Evidence map›Paper›PMID 37453025›Full record

ReviewApplied biochemistry and biotechnology2024

Arylacetonitrilases: Potential Biocatalysts for Green Chemistry.

Tek Chand Bhalla, Neerja Thakur, Vijay Kumar

Abstract readReview
PubMed Publisher
In one paragraph

Review in Applied biochemistry and biotechnology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Review
  2. Article
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.

Tek Chand BhallaDepartment of Biotechnology, Himachal Pradesh University, Himachal Pradesh, Gyan-Path, Shimla, 171005, India. bhallatc@rediffmail.com.
Neerja ThakurDepartment of Biotechnology, Himachal Pradesh University, Himachal Pradesh, Gyan-Path, Shimla, 171005, India.
Vijay KumarDepartment of Biotechnology, Himachal Pradesh University, Himachal Pradesh, Gyan-Path, Shimla, 171005, India.

Funding

Basic Scientific Research, UGC-New Delhi (IN) UGC-BSR Faculty Fellowship award number F.No. 18-1/2011(BSR)/24 February 2014
6 · The paper itself

Abstract

Nitrilases are the enzymes that catalyze the hydrolysis of nitriles to corresponding carboxylic acid and ammonia. They are broadly categorized into aromatic, aliphatic, and arylacetonitrilases based on their substrate specificity. Most of the studies pertaining to these enzymes in the literature have focused on aromatic and aliphatic nitrilases. However, arylacetonitrilases have attracted the attention of academia and industry in the last several years due to their aryl specificity and enantioselectivity. They have emerged as interesting biocatalytic tools in green chemistry to synthesize useful aryl acids such as mandelic acid and derivatives of phenylacetic acid. The aim of the present review is to collate information on the arylacetonitrilases and their catalytic properties including enantioselectivity and potential applications in organic synthesis.

Indexed as

AminohydrolasesBiocatalysisGreen Chemistry TechnologyMandelic AcidsNitrilesStereoisomerismSubstrate SpecificityAminohydrolasesmandelic acidMandelic AcidsnitrilaseNitrilesArylacetic acidsArylacetonitrilaseBiocatalystEnantioselectivityNitrilase

Identifiers

What OpenQuestion holds

Textmetadata
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.