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Purification and characterization of the bacterial UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase WecA
scientific journal article
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scholarly article
1 reference
stated in
PubMed
PubMed ID
18723618
retrieved
24 January 2017
title
Purification and characterization of the bacterial UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase WecA
(English)
1 reference
stated in
PubMed
PubMed ID
18723618
retrieved
24 January 2017
main subject
N-acetyl-D-glucosaminyl-1-diphospho-ditrans,polycis-undecaprenol(2-)
1 reference
stated in
ChEBI release 2020-05-28
ChEBI ID
60047
author
Ahmed Bouhss
series ordinal
3
object named as
Ahmed Bouhss
0 references
Dominique Mengin-Lecreulx
object named as
Dominique Mengin-Lecreulx
series ordinal
2
0 references
author name string
Bayan Al-Dabbagh
series ordinal
1
1 reference
stated in
PubMed
PubMed ID
18723618
retrieved
24 January 2017
Ahmed Bouhss
series ordinal
3
1 reference
stated in
PubMed
PubMed ID
18723618
retrieved
24 January 2017
language of work or name
English
0 references
publication date
1 November 2008
1 reference
stated in
PubMed
PubMed ID
18723618
retrieved
24 January 2017
published in
Journal of Bacteriology
1 reference
stated in
PubMed
PubMed ID
18723618
retrieved
24 January 2017
volume
190
1 reference
stated in
PubMed
PubMed ID
18723618
retrieved
24 January 2017
issue
21
1 reference
stated in
PubMed
PubMed ID
18723618
retrieved
24 January 2017
page(s)
7141–7146
1 reference
stated in
PubMed
PubMed ID
18723618
retrieved
24 January 2017
cites work
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Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
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The biosynthesis of peptidoglycan lipid-linked intermediates
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Functional characterization and membrane topology of Escherichia coli WecA, a sugar-phosphate transferase initiating the biosynthesis of enterobacterial common antigen and O-antigen lipopolysaccharide
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Modeling bacterial UDP-HexNAc: polyprenol-P HexNAc-1-P transferases
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The bacA gene of Escherichia coli encodes an undecaprenyl pyrophosphate phosphatase activity
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Purification and characterization of the bacterial MraY translocase catalyzing the first membrane step of peptidoglycan biosynthesis
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Synthesis and inhibition properties of conformational probes for the mutase-catalyzed UDP-galactopyranose/furanose interconversion.
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Three monophyletic superfamilies account for the majority of the known glycosyltransferases
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Genetic modulation of Shigella flexneri 2a lipopolysaccharide O antigen modal chain length reveals that it has been optimized for virulence.
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The N-terminal region of the Escherichia coli WecA (Rfe) protein, containing three predicted transmembrane helices, is required for function but not for membrane insertion.
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Polyisoprenyl phosphate specificity of UDP-GlcNAc:undecaprenyl phosphate N-acetylglucosaminyl 1-P transferase from E.coli
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PubMed Central
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Biosynthesis of lipopolysaccharide O antigens
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PubMed Central
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Role of the rfe gene in the biosynthesis of the Escherichia coli O7-specific lipopolysaccharide and other O-specific polysaccharides containing N-acetylglucosamine
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PubMed Central
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29 September 2017
Prolonged incubation in calcium chloride improves the competence of Escherichia coli cells
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PubMed Central
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29 September 2017
Conserved aspartic acids are essential for the enzymic activity of the WecA protein initiating the biosynthesis of O-specific lipopolysaccharide and enterobacterial common antigen in Escherichia coli
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PubMed Central
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Mechanism of action of tunicamycin on the UDP-GlcNAc:dolichyl-phosphate GlcNAc-1-phosphate transferase
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PubMed Central
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20 June 2018
Conserved amino acid residues found in a predicted cytosolic domain of the lipopolysaccharide biosynthetic protein WecA are implicated in the recognition of UDP-N-acetylglucosamine
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reference URL
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27 November 2018
Topological analysis of the MraY protein catalysing the first membrane step of peptidoglycan synthesis.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2580700
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27 November 2018
A family of UDP-GlcNAc/MurNAc: polyisoprenol-P GlcNAc/MurNAc-1-P transferases.
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2580700
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27 November 2018
Topological and mutational analysis of KpsM, the hydrophobic component of the ABC-transporter involved in the export of polysialic acid in Escherichia coli K1
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/18723618
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Conserved sequences in enzymes of the UDP-GlcNAc/MurNAc family are essential in hamster UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/18723618
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
UDP-N- acetylglucosamine:N -acetylmuramoyl-(pentapeptide) pyrophosphoryl undecaprenol N -acetylglucosamine transferase from Escherichia coli : overproduction, solubilization, and purification
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/18723618
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Conserved cytoplasmic motifs that distinguish sub-groups of the polyprenol phosphate:N-acetylhexosamine-1-phosphate transferase family
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/18723618
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1128/JB.00676-08
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3536269
OpenCitations bibliographic resource ID
3536269
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3536269
PMCID
2580700
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3536269
PubMed ID
18723618
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3536269
ResearchGate publication ID
23190476
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