Developing and enhancing promiscuous activity for NAD(P)H-dependent flavin reductase via elimination of cofactor.

Amene Navaser, Hamid R Kalhor, Fatemeh Hayati

Open access · goldAbstract read

In one paragraph

Article in Heliyon, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing papers in PubMed

0.3field-weighted citation impact, top 36% 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

0 citing papers in PubMed, 2 citations in OpenAlex.

No citing paper in PubMed yet.

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

3 authors at 1 institution in 1 country.

Amene NavaserBiochemistry and Chemical Biology Research Laboratory, Chemistry Department, Sharif University of Technology, Tehran, Iran.

Hamid R KalhorBiochemistry and Chemical Biology Research Laboratory, Chemistry Department, Sharif University of Technology, Tehran, Iran.

Fatemeh HayatiBiochemistry and Chemical Biology Research Laboratory, Chemistry Department, Sharif University of Technology, Tehran, Iran.

Sharif University of Technology · IR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Promiscuous enzymes have shown their synthetic abilities in generating various organic compounds with high selectively and efficiency under mild conditions. Therefore, the design and development of conditions to raise promiscuity to the enzymes have been under the spotlight in recent years. Flavin reductase, that reduces flavins by using NADH as a cofactor, has not been studied in promiscuous reactions. In the present study, it was aimed to develop a catalytic promiscuous activity in the recombinant

Indexed as

BiocatalystEnzyme promiscuityFlavin reductaseKnoevenagel condensation-Michael addition reactionTetraketone synthesis

Identifiers

PMID37809429

DOI10.1016/j.heliyon.2023.e19315

PMCPMC10558354

OpenAlexW4386163008

What OpenQuestion holds

Textmetadata

LicenceCC BY-NC-ND

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.