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Information on EC 2.3.1.136 - polysialic-acid O-acetyltransferase
for references in articles please use BRENDA:EC2.3.1.136
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.136 polysialic-acid O-acetyltransferase
IUBMB Comments
Acts only on substrates containing more than 14 sialosyl residues. Catalyses the modification of capsular polysaccharides in some strains of Escherichia coli.
The enzyme appears in viruses and cellular organisms
- 2.3.1.136
-
retinyl
-
retinoids
- esterification
-
retinol-binding
-
arats
- crbp
- 11-cis-retinal
-
a-deficient
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acyl-coa:retinol
-
cyp26a1
-
stra6s
-
all-trans-ra
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coa:retinol
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all-trans-retinyl
Reaction Schemes
showSynonyms
lecithin:retinol acyltransferase, oatwy, polysialic acid o-acetyltransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
lecithin:retinol acyltransferase
-
-
-
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LRAT
-
-
-
-
NeuO
polysialic acid O-acetyltransferase
polysialic acid O-AcTase
polysialic-acid O-acetyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + an alpha-2,8-linked polymer of sialic acid = CoA + polysialic acid acetylated at O-7 or O-9
acetyl-CoA + an alpha-2,8-linked polymer of sialic acid = CoA + polysialic acid acetylated at O-7 or O-9
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-
-
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acetyl-CoA + an alpha-2,8-linked polymer of sialic acid = CoA + polysialic acid acetylated at O-7 or O-9
identification of highly conserved active site residues and catalytic mechanism, residues His147, Trp171, His119, and Trp143 are important, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:polysialic-acid O-acetyltransferase
Acts only on substrates containing more than 14 sialosyl residues. Catalyses the modification of capsular polysaccharides in some strains of Escherichia coli.
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CAS REGISTRY NUMBER
COMMENTARY
116412-21-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + ([Glc-(alpha1-4)-Sia])
?
Substrates: relative activity: 19.2%
Products: -
Products: -
?
acetyl-CoA + ([Glc-(alpha1-4)-Sia]n)
?
Substrates: relative activity: 100%
Products: -
Products: -
?
acetyl-CoA + an alpha-2,8-linked polymer of sialic acid
CoA + silaic acid acetylated at O-7 or O-9
acetyl-CoA + colominic acid
?
Substrates: relative activity: 2.1%
Products: -
Products: -
?
acetyl-CoA + sialic acid polymer of length 12-14
CoA + O-acetyl sialic acid polymer
-
Substrates: -
Products: -
Products: -
?
Neisseria meningitidis serogroup C capsular polysaccharide + acetyl-CoA
?
-
Substrates: relative activity: 100%
Products: -
Products: -
?
Neisseria meningitidis serogroup C capsular polysaccharide + propionyl-CoA
?
-
Substrates: relative activity: 21.4%
Products: -
Products: -
?
propionyl-CoA + colominic acid
CoA + O-(propionyl)-colominic acid
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an alpha-2,8-linked polymer of sialic acid
CoA + silaic acid acetylated at O-7 or O-9
Q58WP5
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an alpha-2,8-linked polymer of sialic acid
CoA + silaic acid acetylated at O-7 or O-9
Q58WP5
Substrates: -
Products: -
Products: -
?
acetyl-CoA + colominic acid
CoA + O-(acetyl)-colominic acid
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + colominic acid
CoA + O-(acetyl)-colominic acid
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Substrates: 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
Products: product is polysialic acid 7- or 9-O-acetylated
Products: product is polysialic acid 7- or 9-O-acetylated
?
additional information
?
-
Q58WP5
Substrates: the enzyme does not require constant association with its substrate for activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not require constant association with its substrate for activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme shows a high substrate specificity toward polysialic acid with more than 14 residues
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Q58WP5
Substrates: the enzyme does not require constant association with its substrate for activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: when S-(2-oxopropyl)-CoA is used as a donor activity is dramatically reduced
Products: -
Products: -
?
additional information
?
-
-
Substrates: when S-(2-oxopropyl)-CoA is used as a donor activity is dramatically reduced
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an alpha-2,8-linked polymer of sialic acid
CoA + silaic acid acetylated at O-7 or O-9
Q58WP5
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an alpha-2,8-linked polymer of sialic acid
CoA + silaic acid acetylated at O-7 or O-9
Q58WP5
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Blindness
Loss of cone photoreceptors caused by chromophore depletion is partially prevented by the artificial chromophore pro-drug, 9-cis-retinyl acetate.
Breast Neoplasms
Reduced lecithin:retinol acyltransferase expression in human breast cancer.
Carcinogenesis
Diethylnitrosamine-induced hepatocarcinogenesis is suppressed in lecithin:retinol acyltransferase-deficient mice primarily through retinoid actions immediately after carcinogen administration.
Carcinogenesis
Non-alcoholic steatohepatitis-related liver tumorigenesis is suppressed in mice lacking hepatic retinoid storage.
Carcinogenesis
Oral carcinogenesis induced by 4-nitroquinoline 1-oxide in lecithin:retinol acyltransferase gene knockout mice.
Carcinogenesis
Overexpression of lecithin:retinol acyltransferase in the epithelial basal layer makes mice more sensitive to oral cavity carcinogenesis induced by a carcinogen.
Carcinoma
Esterification of all-trans-retinol in normal human epithelial cell strains and carcinoma lines from oral cavity, skin and breast: reduced expression of lecithin:retinol acyltransferase in carcinoma lines.
Carcinoma
Retinol metabolism and lecithin:retinol acyltransferase levels are reduced in cultured human prostate cancer cells and tissue specimens.
Cholestasis
Altered Expression of Retinol Metabolism-Related Genes in an ANIT-Induced Cholestasis Rat Model.
Fatty Liver
Non-alcoholic steatohepatitis-related liver tumorigenesis is suppressed in mice lacking hepatic retinoid storage.
Infections
Mycobacterium tuberculosis infection is exacerbated in mice lacking lecithin:retinol acyltransferase.
Kidney Neoplasms
Differential expression of the enzyme that esterifies retinol, lecithin:retinol acyltransferase, in subtypes of human renal cancer and normal kidney.
Leber Congenital Amaurosis
Loss of cone photoreceptors caused by chromophore depletion is partially prevented by the artificial chromophore pro-drug, 9-cis-retinyl acetate.
Neoplasms
LRAT-specific domain facilitates vitamin A metabolism by domain swapping in HRASLS3.
Prostatic Neoplasms
Retinol metabolism and lecithin:retinol acyltransferase levels are reduced in cultured human prostate cancer cells and tissue specimens.
Retinitis Pigmentosa
Safety and Proof-of-Concept Study of Oral QLT091001 in Retinitis Pigmentosa Due to Inherited Deficiencies of Retinal Pigment Epithelial 65 Protein (RPE65) or Lecithin:Retinol Acyltransferase (LRAT).
Tuberculosis
Mycobacterium tuberculosis infection is exacerbated in mice lacking lecithin:retinol acyltransferase.
Vision Disorders
Loss of cone photoreceptors caused by chromophore depletion is partially prevented by the artificial chromophore pro-drug, 9-cis-retinyl acetate.
Vitamin A Deficiency
Disruption of the lecithin:retinol acyltransferase gene makes mice more susceptible to vitamin A deficiency.
Vitamin A Deficiency
Retinoid X receptor beta (RXRB) expression in Sertoli cells controls cholesterol homeostasis and spermiation.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
190
([-6)-Glc-(alpha1-4)-Sia-(alpha2-]n) oder ([-6)-Glc-(alpha1-4)-Sia-(alpha2-]n)
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzymatic activity increases linearly with increasing numbers of repeats
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
eventually membrane-bound or membrane-associated protein
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
the homotrimeric enzyme belongs to the left-handed beta-helix family of acyltransferases and is characterized by an unusual funnel-shaped outline
physiological function
-
K1 capsule O-acetylation undergoes highfrequency phase-variation involving also the polysialic acid specific O-acetyltransferase
additional information
-
the enzymatic activity linearly increases with the length of the N-terminal poly-psi-domain which is composed of a variable number of tandem copies of an RLKTQDS heptad, the poly-psi-domain is not resolved in the crystal structure
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A402DK36_MICAE
191
1
22015
TrEMBL
-
A0A5A5RWP6_MICAE
76
0
8223
TrEMBL
-
A0A402DEK2_MICAE
202
0
22512
TrEMBL
-
A0A5A5RD94_MICAE
198
1
22916
TrEMBL
-
A0A645JEX0_9ZZZZ
137
1
14825
TrEMBL
other Location (Reliability: 2)
A0A2H9T429_9ZZZZ
92
0
11389
TrEMBL
other Location (Reliability: 1)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
54000
-
SDS-PAGE, the first 34 amino acids form an efficient oligomerization domain, 2 * 54000 Da
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
-
SDS-PAGE, the first 34 amino acids form an efficient oligomerization domain, 2 * 54000 Da
homotrimer
additional information
homotrimer
-
the enzyme belongs to the left-handed beta-helix family of acyltransferases and is characterized by an unusual funnel-shaped outline. NeuO displays an unusual quaternary structure arrangement presumably is an adaptation to accommodate the exceptionally long polySia acceptor
additional information
Q58WP5
enzyme consists of a catalytic and a non-catalytic domain encoded by a tandem heptanucleotide repeat region
additional information
-
enzyme consists of a catalytic and a non-catalytic domain encoded by a tandem heptanucleotide repeat region
additional information
-
domain structures, and three-dimensional structure of NeuO, modelling, overview
additional information
-
enzyme consists of a catalytic and a non-catalytic domain encoded by a tandem heptanucleotide repeat region
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified engineered apo-NeuO, a protein variant with four N-terminal RLKTQDS heptads, sitting drop vapour diffusion, 6.3 mg/ml protein in 10 mM Tris-HCl pH 7.5 and 150 mM NaCl, mixed with precipitant solution containing 0.1 M Tris, pH 7.2, 0.45 M glycine, 0.2 M NH4NO3, 7% PEG 4000 w/v, 1 week, 20°C, X-ray diffraction structure determination and analysis at 1.7 A resolution, molecular replacement
-
OatWY is crystalised with bound substrate acetyl-CoA and its analogs (CoA, S-(2-oxopropyl)-CoA) using the hanging drop vapor diffusion technique. The structure of OatWY reveals an intimate homotrimer of left-handed beta-helix motifs that frame a deep active site cleft selective for the polysialic acid-bearing substrate. A significant movement of Tyr-171 blocks the active site of the enzyme in its native form
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H119A
-
complete loss of enzymatic activity without affecting the oligomerization state
NeuO + 12 hepta-nucleotide repeats
-
a set of NeuO alleles with N-terminal 0, 12, 24, and 36 hepta-nucleotide repeats are generated: protein yield: 3.7 mg/L, Km (mM): 0.22 (acetyl-CoA), 1.1 (colomnic acid), kcat (1/sec): 0.56 (acetyl-CoA), 1.85 (colomnic acid)
NeuO + 24 hepta-nucleotide repeats
-
a set of NeuO alleles with N-terminal 0, 12, 24, and 36 hepta-nucleotide repeats are generated: protein yield: 5.0 mg/L, Km (mM): 0.27 (acetyl-CoA), 1.0 (colomnic acid), kcat (1/sec): 1.07 (acetyl-CoA), 2.57 (colomnic acid)
NeuO + 36 hepta-nucleotide repeats
-
a set of NeuO alleles with N-terminal 0, 12, 24, and 36 hepta-nucleotide repeats are generated: protein yield: 5.0 mg/L, Km (mM): 0.22 (acetyl-CoA), 0.22 (propionyl-CoA) 1.6 (colomnic acid), kcat (1/sec): 1.16 (acetyl-CoA), 0.09 (propionyl-CoA), 3.84 (colomnic acid)
W143A
-
complete loss of enzymatic activity without affecting the oligomerization state
DELTA1-103
-
mutant lacking the first 103 amino acids: after purification mutant is found as a monomer, indicating that dimerization of OatC depends on the first 34 amino acids. Mutant shows no activity
DELTA1-34
-
mutant lacking the first 34 amino acids: after purification mutant is found as a monomer, indicating that dimerization of OatC depends on the first 34 amino acids. Mutant retains 25% activity
H456A
-
mutant shows reduced enzymatic activity, 70% of wild-type level
additional information
additional information
Q58WP5
deletion of gene neuO in strain EV291 eliminates enzyme activity, which can be complemented in trans, mutagenesis method, overview, nonfunctional enzyme encoded by inserted gene neuO-4 allele from unequal or mispairing recombination, GenBank AY779019, role of redistribution variant neuO alleles in pathogen evolution, function of localized hypermutability
additional information
-
deletion of gene neuO in strain EV291 eliminates enzyme activity, which can be complemented in trans, mutagenesis method, overview, nonfunctional enzyme encoded by inserted gene neuO-4 allele from unequal or mispairing recombination, GenBank AY779019, role of redistribution variant neuO alleles in pathogen evolution, function of localized hypermutability
additional information
-
engineering of a neuO gene that allows phase-stable expression of NeuO with four N-terminal heptads
additional information
-
deletion of gene neuO in strain EV291 eliminates enzyme activity, which can be complemented in trans, mutagenesis method, overview, nonfunctional enzyme encoded by inserted gene neuO-4 allele from unequal or mispairing recombination, GenBank AY779019, role of redistribution variant neuO alleles in pathogen evolution, function of localized hypermutability
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
endogenous polysialic acid stabilizes by a close non-covalent association with the enzyme
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant engineered C-terminally His6-tagged NeuO mutant from Escherichia coli strain BL21 gold (DE3) by nickel affinity chromatography, gel filtration, and ultrafiltration
-
using a HisTrap HP column and a a Superdex 200 HR 10/30 column. FInal yield: 24 mg of enzyme from 500 ml of bacterial culture
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a C-terminal hexahistidine tagged fusion protein
-
expressed in Escherichia coli as a C-terminal hexahistidine-tagged fusion protein
-
expression of the engineered C-terminally His6-tagged NeuO mutant in Escherichia coli strain BL21 gold (DE3)
-
gene neuO, allelic variants, DNA and amino acid sequence determination and analysis, the enzyme is genetically linked to the endo-neuraminidase tail protein gene of a chromosomal accretion element CUS-3, genetic structure, role of heptanucleotide repeat regions, overview
Q58WP5
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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
brenda
Varki, A.; Higa, H.
Studies of the O-acetylation and (in)stability of polysialic acid
Polysialic Acid
1993
165-170
1993
Escherichia coli
-
brenda
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)
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
EXTERNAL LINKS (specific for EC-Number 2.3.1.136)