Evidence map›Paper›PMID 30353294›Full record

ReviewJournal of industrial microbiology & biotechnology2018

Dynamic kinetic resolution of Vince lactam catalyzed by γ-lactamases: a mini-review.

Shaozhou Zhu, Guojun Zheng

Open access · bronzeAbstract readReview
PubMed Publisher
In one paragraph

Review in Journal of industrial microbiology & biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

6 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Synthesis of Cyclohexanones by a Tandem Photocatalyzed Annulation.Journal of the American Chemical Society · 2022
    Article
  4. Article
  5. Nanoreactor Design Based on Self-Assembling Protein Nanocages.International journal of molecular sciences · 2019
    Review
  6. 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

2 authors at 1 institution in 1 country.

Shaozhou ZhuState Key Laboratory of Chemical Resources Engineering, Beijing University of Chemical Technology, Beijing, People's Republic of China.
Guojun ZhengState Key Laboratory of Chemical Resources Engineering, Beijing University of Chemical Technology, Beijing, People's Republic of China. zhenggj@mail.buct.edu.cn.
Beijing University of Chemical Technology · CN

Funding

National Natural Science Foundation of China 21706005
6 · The paper itself

Abstract

γ-Lactamases are versatile enzymes used for enzymatic kinetic resolution of racemic Vince lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) in the industry. Optically pure enantiomers and their hydrolytic products are widely employed as key chemical intermediates for developing a wide range of carbocyclic nucleoside medicines, including US FDA-approved drugs peramivir and abacavir. Owing to the broad applications in the healthcare industry, the resolution process of Vince lactam has witnessed tremendous progress during the past decades. Some of the most important advances are the enzymatic strategies involving γ-lactamases. The strong industrial demand drives the progress in various strategies for discovering novel biocatalysts. In the past few years, several new scientific breakthroughs, including the genome-mining strategy and elucidation of several crystal structures, boosted the research on γ-lactamases. So far, several families of γ-lactamases for resolution of Vince lactam have been discovered, and their number is continuously increasing. The purpose of this mini-review is to describe the discovery strategy and classification of these intriguing enzymes and to cover our current knowledge on their potential biological functions. Moreover, structural properties are described in addition to their possible catalytic mechanisms. Additionally, recent advances in the newest approaches, such as immobilization to increase stability, and other engineering efforts are introduced.

Indexed as

AmidohydrolasesCatalysisEnzymes, ImmobilizedHydrolysisLactamsProtein ConformationProtein EngineeringStereoisomerismAmidohydrolasesEnzymes, Immobilizedgamma-lactamaseLactamsAbacavirAcetamidaseBiocatalysisCarbocyclic nucleosidesEnzymatic kinetic resolutionFormamidaseGamma lactamaseIsochorismataseSignature amidaseVince lactam

Identifiers

PMID30353294
OpenAlexW2897978916

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.