Functional expression and characterization of eryA, the erythritol kinase of Brucella abortus, and enzymatic synthesis of l-Erythritol-4-phosphate

Bioorganic & Medicinal Chemistry Letters
2003.0

Abstract

The eryA gene of the bacterial pathogen Brucella abortus has been functionally expressed in Escherichia coli. The resultant EryA was shown to catalyze the ATP-dependent conversion of erythritol to L-erythritol-4-phosphate (L-E4P). The steady state kinetic parameters of this reaction were determined and the enzyme was used to prepare L-E4P which was shown to be a weak inhibitor of 2-C-methyl-D-erythritol-4-phosphate cytidyltransferase (YgbP).

Knowledge Graph

Similar Paper

Functional expression and characterization of eryA, the erythritol kinase of Brucella abortus, and enzymatic synthesis of l-Erythritol-4-phosphate
Bioorganic & Medicinal Chemistry Letters 2003.0
Escherichia coli YrbH Is a D-Arabinose 5-Phosphate Isomerase
Journal of Biological Chemistry 2003.0
An Erythromycin Derivative Produced by Targeted Gene Disruption in <i>Saccharopolyspora erythraea</i>
Science 1991.0
Cloning and sequencing of Escherichia coli ubiC and purification of chorismate lyase
Journal of Bacteriology 1992.0
A bactericidal product obtained from a mutant of escherichia coli
Biochemical and Biophysical Research Communications 1970.0
A Novel Erythromycin, 6-Desmethyl Erythromycin D, Made by Substituting an Acyltransferase Domain of the Erythromycin Polyketide Synthase
The Journal of Antibiotics 2003.0
Antibacterial activity of 2-amino-4-hydroxypyrimidine-5-carboxylates and binding to Burkholderia pseudomallei 2-C-methyl-d-erythritol-2,4-cyclodiphosphate synthase
Bioorganic &amp; Medicinal Chemistry Letters 2019.0
A Bifunctional 3,5-Epimerase/4-Keto Reductase for Nucleotide-Rhamnose Synthesis in Arabidopsis
Plant Physiology 2004.0
Identification and characterization of genes (xapA, xapB, and xapR) involved in xanthosine catabolism in Escherichia coli
Journal of Bacteriology 1995.0
Inhibition of the Fe<sub>4</sub>S<sub>4</sub>-Cluster-Containing Protein IspH (LytB): Electron Paramagnetic Resonance, Metallacycles, and Mechanisms
Journal of the American Chemical Society 2010.0