Evidence map›Paper›PMID 24121043›Full record

ReviewArchives of biochemistry and biophysics2014

Aspartate aminotransferase: an old dog teaches new tricks.

Michael D Toney

Abstract readReview
In one paragraph

Review in Archives of biochemistry and biophysics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

62 citing papers in PubMed, 136 citations in OpenAlex.

  1. Article
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  8. Review
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  15. Multisubstrate specificity shaped the complex evolution of the aminotransferase family across the tree of life.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. The role of GOT1 in cancer metabolism.Frontiers in oncology · 2024
    Review
  20. Article

2 more citing papers are in PubMed but not listed here.

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

1 author at 1 institution in 1 country.

Michael D ToneyDepartment of Chemistry, University of California, Davis, Davis, CA 95616, USA. Electronic address: mdtoney@ucdavis.edu.
University of California, Davis · US

Funding

REACTION SPECIFICITY OF PYRIDOXAL PHOSPHATE ENZYMESR01GM054779 · NIGMS · YESHIVA UNIVERSITY · PI TONEY, MICHAEL · 1997 to 2011
$2.9M
Reaction Specificity of Pyridoxal Phosphate EnzymesR56GM054779 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI TONEY, MICHAEL · 2007 to 2007
$306k
NIGMS NIH HHS GM54779NIGMS NIH HHS R01 GM054779NIGMS NIH HHS R56 GM054779
6 · The paper itself

Abstract

Aspartate aminotransferase (AAT) is a prototypical pyridoxal 5'-phosphate (PLP) dependent enzyme that catalyzes the reversible interconversion of l-aspartate and α-ketoglutarate with oxalacetate and l-glutamate via a ping-pong catalytic cycle in which the pyridoxamine 5'-phosphate enzyme form is an intermediate. There is a bountiful literature on AAT that spans approximately 60years, and much fundamental mechanistic information on PLP dependent reactions has been gained from its study. Here, we review our recent work on AAT, where we again used it as a test bed for fundamental concepts in PLP chemistry. First, we discuss the role that coenzyme protonation state plays in controlling reaction specificity, then ground state destabilization via hyperconjugation in the external aldimine intermediate is examined. The third topic is light enhancement of catalysis of Cα-H deprotonation by PLP in solution and in AAT, which occurs through a triplet state of the external aldimine intermediate. Lastly, we consider recent advances in our analyses of enzyme multiple sequence alignments for the purpose of predicting mutations that are required to interconvert structurally similar but catalytically distinct enzymes, and the application of our program JANUS to the conversion of AAT into tyrosine aminotransferase.

Indexed as

AnimalsAspartate AminotransferasesComputational BiologyEnzyme ActivationHumansModels, MolecularNitrogenPyridoxal PhosphateAspartate AminotransferasesNitrogenPyridoxal PhosphateAsparate aminotransferaseBinding isotope effectBioinformaticsCoenzyme analogueLight activationNitrogen metabolismPyridoxal phosphateVitamin B6

Identifiers

PMID24121043
PMCPMC3946379
OpenAlexW2167385968

What OpenQuestion holds

Textmetadata
LicenceTDM
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.