycerol acyltransferase and phospholipid:diacylglycerol acyltransferase from terrestrial plants and microalgae. Lipids, 53 7:663-688, Jul 2018. URL: https://doi.org/10.1002/lipd.12081, doi:10.1002/lipd.12081. This article has 120 citations and is from a domain leading peer-reviewed journal.
(xu2018propertiesandbiotechnological pages 33-36): Yang Xu, Kristian Mark P. Caldo, Dipasmita Pal‐Nath, Jocelyn Ozga, M. Joanne Lemieux, Randall J. Weselake, and Guanqun Chen. Properties and biotechnological applications of acyl-coa:diacylglycerol acyltransferase and phospholipid:diacylglycerol acyltransferase from terrestrial plants and microalgae. Lipids, 53 7:663-688, Jul 2018. URL: https://doi.org/10.1002/lipd.12081, doi:10.1002/lipd.12081. This article has 120 citations and is from a domain leading peer-reviewed journal.
(xu2023proteininteractomesfor pages 4-6): Yang Xu, Stacy D. Singer, and Guanqun Chen. Protein interactomes for plant lipid biosynthesis and their biotechnological applications. Plant Biotechnology Journal, 21:1734-1744, Mar 2023. URL: https://doi.org/10.1111/pbi.14027, doi:10.1111/pbi.14027. This article has 34 citations and is from a highest quality peer-reviewed journal.
(zhou2024regulationofoil pages 7-9): Lixia Zhou, Qiufei Wu, Yaodong Yang, Qihong Li, Rui Li, and Jianqiu Ye. Regulation of oil biosynthesis and genetic improvement in plants: advances and prospects. Genes, 15:1125, Aug 2024. URL: https://doi.org/10.3390/genes15091125, doi:10.3390/genes15091125. This article has 23 citations.
(behera2023acylcoadependentandacylcoaindependent pages 1-2): Jyoti Behera, Md Mahbubur Rahman, Jay Shockey, and Aruna Kilaru. Acyl-coa-dependent and acyl-coa-independent avocado acyltransferases positively influence oleic acid content in nonseed triacylglycerols. Frontiers in Plant Science, Jan 2023. URL: https://doi.org/10.3389/fpls.2022.1056582, doi:10.3389/fpls.2022.1056582. This article has 17 citations.
(xu2018propertiesandbiotechnological pages 8-11): Yang Xu, Kristian Mark P. Caldo, Dipasmita Pal‐Nath, Jocelyn Ozga, M. Joanne Lemieux, Randall J. Weselake, and Guanqun Chen. Properties and biotechnological applications of acyl-coa:diacylglycerol acyltransferase and phospholipid:diacylglycerol acyltransferase from terrestrial plants and microalgae. Lipids, 53 7:663-688, Jul 2018. URL: https://doi.org/10.1002/lipd.12081, doi:10.1002/lipd.12081. This article has 120 citations and is from a domain leading peer-reviewed journal.
(aulakh2018transcriptomicandlipidomic pages 100-104): KS Aulakh. Transcriptomic and lipidomic profiling in developing seeds of two brassicaceae species to identify key regulators associated with storage oil synthesis. Unknown journal, 2018.
(xu2018propertiesandbiotechnological pages 43-45): Yang Xu, Kristian Mark P. Caldo, Dipasmita Pal‐Nath, Jocelyn Ozga, M. Joanne Lemieux, Randall J. Weselake, and Guanqun Chen. Properties and biotechnological applications of acyl-coa:diacylglycerol acyltransferase and phospholipid:diacylglycerol acyltransferase from terrestrial plants and microalgae. Lipids, 53 7:663-688, Jul 2018. URL: https://doi.org/10.1002/lipd.12081, doi:10.1002/lipd.12081. This article has 120 citations and is from a domain leading peer-reviewed journal.