Evidence map›Paper›PMID 37498333›Full record

ArticleApplied microbiology and biotechnology2023

Functions and substrate selectivity of diacylglycerol acyltransferases from Mortierella alpina.

Jun Li, Haiqin Chen, Lulu Chang, Chen Wu, Hao Zhang, Yong Q Chen, Wei Chen

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In one paragraph

Article in Applied microbiology and biotechnology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.3field-weighted citation impact, top 22% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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3 · Its place in the literature

Who cites it

5 citing papers in PubMed, 7 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 1 institution in 2 countries.

Jun LiState Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu, 214122, People's Republic of China.
Haiqin ChenState Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu, 214122, People's Republic of China. haiqinchen@jiangnan.edu.cn.ORCID http://orcid.org/0000-0002-2359-2622
Lulu ChangState Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu, 214122, People's Republic of China.
Chen WuState Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu, 214122, People's Republic of China.
Hao ZhangState Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu, 214122, People's Republic of China.
Yong Q ChenState Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu, 214122, People's Republic of China.
Wei ChenState Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu, 214122, People's Republic of China.
Jiangnan University · CN

Funding

National Key Research and Development Program of China 2021YFC2100700National Natural Science Foundation of China 31722041
6 · The paper itself

Abstract

Mortierella alpina produces various polyunsaturated fatty acids in the form of triacylglycerols (TAG). Diacylglycerol acyltransferase (DGAT) catalyzes the binding of acyl-CoA to diacylglycerol to form TAG and is the key enzyme involved in TAG synthesis. A variety of DGATs are present in M. alpina; however, comparative analysis of the functional properties and substrate selectivity of these DGATs is insufficient. In this study, DGAT1 (MaDGAT1A/1B/1C) and DGAT2 (MaDGAT2A/2B) isoforms from M. alpina were analyzed and heterologously expressed in S. cerevisiae H1246. The results showed that MaDGAT1A/1B/2A/2B were able to restore TAG synthesis, and the corresponding TAG content in recombinant yeasts was 2.92 ± 0.42%, 3.62 ± 0.22%, 0.86 ± 0.34%, and 0.18 ± 0.09%, respectively. In S. cerevisiae H1246, MaDGAT1A preferred C16:1 among monounsaturated fatty acids, MaDGAT1B preferred C16:0 among saturated fatty acids (SFAs), and MaDGAT2A/2B preferred C18:0 among SFAs. Under exogenous addition of polyunsaturated fatty acids (PUFAs), MaDGAT1A and 2A preferentially assembled linoleic acid into TAG, and MaDGAT2B had substrate selectivity for eicosapentaenoic and linoleic acids in ω-6 PUFAs. In vitro, MaDGAT1A showed no obvious acyl-CoA selectivity and MaDGAT1B preferred C20:5-CoA. MaDGAT1A/1B preferred C18:1/C18:1-DAG compared with C20:4/C20:4-DAG. This study indicates that MaDGATs have the potential to be used in the production of LA/EPA-rich TAG and provide a reference for improving the production of TAGs in oleaginous fungi. KEY POINTS: • MaDGAT1A preferred C16:1 among MUFAs, MaDGAT1B and MaDGAT2A/2B preferred C16:0 and C18:0 among SFAs, respectively • MaDGAT1A/2A preferentially assembled linoleic acid into TAG, and MaDGAT2B has substrate selectivity for eicosapentaenoic acid and linoleic acid in ω-6 PUFAs • MaDGAT1A showed no obvious acyl-CoA selectivity, and MaDGAT1B preferred C20:5-CoA. MaDGAT1A/1B preferred to select C18:1/C18:1-DAG compared with C20:4/C20:4-DAG.

Indexed as

Diacylglycerol O-AcyltransferaseSaccharomyces cerevisiaeAcyltransferasesDiglyceridesFatty AcidsFatty Acids, UnsaturatedLinoleic AcidMortierellaTriglyceridesAcyltransferasesDiacylglycerol O-AcyltransferaseDiglyceridesFatty AcidsFatty Acids, UnsaturatedLinoleic AcidTriglyceridesDiacylglycerol acyltransferaseMortierella alpinaPolyunsaturated fatty acidsSubstrate selectivityTriacylglycerol

Identifiers

PMID37498333
OpenAlexW4385294695

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.