Oxygen requirement for the biosynthesis of the S-2-hydroxymyristate moiety in Salmonella typhimurium lipid A. Function of LpxO, A new Fe2+/alpha-ketoglutarate-dependent dioxygenase homologue

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Oxygen requirement for the biosynthesis of the S-2-hydroxymyristate moiety in Salmonella typhimurium lipid A. Function of LpxO, A new Fe2+/alpha-ketoglutarate-dependent dioxygenase homologue is …
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scholarly articleQ13442814

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P356DOI10.1074/JBC.M005779200
P698PubMed publication ID10903325

P2093author name stringLin S
Raetz CR
Cotter RJ
Gibbons HS
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A fully active catalytic domain of bovine aspartyl (asparaginyl) beta-hydroxylase expressed in Escherichia coli: characterization and evidence for the identification of an active-site region in vertebrate alpha-ketoglutarate-dependent dioxygenasesQ35623050
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P433issue42
P407language of work or nameEnglishQ1860
P921main subjectSalmonella TyphimuriumQ166491
P304page(s)32940-32949
P577publication date2000-10-01
P1433published inJournal of Biological ChemistryQ867727
P1476titleOxygen requirement for the biosynthesis of the S-2-hydroxymyristate moiety in Salmonella typhimurium lipid A. Function of LpxO, A new Fe2+/alpha-ketoglutarate-dependent dioxygenase homologue
P478volume275

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