Evidence map›Paper›PMID 26555263›Full record

ArticleThe Journal of biological chemistry2016

The Structural and Functional Characterization of Mammalian ADP-dependent Glucokinase.

Jan P Richter, Alexander K Goroncy, Ron S Ronimus, Andrew J Sutherland-Smith

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

17 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
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  5. Sugar-sensing swodkoreceptors and swodkocrine signaling.Animal models and experimental medicine · 2025
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  6. Review
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  9. Inborn errors of metabolite repair.Journal of inherited metabolic disease · 2020
    Review
  10. Article
  11. Article
  12. Failure to eliminate a phosphorylated glucose analog leads to neutropenia in patients with G6PT and G6PC3 deficiency.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  13. Article
  14. Article
  15. Article
  16. ADP-Dependent Kinases From the Archaeal OrderFrontiers in microbiology · 2018
    Article
  17. 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

4 authors at 2 institutions in 1 country.

Jan P RichterFrom the Institute of Fundamental Sciences, Massey University, Palmerston North 4410, New Zealand and.
Alexander K GoroncyFrom the Institute of Fundamental Sciences, Massey University, Palmerston North 4410, New Zealand and.
Ron S RonimusAgResearch Limited, Palmerston North 4442, New Zealand ron.ronimus@agresearch.co.nz.
Andrew J Sutherland-SmithFrom the Institute of Fundamental Sciences, Massey University, Palmerston North 4410, New Zealand and A.J.Sutherland-Smith@massey.ac.nz.
Massey University · NZAgResearch · NZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The enzyme-catalyzed phosphorylation of glucose to glucose-6-phosphate is a reaction central to the metabolism of all life. ADP-dependent glucokinase (ADPGK) catalyzes glucose-6-phosphate production, utilizing ADP as a phosphoryl donor in contrast to the more well characterized ATP-requiring hexokinases. ADPGK is found in Archaea and metazoa; in Archaea, ADPGK participates in a glycolytic role, but a function in most eukaryotic cell types remains unknown. We have determined structures of the eukaryotic ADPGK revealing a ribokinase-like tertiary fold similar to archaeal orthologues but with significant differences in some secondary structural elements. Both the unliganded and the AMP-bound ADPGK structures are in the "open" conformation. The structures reveal the presence of a disulfide bond between conserved cysteines that is positioned at the nucleotide-binding loop of eukaryotic ADPGK. The AMP-bound ADPGK structure defines the nucleotide-binding site with one of the disulfide bond cysteines coordinating the AMP with its main chain atoms, a nucleotide-binding motif that appears unique to eukaryotic ADPGKs. Key amino acids at the active site are structurally conserved between mammalian and archaeal ADPGK, and site-directed mutagenesis has confirmed residues essential for enzymatic activity. ADPGK is substrate inhibited by high glucose concentration and shows high specificity for glucose, with no activity for other sugars, as determined by NMR spectroscopy, including 2-deoxyglucose, the glucose analogue used for tumor detection by positron emission tomography.

Indexed as

Protein FoldingAmino Acid MotifsAnimalsGlucokinaseGlucoseHumansMiceNuclear Magnetic Resonance, BiomolecularProtein Structure, TertiaryStructure-Activity RelationshipADP-dependent glucokinaseGlucokinaseGlucoseADPADP-dependent glucokinaseAMPenzyme structureglucokinaseglucose-6-phosphateglucose metabolismNMR spectroscopyribokinasex-ray crystallography

Identifiers

PMID26555263
PMCPMC4759153
OpenAlexW2111565594

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.