Evidence map›Paper›PMID 33837188›Full record

ArticleNature communications2021

Creating enzymes and self-sufficient cells for biosynthesis of the non-natural cofactor nicotinamide cytosine dinucleotide.

Xueying Wang, Yanbin Feng, Xiaojia Guo, Qian Wang, Siyang Ning, Qing Li, Junting Wang, Lei Wang, Zongbao K Zhao

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

20 citing papers in PubMed, 49 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

9 authors at 1 institution in 1 country.

Xueying WangLaboratory of Biotechnology, Dalian Institute of Chemical Physics, CAS, Dalian, PR China.
Yanbin FengLaboratory of Biotechnology, Dalian Institute of Chemical Physics, CAS, Dalian, PR China.ORCID 0000-0001-8910-1761
Xiaojia GuoLaboratory of Biotechnology, Dalian Institute of Chemical Physics, CAS, Dalian, PR China.
Qian WangLaboratory of Biotechnology, Dalian Institute of Chemical Physics, CAS, Dalian, PR China.
Siyang NingLaboratory of Biotechnology, Dalian Institute of Chemical Physics, CAS, Dalian, PR China.
Qing LiLaboratory of Biotechnology, Dalian Institute of Chemical Physics, CAS, Dalian, PR China.
Junting WangLaboratory of Biotechnology, Dalian Institute of Chemical Physics, CAS, Dalian, PR China.
Lei WangLaboratory of Biotechnology, Dalian Institute of Chemical Physics, CAS, Dalian, PR China.
Zongbao K ZhaoLaboratory of Biotechnology, Dalian Institute of Chemical Physics, CAS, Dalian, PR China. zhaozb@dicp.ac.cn.ORCID 0000-0003-0654-1193
Dalian Institute of Chemical Physics · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nicotinamide adenine dinucleotide (NAD) and its reduced form are indispensable cofactors in life. Diverse NAD mimics have been developed for applications in chemical and biological sciences. Nicotinamide cytosine dinucleotide (NCD) has emerged as a non-natural cofactor to mediate redox transformations, while cells are fed with chemically synthesized NCD. Here, we create NCD synthetase (NcdS) by reprograming the substrate binding pockets of nicotinic acid mononucleotide (NaMN) adenylyltransferase to favor cytidine triphosphate and nicotinamide mononucleotide over their regular substrates ATP and NaMN, respectively. Overexpression of NcdS alone in the model host Escherichia coli facilitated intracellular production of NCD, and higher NCD levels up to 5.0 mM were achieved upon further pathway regulation. Finally, the non-natural cofactor self-sufficiency was confirmed by mediating an NCD-linked metabolic circuit to convert L-malate into D-lactate. NcdS together with NCD-linked enzymes offer unique tools and opportunities for intriguing studies in chemical biology and synthetic biology.

Indexed as

Protein EngineeringCoenzymesCytidine TriphosphateEnzyme AssaysEscherichia coliEscherichia coli ProteinsHigh-Throughput Screening AssaysLactic AcidMalatesNiacinamideNicotinamide MononucleotideNicotinamide-Nucleotide AdenylyltransferaseOxidation-ReductionSubstrate SpecificitySynthetic BiologyCoenzymesCytidine TriphosphateEscherichia coli ProteinsLactic AcidMalatesmalic acidNiacinamideNicotinamide MononucleotideNicotinamide-Nucleotide Adenylyltransferasenicotinic acid mononucleotide adenylyltransferase

Identifiers

PMID33837188
PMCPMC8035330
OpenAlexW3150742668

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

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.