Evidence map›Paper›PMID 25204504›Full record

ArticleBiochemical and biophysical research communications2014

Kdo hydroxylase is an inner core assembly enzyme in the Ko-containing lipopolysaccharide biosynthesis.

Hak Suk Chung, Eun Gyeong Yang, Dohyeon Hwang, Ji Eun Lee, Ziqiang Guan, Christian R H Raetz

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochemical and biophysical research communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.4field-weighted citation impact, top 32% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Lipopolysaccharide of theBiomolecules · 2021
    Review
  2. International journal of molecular sciences · 2021
    Article
  3. Article
  4. 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

6 authors at 3 institutions in 2 countries.

Hak Suk ChungCenter for Theragnosis, Korea Institute of Science and Technology, Seoul 136-791, Republic of Korea; Department of Biological Chemistry, KIST Campus, Korea University of Science and Technology (UST), Seoul 136-791, Republic of Korea. Electronic address: hschung@kist.re.kr.
Eun Gyeong YangCenter for Theragnosis, Korea Institute of Science and Technology, Seoul 136-791, Republic of Korea; Department of Biological Chemistry, KIST Campus, Korea University of Science and Technology (UST), Seoul 136-791, Republic of Korea.
Dohyeon HwangDepartment of Biological Chemistry, KIST Campus, Korea University of Science and Technology (UST), Seoul 136-791, Republic of Korea.
Ji Eun LeeCenter for Theragnosis, Korea Institute of Science and Technology, Seoul 136-791, Republic of Korea.
Ziqiang GuanDepartment of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
Christian R H RaetzDepartment of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
Duke Medical Center · USKorea Institute of Science and Technology · KRKorea University of Science and Technology · KR

Funding

STEROL LIPIDSU54GM069338 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DENNIS, EDWARD A · 2003 to 2013
$72.2M
BIOSYNTHESIS AND FUNCTION OF LIPOPOLYSACCHARIDESR01GM051310 · NIGMS · DUKE UNIVERSITY · PI ZHOU, PEI · 1994 to 2013
$8.1M
NIGMS NIH HHS GM-069338NIGMS NIH HHS GM-51310NIGMS NIH HHS R01 GM051310NIGMS NIH HHS U54 GM069338
6 · The paper itself

Abstract

The lipopolysaccharide (LPS) isolated from certain important Gram-negative pathogens including a human pathogen Yersinia pestis and opportunistic pathogens Burkholderia mallei and Burkholderia pseudomallei contains d-glycero-d-talo-oct-2-ulosonic acid (Ko), an isosteric analog of 3-deoxy-d-manno-oct-2-ulosonic acid (Kdo). Kdo 3-hydroxylase (KdoO), a Fe(2+)/α-KG/O2 dependent dioxygenase from Burkholderia ambifaria and Yersinia pestis is responsible for Ko formation with Kdo2-lipid A as a substrate, but in which stage KdoO functions during the LPS biosynthesis has not been established. Here we purify KdoO from B. ambifaria (BaKdoO) to homogeneity for the first time and characterize its substrates. BaKdoO utilizes Kdo2-lipid IVA or Kdo2-lipid A as a substrate, but not Kdo-lipid IVAin vivo as well as in vitro and Kdo-(Hep)kdo-lipid A in vitro. These data suggest that KdoO is an inner core assembly enzyme that functions after the Kdo-transferase KdtA but before the heptosyl-transferase WaaC enzyme during the Ko-containing LPS biosynthesis.

Indexed as

BurkholderiaCations, DivalentGene ExpressionGlycolipidsGlycosyltransferasesIronKetoglutaric AcidsLipid ALipopolysaccharidesMixed Function OxygenasesOxygenSubstrate SpecificityTransferases3-deoxy-D-manno-octulosonate transferaseCations, DivalentGlycolipidsGlycosyltransferasesIronKdo2-lipid AKetoglutaric AcidsLipid Alipid A precursors, bacteriallipooligosaccharide 1,5-heptosyltransferaseLipopolysaccharidesMixed Function OxygenasesOxygenTransferasesBurkholderia LPSFe(2+)/O(2)/α-KG dependent dioxygenaseKdo hydroxylaseKo formationLPS inner core assembly

Identifiers

PMID25204504
PMCPMC4282518
OpenAlexW2136805261

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.