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
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2.3.1.136
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retinyl
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retinoids
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esterification
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retinol-binding
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arats
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crbp
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11-cis-retinal
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a-deficient
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acyl-coa:retinol
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cyp26a1
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stra6s
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all-trans-ra
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coa:retinol
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all-trans-retinyl
- 2.3.1.136
-
retinyl
-
retinoids
- esterification
-
retinol-binding
-
arats
- crbp
- 11-cis-retinal
-
a-deficient
-
acyl-coa:retinol
-
cyp26a1
-
stra6s
-
all-trans-ra
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coa:retinol
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all-trans-retinyl
Reaction
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
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Substrates Products
Substrates Products on EC 2.3.1.136 - polysialic-acid O-acetyltransferase
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REACTION DIAGRAM
acetyl-CoA + ([Glc-(alpha1-4)-Sia])
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relative activity: 19.2%
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acetyl-CoA + ([Glc-(alpha1-4)-Sia]n)
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relative activity: 100%
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acetyl-CoA + an alpha-2,8-linked polymer of sialic acid
CoA + silaic acid acetylated at O-7 or O-9
acetyl-CoA + sialic acid polymer of length 12-14
CoA + O-acetyl sialic acid polymer
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Neisseria meningitidis serogroup C capsular polysaccharide + acetyl-CoA
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relative activity: 100%
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Neisseria meningitidis serogroup C capsular polysaccharide + propionyl-CoA
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relative activity: 21.4%
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CoA + silaic acid acetylated at O-7 or O-9
Q58WP5
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acetyl-CoA + an alpha-2,8-linked polymer of sialic acid
CoA + silaic acid acetylated at O-7 or O-9
Q58WP5
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acetyl-CoA + colominic acid
CoA + O-(acetyl)-colominic acid
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substrate is a commercially available mixture of polysialic acid fragments, about 15 sialic acid residues per polymer, polysialic acids with more than 14 residues are acylated
product is polysialic acid 7- or 9-O-acetylated
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Q58WP5
the enzyme does not require constant association with its substrate for activity
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additional information
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the enzyme does not require constant association with its substrate for activity
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additional information
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polysialic-acid O-acetyltransferase is responsible for the majority of bacterial capsule modification that takes place in vivo. In addition, there exists a minor polysialic-acid O-acetyltransferase independent pathway involving O-acetylation of monomeric sialic acid
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additional information
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enzyme shows a high substrate specificity toward polysialic acid with more than 14 residues
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additional information
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polysialic-acid O-acetyltransferase is responsible for the majority of bacterial capsule modification that takes place in vivo. In addition, there exists a minor polysialic-acid O-acetyltransferase independent pathway involving O-acetylation of monomeric sialic acid
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additional information
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Q58WP5
the enzyme does not require constant association with its substrate for activity
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additional information
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no enzymatic activity is detected for free Neu5Ac and CMP-Neu5Ac, indicating that OatC is specific for oligo- or polySia. Since only Neisseria meningitidis serogroup C capsular polysaccharide (NmC-CPS) serves as an acceptor, this demonstrates that OatC is highly specific for alpha2,9-linked polySia
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additional information
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when S-(2-oxopropyl)-CoA is used as a donor activity is dramatically reduced
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additional information
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when S-(2-oxopropyl)-CoA is used as a donor activity is dramatically reduced
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