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2-acetamido-6-azido-2,6-dideoxy-D-mannose + phosphoenolpyruvate + H2O
5-acetamido-9-azido-3,5,9-trideoxy-D-glycero-D-galacto-2-nonulosonic acid + phosphate
N-acetyl-D-galactosamine + phosphoenolpyruvate + H2O
?
-
15% of the activity with N-acetyl-D-mannosamine
-
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
N-acetylneuraminate + phosphate
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
N-acetylneuraminate + phosphate
-
-
-
?
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
phosphate + N-acetylneuraminate
phosphoenolpyruvate + N-butanoyl-D-mannosamine + H2O
phosphate + N-butanoylneuraminate
-
-
-
-
?
phosphoenolpyruvate + N-pentanoyl-D-mannosamine + H2O
phosphate + N-pentanoylneuraminate
-
-
-
-
?
phosphoenolpyruvate + N-propanoyl-D-mannosamine + H2O
phosphate + N-propanoylneuraminate
-
-
-
-
?
additional information
?
-
2-acetamido-6-azido-2,6-dideoxy-D-mannose + phosphoenolpyruvate + H2O
5-acetamido-9-azido-3,5,9-trideoxy-D-glycero-D-galacto-2-nonulosonic acid + phosphate
-
-
-
?
2-acetamido-6-azido-2,6-dideoxy-D-mannose + phosphoenolpyruvate + H2O
5-acetamido-9-azido-3,5,9-trideoxy-D-glycero-D-galacto-2-nonulosonic acid + phosphate
-
-
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
?
-
the neuB genes appear to be involved in the biosynthesis of at least two distinct surface structures: lipooligosaccharide and flagella
-
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
?
-
the neuB genes appear to be involved in the biosynthesis of at least two distinct surface structures: lipooligosaccharide and flagella
-
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
?
-
the enzyme is necessary for the synthesis of N-acetylneuraminate which is required for synthesis of the capsular polysaccharide alpha(2-8)poly-N-acetylneuraminic acid. This polysaccharide is an essential virulence factor of the neuropathogenic bacteria
-
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
?
-
the enzyme is necessary for the synthesis of N-acetylneuraminate which is required for synthesis of the capsular polysaccharide alpha(2-8)poly-N-acetylneuraminic acid. This polysaccharide is an essential virulence factor of the neuropathogenic bacteria
-
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
?
-
the enzyme is involved in sialic acid synthesis
-
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
?
-
the enzyme is involved in sialic acid synthesis
-
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
?
-
the enzyme is involved in sialic acid synthesis
-
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
N-acetylneuraminate + phosphate
-
-
-
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
N-acetylneuraminate + phosphate
-
-
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
N-acetylneuraminate + phosphate
-
-
-
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
N-acetylneuraminate + phosphate
-
-
-
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
N-acetylneuraminate + phosphate
-
specific for
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
N-acetylneuraminate + phosphate
-
specific for
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
N-acetylneuraminate + phosphate
-
-
-
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
N-acetylneuraminate + phosphate
-
-
-
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
N-acetylneuraminate + phosphate
-
specific for
-
ir
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
N-acetylneuraminate + phosphate
-
the reaction strongly favors the formation of N-acetylneuraminic acid and appears to be irreversible
-
ir
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
N-acetylneuraminate + phosphate
-
-
-
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
N-acetylneuraminate + phosphate
-
-
-
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
N-acetylneuraminate + phosphate
-
-
-
-
?
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
phosphate + N-acetylneuraminate
-
-
-
-
?
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
phosphate + N-acetylneuraminate
-
-
-
-
?
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
phosphate + N-acetylneuraminate
-
-
-
-
?
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
phosphate + N-acetylneuraminate
-
-
-
ir
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
phosphate + N-acetylneuraminate
-
-
-
ir
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
phosphate + N-acetylneuraminate
-
-
-
?
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
phosphate + N-acetylneuraminate
-
-
-
?
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
phosphate + N-acetylneuraminate
-
-
-
-
?
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
phosphate + N-acetylneuraminate
-
-
-
?
additional information
?
-
-
enzyme catalyzes the condensation of the si face of phosphoenolpyruvate with the aldehyde sugar
-
-
?
additional information
?
-
the enzyme shows activity towards 2-acetamido-4-O-acetyl-2-deoxy-D-mannopyranose resulting in formation of 4-O-acetyl-ManNAc
-
-
?
additional information
?
-
-
the enzyme shows activity towards 2-acetamido-4-O-acetyl-2-deoxy-D-mannopyranose resulting in formation of 4-O-acetyl-ManNAc
-
-
?
additional information
?
-
the enzyme shows activity towards 2-acetamido-4-O-acetyl-2-deoxy-D-mannopyranose resulting in formation of 4-O-acetyl-ManNAc
-
-
?
additional information
?
-
binding of phosphoenolpyruvate is associated with a change in the average conformation of enzyme NmeNANAS causing changes in flexibility in both AFPL domain and ManNAc binding loop
-
-
?
additional information
?
-
-
binding of phosphoenolpyruvate is associated with a change in the average conformation of enzyme NmeNANAS causing changes in flexibility in both AFPL domain and ManNAc binding loop
-
-
?
additional information
?
-
binding of phosphoenolpyruvate is associated with a change in the average conformation of enzyme NmeNANAS causing changes in flexibility in both AFPL domain and ManNAc binding loop
-
-
?
additional information
?
-
-
arginine residues are present in the active site and are involved in substrate recognition and binding
-
-
?
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N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
?
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
N-acetylneuraminate + phosphate
-
-
-
?
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
phosphate + N-acetylneuraminate
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
?
-
the neuB genes appear to be involved in the biosynthesis of at least two distinct surface structures: lipooligosaccharide and flagella
-
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
?
-
the neuB genes appear to be involved in the biosynthesis of at least two distinct surface structures: lipooligosaccharide and flagella
-
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
?
-
the enzyme is necessary for the synthesis of N-acetylneuraminate which is required for synthesis of the capsular polysaccharide alpha(2-8)poly-N-acetylneuraminic acid. This polysaccharide is an essential virulence factor of the neuropathogenic bacteria
-
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
?
-
the enzyme is necessary for the synthesis of N-acetylneuraminate which is required for synthesis of the capsular polysaccharide alpha(2-8)poly-N-acetylneuraminic acid. This polysaccharide is an essential virulence factor of the neuropathogenic bacteria
-
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
?
-
the enzyme is involved in sialic acid synthesis
-
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
?
-
the enzyme is involved in sialic acid synthesis
-
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
?
-
the enzyme is involved in sialic acid synthesis
-
-
?
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
phosphate + N-acetylneuraminate
-
-
-
ir
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
phosphate + N-acetylneuraminate
-
-
-
ir
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
phosphate + N-acetylneuraminate
-
-
-
?
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
phosphate + N-acetylneuraminate
-
-
-
?
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
phosphate + N-acetylneuraminate
-
-
-
-
?
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
phosphate + N-acetylneuraminate
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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5-(carboxyamino)-3,5-dideoxy-2-O-phosphono-D-erythro-L-manno-nononic acid
-
residues Glu25, Gln55, Asn74, Thr110, Phe112, Lys129, Asn184, Tyr186, Ser213, His215, Glu234, Phe288, and Arg314 amino acids are in close proximity and have essential interactions with the ligand
5-acetamido-4,6,7,8,9-pentahydroxy-2-phosphorylnonanoic acid ditriethylammonium salt
4.5/1 mixture of 2S-inhibitor/2R-inhibitor, competitive inhibitor against phosphoenolpyruvate
AgNO3
-
1 mM, 61% inhibition
Co2+
stabilizes at low and inhibits at higher concentrations
ethyl 3-benzoyl-2,7-dimethyl indolizine-1-carboxylate
-
inhibitor identified by molecular modeling. The compound shows important polar interactions with the Mn2+ ion, as well as with the Gln55, Asn184, and Arg314 residues
Fe2+
-
1 mM FeCl2, 40% inhibition
HgCl2
-
at 0.01 mM 85% inhibition, at 0.1 mM complete inhibition
hydroxylamine
-
1 mM, 23% inhibition
Iodine
-
1 mM, 30% inhibition
Li+
-
1 mM LiCl, 30% inhibition
N-bromosuccinimide
-
1 mM, 24% inhibition
PCMB
-
1 mM, complete inhibition
Phenylglyoxal
-
N-acetylmannosamine or phosphoenolpyruvate protect
Semicarbazide
-
1 mM, 20% inhibition
Cu2+
-
1 mM CuCl2, 29% inhibition
Cu2+
-
10 mM CuCl2, 90% inhibition
EDTA
-
10 mM, complete inhibition
EDTA
slightly inhibitory at 1 mM
EDTA
-
10 mM, complete inhibition
EDTA
-
1 or 10 mM, 97% inhibition
K+
27% inhibition at 1 mM
K+
-
1 mM KCl, 92% inhibition
Na+
slightly inhibitory at 1 mM
Na+
-
1 mM NaCl, 20% inhibition
Zn2+
-
0.1 mM, 68% of initial activity
Zn2+
-
1 mM ZnCl2, 80% inhibition
additional information
no or poor effect by Mg2+ and Ca2+ at 1 mM
-
additional information
-
no or poor effect by Mg2+ and Ca2+ at 1 mM
-
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metabolism
formation of sialic acid or N-acetylneuraminic acid to produce a capsular polysacccharide of polysialic acid to evade the host's immune system by mimicking its own cell surface polysaccharides
malfunction
a truncated variant of the enzyme lacking the C-terminal AFPL domain is soluble and catalytically inactive, loss of the AFPL domain destabilizes the dimeric form of the enzyme. The AFPL domain plays a critical role for both the catalytic function and quaternary structure stability of N-acetylneuraminic acid synthase. phosphoenolpyruvate has a major effect on the thermal stability of the enzyme and loss of the AFPL domain in mutant G272Term eliminates this property
malfunction
biallelic mutations in gene NANS, the gene encoding N-acetylneuraminic acid synthase, in nine individuals causes infantile-onset severe developmental delay and skeletal dysplasia. The main clinical features of the disorder included a prenatal history that is unremarkable in all patients except for one, in whom prenatal hydrocephalus is diagnosed. Patient body fluids show an elevation in N-acetyl-D-mannosamine levels, and patient-derived fibroblasts have reduced enzyme activity and are unable to incorporate sialic acid precursors into sialylated glycoproteins, phenotypes, overview
malfunction
knockdown of nansa in zebrafish embryos results in abnormal skeletal development, but with normal sialylation of plasma proteins, and exogenously added sialic acid partially rescues the skeletal phenotype
malfunction
-
a truncated variant of the enzyme lacking the C-terminal AFPL domain is soluble and catalytically inactive, loss of the AFPL domain destabilizes the dimeric form of the enzyme. The AFPL domain plays a critical role for both the catalytic function and quaternary structure stability of N-acetylneuraminic acid synthase. phosphoenolpyruvate has a major effect on the thermal stability of the enzyme and loss of the AFPL domain in mutant G272Term eliminates this property
-
physiological function
enzyme-mediated synthesis of sialic acid is required for early brain development and skeletal growth
physiological function
key enzyme in microorganisms for producing N-acetylneuraminic acid through the irreversible condensation of N-acetylmannosamine and phosphoenolpyruvate
physiological function
sialic acid N-acetylneuraminic acid (NANA) has a key role in the pathogenesis of a select number of neuroinvasive bacteria such as Neisseria meningitidis. These pathogens coat themselves with polysialic acids, mimicking the exterior surface of mammalian cells and consequentially concealing the bacteria from the host's immune system. N-acetylneuraminic acid is synthesized in bacteria by the homodimeric enzyme NANA synthase (NANAS), which catalyzes a condensation reaction between phosphoenolpyruvate (PEP) and N-acetylmannosamine
physiological function
-
key enzyme in microorganisms for producing N-acetylneuraminic acid through the irreversible condensation of N-acetylmannosamine and phosphoenolpyruvate
-
physiological function
-
sialic acid N-acetylneuraminic acid (NANA) has a key role in the pathogenesis of a select number of neuroinvasive bacteria such as Neisseria meningitidis. These pathogens coat themselves with polysialic acids, mimicking the exterior surface of mammalian cells and consequentially concealing the bacteria from the host's immune system. N-acetylneuraminic acid is synthesized in bacteria by the homodimeric enzyme NANA synthase (NANAS), which catalyzes a condensation reaction between phosphoenolpyruvate (PEP) and N-acetylmannosamine
-
additional information
a complex hydrogen-bonding relay links the roles of the catalytic and AFPL domains across subunit boundaries, analyzed by small angle X-ray scattering, molecular dynamics simulations, and amino acid substitutions, overview
additional information
-
a complex hydrogen-bonding relay links the roles of the catalytic and AFPL domains across subunit boundaries, analyzed by small angle X-ray scattering, molecular dynamics simulations, and amino acid substitutions, overview
additional information
residue Arg314 is essential for catalysis, the delocalized positively charged guanidinium functionality of this residue provides steering of the sugar substrate ManNAc for suitable placement in the active site and thus reaction with phosphoenolpyruvate
additional information
-
residue Arg314 is essential for catalysis, the delocalized positively charged guanidinium functionality of this residue provides steering of the sugar substrate ManNAc for suitable placement in the active site and thus reaction with phosphoenolpyruvate
additional information
-
residue Arg314 is essential for catalysis, the delocalized positively charged guanidinium functionality of this residue provides steering of the sugar substrate ManNAc for suitable placement in the active site and thus reaction with phosphoenolpyruvate
-
additional information
-
a complex hydrogen-bonding relay links the roles of the catalytic and AFPL domains across subunit boundaries, analyzed by small angle X-ray scattering, molecular dynamics simulations, and amino acid substitutions, overview
-
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?
-
x * 43300, His-tagged recombinant enzyme, MALDI-TOF MS
dimer
-
2 * 52000, SDS-PAGE
dimer
-
2 * 52000, SDS-PAGE
-
dimer
-
2 * 39000, SDS-PAGE
dimer
-
2 * 38987, electrospray ionisation mass spectrometry
homodimer
2 * 45000, about, recombinant enzyme, SDS-PAGE, 2 * 41000, about, recombinant enzyme, HPLC/MS/ESI
homodimer
-
2 * 45000, about, recombinant enzyme, SDS-PAGE, 2 * 41000, about, recombinant enzyme, HPLC/MS/ESI
-
homodimer
2 * 38935, sequence calculation, 2 * 38000, about, recombinant enzyme, SDS-PAGE
homodimer
the enzyme comprises two distinct domains, an N-terminal catalytic (beta/alpha)8 barrel linked to a C-terminal antifreeze protein-like (AFPL) domain. Loss of the AFPL domain destabilizes the dimeric form of the enzyme nd renders it inactive. The AFPL domain plays a critical role for both the catalytic function and quaternary structure stability of N-acetylneuraminic acid synthase. The enzyme mutant G272Term lacking the AFPL domain is partly monomeric
homodimer
-
the enzyme comprises two distinct domains, an N-terminal catalytic (beta/alpha)8 barrel linked to a C-terminal antifreeze protein-like (AFPL) domain. Loss of the AFPL domain destabilizes the dimeric form of the enzyme nd renders it inactive. The AFPL domain plays a critical role for both the catalytic function and quaternary structure stability of N-acetylneuraminic acid synthase. The enzyme mutant G272Term lacking the AFPL domain is partly monomeric
-
monomer
-
1 * 38629, calculated from amino acid sequence
monomer
-
1 * 38649, ESI-MS
tetramer
-
4 * 40538, LC-MS analysis
tetramer
-
ESI-MS, possibly dimer of dimers
tetramer
-
ESI-MS, possibly dimer of dimers
additional information
the enzyme structure has a distinct domain architecture 4 without a cystathionine-beta-synthase domain (cystathionine-beta-synthetase domain), unlike domain architecture 3. The arginine essential for catalysis, that is present in antifreeze-like domain (block X), is not fully conserved in NeuB, but is replaced by a serine in domain architectures 3 and 4, three-dimensional structure comparison, and secondary structure element comparisons, detailed overview
additional information
-
the enzyme structure has a distinct domain architecture 4 without a cystathionine-beta-synthase domain (cystathionine-beta-synthetase domain), unlike domain architecture 3. The arginine essential for catalysis, that is present in antifreeze-like domain (block X), is not fully conserved in NeuB, but is replaced by a serine in domain architectures 3 and 4, three-dimensional structure comparison, and secondary structure element comparisons, detailed overview
additional information
-
the enzyme structure has a distinct domain architecture 4 without a cystathionine-beta-synthase domain (cystathionine-beta-synthetase domain), unlike domain architecture 3. The arginine essential for catalysis, that is present in antifreeze-like domain (block X), is not fully conserved in NeuB, but is replaced by a serine in domain architectures 3 and 4, three-dimensional structure comparison, and secondary structure element comparisons, detailed overview
-
additional information
structure comparisons
additional information
-
structure comparisons
additional information
the enzyme contains an antifreeze protein like (AFPL) domain, which extends from the C-terminal of the (beta/alpha)8 barrel containing the active site and contributes a highly conserved arginine, Arg314, into the active site of the opposing monomer chain
additional information
-
the enzyme contains an antifreeze protein like (AFPL) domain, which extends from the C-terminal of the (beta/alpha)8 barrel containing the active site and contributes a highly conserved arginine, Arg314, into the active site of the opposing monomer chain
additional information
-
the enzyme contains an antifreeze protein like (AFPL) domain, which extends from the C-terminal of the (beta/alpha)8 barrel containing the active site and contributes a highly conserved arginine, Arg314, into the active site of the opposing monomer chain
-
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Masson, L.; Holbein, B.E.
Physiology of sialic acid capsular polysaccharide synthesis in serogroup B Neisseria meningitidis
J. Bacteriol.
154
728-736
1983
Neisseria meningitidis, Neisseria meningitidis PRM102
brenda
Blacklow, R.S.; Warren, L.
Biosynthesis of sialic acids by Neisseria meningitidis
J. Biol. Chem.
237
3520-3526
1962
Neisseria meningitidis
brenda
Brossmer, R.; Rose, U.
Enzymic synthesis of 5-acetamido-9-azido-3,5,9-trideoxy-D-glycero-D-galacto-2-nonulosonic acid, a 9-azido-9-deoxy derivative of N-acetylneuraminic acid
Biochem. Biophys. Res. Commun.
96
1282-1289
1980
Neisseria meningitidis, Neisseria meningitidis 60E
brenda
Vann, W.F.; Tavarez, J.J.; Crowley, J.; Vimr, E.; Silver, R.P.
Purification and characterization of the Escherichia coli K1 neuB gene product N-acetylneuraminic acid synthetase
Glycobiology
7
697-701
1997
Escherichia coli, Escherichia coli K1
brenda
Komaki, E.; Ohta, Y.; Tsukada, Y.
Purification and characterization of N-acetylneuraminate synthase from Escherichia coli K1-M12
Biosci. Biotechnol. Biochem.
61
2046-2050
1997
Escherichia coli, Escherichia coli K1-M12
brenda
Tabata, K.; Koizumi, S.; Endo, T.; Ozaki, A.
Production of N-acetyl-D-neuraminic acid by coupling bacteria expressing N-acetyl-D-glucosamine 2-epimerase and N-acetyl-D-neuraminic acid synthetase
Enzyme Microb. Technol.
30
327-333
2002
Escherichia coli
-
brenda
Hwang, T.S.; Hung, C.H.; Teo, C.F.; Chen, G.T.; Chang, L.S.; Chen, S.F.; Chen, Y.J.; Lin, C.H.
Structural characterization of Escherichia coli sialic acid synthase
Biochem. Biophys. Res. Commun.
295
167-173
2002
Escherichia coli
brenda
Linton, D.; Karlyshev, A.V.; Hitchen, P.G.; Morris, H.R.; Dell, A.; Gregson, N.A.; Wren, B.W.
Multiple N-acetyl neuraminic acid synthetase (neuB) genes in Campylobacter jejuni: identification and characterization of the gene involved in sialylation of lipo-oligosaccharide
Mol. Microbiol.
35
1120-1134
2000
Campylobacter jejuni, Campylobacter jejuni NCTC
brenda
Suryanti, V.; Nelson, A.; Berry, A.
Cloning, over-expression, purification, and characterization of N-acetylneuraminate synthase from Streptococcus agalactiae
Protein Expr. Purif.
27
346-356
2003
Streptococcus agalactiae
brenda
Sundaram, A.K.; Pitts, L.; Muhammad, K.; Wu, J.; Betenbaugh, M.; Woodard, R.W.; Vann, W.F.
Characterization of N-acetylneuraminic acid synthase isoenzyme 1 from Campylobacter jejuni
Biochem. J.
383
83-89
2004
Campylobacter jejuni
brenda
Huang, H.H.; Liao, H.K.; Chen, Y.J.; Hwang, T.S.; Lin, Y.H.; Lin, C.H.
Structural characterization of sialic acid synthase by electrospray mass spectrometry--a tetrameric enzyme composed of dimeric dimers
J. Am. Soc. Mass Spectrom.
16
324-332
2005
Escherichia coli, Streptococcus agalactiae
brenda
Gunawan, J.; Simard, D.; Gilbert, M.; Lovering, A.L.; Wakarchuk, W.W.; Tanner, M.E.; Strynadka, N.C.
Structural and mechanistic analysis of sialic acid synthase NeuB from Neisseria meningitidis in complex with Mn2+, phosphoenolpyruvate, and N-acetylmannosaminitol
J. Biol. Chem.
280
3555-3563
2005
Neisseria meningitidis
brenda
Hao, J.; Balagurumoorthy, P.; Sarilla, S.; Sundaramoorthy, M.
Cloning, expression, and characterization of sialic acid synthases
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Neisseria meningitidis
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Fierfort, N.; Samain, E.
Genetic engineering of Escherichia coli for the economical production of sialylated oligosaccharides
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Campylobacter jejuni (Q93MP9)
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Liu, F.; Lee, H.J.; Strynadka, N.C.; Tanner, M.E.
Inhibition of Neisseria meningitidis sialic acid synthase by a tetrahedral intermediate analogue
Biochemistry
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2009
Neisseria meningitidis (E0NCD4), Neisseria meningitidis
brenda
Ishikawa, M.; Koizumi, S.
Microbial production of N-acetylneuraminic acid by genetically engineered Escherichia coli
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Escherichia coli
brenda
Joseph, D.D.; Jiao, W.; Parker, E.J.
Arg314 is essential for catalysis by N-acetyl neuraminic acid synthase from Neisseria meningitidis
Biochemistry
52
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2013
Neisseria meningitidis (H2VFG5), Neisseria meningitidis, Neisseria meningitidis MC58 (H2VFG5)
brenda
Berg, T.O.; Gurung, M.K.; Altermark, B.; Smalas, A.O.; Raeder, I.L.
Characterization of the N-acetylneuraminic acid synthase (NeuB) from the psychrophilic fish pathogen Moritella viscosa
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Moritella viscosa (A0A090IMH4), Moritella viscosa
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Garcia Garcia, M.I.; Lau, K.; von Itzstein, M.; Garcia Carmona, F.; Sanchez Ferrer, A.
Molecular characterization of a new N-acetylneuraminate synthase (NeuB1) from Idiomarina loihiensis
Glycobiology
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2015
Idiomarina loihiensis (Q5R082), Idiomarina loihiensis, Idiomarina loihiensis L2-TR (Q5R082)
brenda
van Karnebeek, C.D.; Bonafe, L.; Wen, X.Y.; Tarailo-Graovac, M.; Balzano, S.; Royer-Bertrand, B.; Ashikov, A.; Garavelli, L.; Mammi, I.; Turolla, L.; Breen, C.; Donnai, D.; Cormier, V.; Heron, D.; Nishimura, G.; Uchikawa, S.; Campos-Xavier, B.; Rossi, A.; Hennet, T.; Brand-Arzamendi, K.; Rozmus, J.
NANS-mediated synthesis of sialic acid is required for brain and skeletal development
Nat. Genet.
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Danio rerio (Q6P0K4), Homo sapiens (Q9NR45)
brenda
Joseph, D.D.; Jiao, W.; Kessans, S.A.; Parker, E.J.
Substrate-mediated control of the conformation of an ancillary domain delivers a competent catalytic site for N-acetylneuraminic acid synthase
Proteins
82
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2014
Neisseria meningitidis (H2VFG5), Neisseria meningitidis, Neisseria meningitidis MC58 (H2VFG5)
brenda
Zhao, L.; Tian, R.; Shen, Q.; Liu, Y.; Liu, L.; Li, J.; Du, G.
Pathway engineering of Bacillus subtilis for enhanced N-acetylneuraminic acid production via whole-cell biocatalysis
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2019
Staphylococcus hominis
brenda
Yang, P.; Wang, J.; Pang, Q.; Zhang, F.; Wang, J.; Wang, Q.; Qi, Q.
Pathway optimization and key enzyme evolution of N-acetylneuraminate biosynthesis using an in vivo aptazyme-based biosensor
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Escherichia coli, Escherichia coli K1
brenda
Alwassil, O.; Chandrashekharappa, S.; Nayak, S.; Venugopala, K.
Design, synthesis, and structural elucidation of novel NmeNANAS inhibitors for the treatment of meningococcal infection
PLoS ONE
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2019
Neisseria meningitidis
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