Functional expression and characterization of EryA, the erythritol kinase of Brucella abortus, and enzymatic synthesis of L-erythritol-4-phosphate.
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).
Lillo
Antonietta M
AM
Department of Chemistry, Brown University, Providence, RI 02912-9108, USA.
Tetzlaff
Charles N
CN
Sangari
Félix J
FJ
Cane
David E
DE
D000255:Adenosine Triphosphate / Q000378:metabolism; D002003:Brucella abortus / Q000201:enzymology*; D003001:Cloning, Molecular; D004896:Erythritol / Q000031:analogs & derivatives* / Q000096:biosynthesis* / Q000378:metabolism / Q000494:pharmacology; D007700:Kinetics; D009713:Nucleotidyltransferases / Q000037:antagonists & inhibitors; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000235:genetics / Q000378:metabolism*; D013403:Sugar Phosphates / Q000096:biosynthesis* / Q000494:pharmacology
D013403:Sugar Phosphates; C081898:erythritol 4-phosphate; D000255:Adenosine Triphosphate; D017853:Phosphotransferases (Alcohol Group Acceptor); C478753:erythritol kinase; C435808:2-C-methyl erythritol 4-phosphate cytidylyltransferase; D009713:Nucleotidyltransferases; D004896:Erythritol