Two active forms of UDP-N-acetylglucosamine enolpyruvyl transferase in gram-positive bacteria

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Two active forms of UDP-N-acetylglucosamine enolpyruvyl transferase in gram-positive bacteria is …
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scholarly articleQ13442814

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P356DOI10.1128/JB.182.15.4146-4152.2000
P932PMC publication ID101887
P698PubMed publication ID10894720

P2093author name stringHuang J
Brown JR
Du W
Holmes DJ
Payne DJ
Wallis NG
Chalker AF
So CY
Sylvester DR
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MurA (MurZ), the enzyme that catalyzes the first committed step in peptidoglycan biosynthesis, is essential in Escherichia coliQ24671787
Crystal structure of UDP-N-acetylglucosamine enolpyruvyltransferase, the target of the antibiotic fosfomycinQ27733409
Structure of UDP-N-acetylglucosamine enolpyruvyl transferase, an enzyme essential for the synthesis of bacterial peptidoglycan, complexed with substrate UDP-N-acetylglucosamine and the drug fosfomycinQ27734363
Evolutionary relationships of bacterial and archaeal glutamine synthetase genesQ28237950
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Cloning and sequencing of Escherichia coli murZ and purification of its product, a UDP-N-acetylglucosamine enolpyruvyl transferaseQ33202551
Origins of secondary metabolismQ33968455
Integration efficiency and genetic recombination in pneumococcal transformation.Q33982729
The mechanism of action of fosfomycin (phosphonomycin)Q34214482
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Constitutive expression of erythromycin resistance mediated by the ermAM determinant of plasmid pAM beta 1 results from deletion of 5' leader peptide sequencesQ48336078
Selective advantage of deletions enhancing chloramphenicol acetyltransferase gene expression in Streptococcus pneumoniae plasmids.Q54438346
Characterization of a Cys115 to Asp substitution in the Escherichia coli cell wall biosynthetic enzyme UDP-GlcNAc enolpyruvyl transferase (MurA) that confers resistance to inactivation by the antibiotic fosfomycin.Q54590227
Kinetics, stoichiometry, and identification of the reactive thiolate in the inactivation of UDP-GlcNAc enolpyruvoyl transferase by the antibiotic fosfomycinQ72160246
Evidence that the reaction of the UDP-N-acetylglucosamine 1-carboxyvinyltransferase proceeds through the O-phosphothioketal of pyruvic acid bound to Cys115 of the enzymeQ72709263
P433issue15
P407language of work or nameEnglishQ1860
P921main subjectgram-positive bacteriaQ857288
P304page(s)4146-4152
P577publication date2000-08-01
P1433published inJournal of BacteriologyQ478419
P1476titleTwo active forms of UDP-N-acetylglucosamine enolpyruvyl transferase in gram-positive bacteria
P478volume182

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