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2.3.1.136: polysialic-acid O-acetyltransferase

This is an abbreviated version!
For detailed information about polysialic-acid O-acetyltransferase, go to the full flat file.

Word Map on EC 2.3.1.136

Reaction

acetyl-CoA
+
an alpha-2,8-linked polymer of sialic acid
=
CoA
 +
polysialic acid acetylated at O-7 or O-9

Synonyms

lecithin:retinol acyltransferase, LRAT, NeuO, OatC, OatWY, polySia specific O-acetyltransferase, polysialic acid O-acetyltransferase, polysialic acid O-AcTase, polysialic acid specific O-acetyltransferase, polysialic acid-specific O-acetyltransferase, polysialic-acid O-acetyltransferase

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.136 polysialic-acid O-acetyltransferase

Reference

topprint

Reference on EC 2.3.1.136 - polysialic-acid O-acetyltransferase

Please use the Reference Search for a specific query.
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Higa, H.H.; Varki, A.
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
Manually annotated by BRENDA team
Varki, A.; Higa, H.
Studies of the O-acetylation and (in)stability of polysialic acid
Polysialic Acid
1993
165-170
1993
Escherichia coli
-
Manually annotated by BRENDA team
Deszo, E.L.; Steenbergen, S.M.; Freedberg, D.I.; Vimr, E.R.
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 (Q58WP5), Escherichia coli, Escherichia coli RS174 (Q58WP5)
Manually annotated by BRENDA team
Steenbergen, S.M.; Lee, Y.C.; Vann, W.F.; Vionnet, J.; Wright, L.F.; Vimr, E.R.
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, Escherichia coli K1
Manually annotated by BRENDA team
Bergfeld, A.K.; Claus, H.; Vogel, U.; Muehlenhoff, M.
Biochemical characterization of the polysialic acid-specific O-acetyltransferase NeuO of Escherichia coli K1
J. Biol. Chem.
282
22217-22227
2007
Escherichia coli
Manually annotated by BRENDA team
Hiromasa, Y.; Yan, X.; Roche, T.E.
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
Manually annotated by BRENDA team
Lee, H.J.; Rakic, B.; Gilbert, M.; Wakarchuk, W.W.; Withers, S.G.; Strynadka, N.C.
Structural and kinetic characterizations of the polysialic acid O-acetyltransferase OatWY from Neisseria meningitidis
J. Biol. Chem.
284
24501-24511
2009
Neisseria meningitidis (O33391), Neisseria meningitidis
Manually annotated by BRENDA team
Schulz, E.C.; Bergfeld, A.K.; Ficner, R.; Muehlenhoff, M.
Crystal structure analysis of the polysialic acid specific O-acetyltransferase NeuO
PLoS ONE
6
e17403
2011
Escherichia coli
Manually annotated by BRENDA team