The active site of Escherichia coli UDP-N-acetylglucosamine acyltransferase. Chemical modification and site-directed mutagenesis (Q78239814)

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12 December 2019

title

The active site of Escherichia coli UDP-N-acetylglucosamine acyltransferase. Chemical modification and site-directed mutagenesis (English)

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12 December 2019

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T J Wyckoff

1

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12 December 2019

C R Raetz

series ordinal

2

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12 December 2019

language of work or name

English

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publication date

1 September 1999

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Journal of Biological Chemistry

12 December 2019

published in

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12 December 2019

volume

274

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12 December 2019

issue

38

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12 December 2019

page(s)

27047-27055

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Biochemistry of endotoxins

12 December 2019

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Molecular cloning of the genes for lipid A disaccharide synthase and UDP-N-acetylglucosamine acyltransferase in Escherichia coli

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First committed step of lipid A biosynthesis in Escherichia coli: sequence of the lpxA gene

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Biosynthesis of lipid A in Escherichia coli: identification of UDP-3-O-[(R)-3-hydroxymyristoyl]-alpha-D-glucosamine as a precursor of UDP-N2,O3-bis[(R)-3-hydroxymyristoyl]-alpha-D-glucosamine

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The envA permeability/cell division gene of Escherichia coli encodes the second enzyme of lipid A biosynthesis. UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase

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Receptor-dependent mechanisms of cell stimulation by bacterial endotoxin

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Identification of the gene encoding the Escherichia coli lipid A 4'-kinase. Facile phosphorylation of endotoxin analogs with recombinant LpxK.

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A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase

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Eight bacterial proteins, including UDP-N-acetylglucosamine acyltransferase (LpxA) and three other transferases of Escherichia coli, consist of a six-residue periodicity theme

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Three-dimensional structure of tetrahydrodipicolinate N-succinyltransferase

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Structure of the hexapeptide xenobiotic acetyltransferase from Pseudomonas aeruginosa

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Refinement of the NMR structures for acyl carrier protein with scalar coupling data

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Hydrocarbon rulers in UDP-N-acetylglucosamine acyltransferases

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Shortened hydroxyacyl chains on lipid A of Escherichia coli cells expressing a foreign UDP-N-acetylglucosamine O-acyltransferase.

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Regulation of UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase in Escherichia coli. The second enzymatic step of lipid a biosynthesis.

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41 Modification of histidyl residues in proteins by diethylpyrocarbonate

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23 Protein chemical modification as probe of structure-function relationships

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Identifiers

DOI

10.1074/JBC.274.38.27047

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10480918%20AND%20SRC:MED&resulttype=core&format=json

12 December 2019

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