Evidence map›Paper›PMID 15659667›Full record

ArticleJournal of bacteriology2005

Characterization of the RokA and HexA broad-substrate-specificity hexokinases from Bacteroides fragilis and their role in hexose and N-acetylglucosamine utilization.

Christopher J Brigham, Michael H Malamy

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
0.5field-weighted citation impact, top 36% 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

21 citing papers in PubMed, 42 citations in OpenAlex.

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  18. Characterizing a model human gut microbiota composed of members of its two dominant bacterial phyla.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  19. Bacteroides: the good, the bad, and the nitty-gritty.Clinical microbiology reviews · 2007
    Review
  20. 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.

Christopher J BrighamDepartment of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111. michael.malamy@tufts.edu.
Michael H Malamy
Tufts University · US

Funding

GENETIC SYSTEMS TO STUDY VIRULENCE IN B FRAGILISR01AI019497 · NIAID · TUFTS UNIVERSITY BOSTON · PI MALAMY, MICHAEL H · 1985 to 2008
$2.6M
Genetic System to Study Virulence in BacteroidesR21AI019497 · NIAID · TUFTS UNIVERSITY BOSTON · PI MALAMY, MICHAEL H · 2003 to 2003
$390k
NIAID NIH HHS AI 19497NIAID NIH HHS R01 AI019497NIAID NIH HHS R21 AI019497
6 · The paper itself

Abstract

Bacteroides fragilis, a human gastrointestinal commensal and an opportunistic pathogen, utilizes simple and complex sugars and polysaccharides for growth in the large intestine and at sites of infection. Because B. fragilis lacks transport-linked sugar phosphorylation systems, cytoplasmic kinase(s) was expected to be required for the phosphorylation of hexoses and hexosamines. We have now identified two hexose kinases that are important for growth of B. fragilis on glucose, mannose, and other sugars. One kinase (RokA), a member of the ROK family of proteins, was found to be the sole kinase for activation of N-acetyl-D-glucosamine (NAG). The other kinase (HexA) is responsible for the majority of the glucose kinase activity in the cell, although a hexA deletion mutant strain was not defective for growth on any substrate tested. Deletion of both the rokA and hexA kinase genes resulted in inability of the cell to use glucose, mannose, NAG, and many other sugars. We purified RokA and determined its approximate molecular mass to be 36.5 kDa. The purified RokA protein was shown to phosphorylate several substrates, including glucose, NAG, and mannose, but not N-acetylmannosamine or N-acetylneuraminic acid. Phylogenetic analysis of RokA showed that it is most similar to kinases from the Cytophaga-Flavibacterium-Bacteroides group, while HexA was most similar to other bacterial hexokinases and eukaryotic hexokinases.

Indexed as

AcetylglucosamineAmino Acid SequenceBacteroides fragilisBase SequenceConsensus SequenceDNA PrimersEscherichia coliHexokinaseHexosesKineticsMolecular Sequence DataPhylogenyPlasmidsSequence Homology, Amino AcidSubstrate SpecificityAcetylglucosamineDNA PrimersHexokinaseHexoses

Identifiers

PMID15659667
PMCPMC545704
OpenAlexW2146210309

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.