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Results 1 - 10 of 10
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EC Number BRENDA No. Title Journal Volume Pages Year Organism PubMed ID
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.136486288 Acetyl-coenzyme A:polysialic acid O-acetyltransferase from K1-positive Escherichia coli. The enzyme responsible for the O-acetyl plus phenotype and for O-acetyl form variation J. Biol. Chem. 263 8872-8878 1988 Escherichia coli 2897964
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.136687583 Biochemical characterization of the polysialic acid-specific O-acetyltransferase NeuO of Escherichia coli K1 J. Biol. Chem. 282 22217-22227 2007 Escherichia coli 17519228
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.136720818 Crystal structure analysis of the polysialic acid specific O-acetyltransferase NeuO PLoS ONE 6 e17403 2011 Escherichia coli 21390252
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.136660391 Escherichia coli K1 polysialic acid O-acetyltransferase gene, neuO, and the mechanism of capsule form variation involving a mobile contingency locus Proc. Natl. Acad. Sci. USA 102 5564-5569 2005 Escherichia coli 15809431
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.136660391 Escherichia coli K1 polysialic acid O-acetyltransferase gene, neuO, and the mechanism of capsule form variation involving a mobile contingency locus Proc. Natl. Acad. Sci. USA 102 5564-5569 2005 Escherichia coli RS174 15809431
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.136674296 Separate pathways for O acetylation of polymeric and monomeric sialic acids and identification of sialyl O-acetyl esterase in Escherichia coli K1 J. Bacteriol. 188 6195-6206 2006 Escherichia coli 16923886
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.136674296 Separate pathways for O acetylation of polymeric and monomeric sialic acids and identification of sialyl O-acetyl esterase in Escherichia coli K1 J. Bacteriol. 188 6195-6206 2006 Escherichia coli K1 16923886
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.136702229 Specific ion influences on self-association of pyruvate dehydrogenase kinase isoform 2 (PDHK2), binding of PDHK2 to the L2 lipoyl domain, and effects of the lipoyl group-binding site inhibitor, Nov3r Biochemistry 47 2312-2324 2008 Neisseria meningitidis 18220415
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.136704530 Structural and kinetic characterizations of the polysialic acid O-acetyltransferase OatWY from Neisseria meningitidis J. Biol. Chem. 284 24501-24511 2009 Neisseria meningitidis 19525232
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.136486289 Studies of the O-acetylation and (in)stability of polysialic acid Polysialic Acid 1993 165-170 1993 Escherichia coli -
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