Evidence map›Paper›PMID 24618038›Full record

ArticleThe FEBS journal2014

The substrate specificity, enantioselectivity and structure of the (R)-selective amine : pyruvate transaminase from Nectria haematococca.

Christopher Sayer, Ruben J Martinez-Torres, Nina Richter, Michail N Isupov, Helen C Hailes, Jennifer A Littlechild, John M Ward

Open access · hybridAbstract read
In one paragraph

Article in The FEBS journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.8field-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

16 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Transaminases for industrial biocatalysis: novel enzyme discovery.Applied microbiology and biotechnology · 2020
    Review
  9. An (Frontiers in bioengineering and biotechnology · 2020
    Article
  10. Article
  11. Article
  12. Thermostable Branched-Chain Amino Acid Transaminases From the ArchaeaFrontiers in bioengineering and biotechnology · 2019
    Article
  13. Article
  14. Article
  15. The Industrial Age of Biocatalytic Transamination.European journal of organic chemistry · 2015
    Article
  16. 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

7 authors at 2 institutions in 1 country.

Christopher SayerHenry Wellcome Building for Biocatalysis, College of Life and Environmental Sciences, University of Exeter, EX4 4QD, UK.
Ruben J Martinez-Torres
Nina Richter
Michail N Isupov
Helen C Hailes
Jennifer A Littlechild
John M Ward
University College London · GBUniversity of Exeter · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L002035/1Wellcome Trust
6 · The paper itself

Abstract

unlabelledDuring the last decade the use of transaminases for the production of pharmaceutical and fine chemical intermediates has attracted a great deal of attention. Transaminases are versatile biocatalysts for the efficient production of amine intermediates and many have (S)-enantiospecificity. Transaminases with (R)-specificity are needed to expand the applications of these enzymes in biocatalysis. In this work we have identified a fungal putative (R)-specific transaminase from the Eurotiomycetes Nectria haematococca, cloned a synthetic version of this gene, demonstrated (R)-selective deamination of several substrates including (R)-α-methylbenzylamine, as well as production of (R)-amines, and determined its crystal structure. The crystal structures of the holoenzyme and the complex with an inhibitor gabaculine offer the first detailed insight into the structural basis for substrate specificity and enantioselectivity of the industrially important class of (R)-selective amine : pyruvate transaminases. DATABASE: The atomic coordinates and structure factors for the Nectria TAm in holoenzyme and gabaculine-bound forms have been deposited in the PDB as entries 4cmd and 4cmf respectively.

Indexed as

Amino Acid SequenceBiocatalysisCloning, MolecularGenes, FungalModels, MolecularMolecular Sequence DataNectriaProtein ConformationStereoisomerismSubstrate SpecificityTransaminasesTransaminasesaminotransferaseindustrial biocatalysisprotein structure(R)-selectivesubstrate specificitytransaminase

Identifiers

PMID24618038
PMCPMC4255305
OpenAlexW2112047015

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.