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Information on EC 2.5.1.56 - N-acetylneuraminate synthase
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EC Tree
2.5.1.56 N-acetylneuraminate synthaseSpecify your search results
Word Map
- 2.5.1.56
- n-acetylmannosamine
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antifreeze
- mannac
- meningitidis
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polysialic
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neunacs
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neuroinvasive
- synthesis
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cmp-sialic
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2-epimerase
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ice-binding
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
sialic acid synthase, neub1, nanas, neuac synthase, neunac synthase, n-acetylneuraminic acid synthase, nmenanas, n-acetylneuraminate synthase, nana synthase, nana condensing enzyme, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(NANA) condensing enzyme
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-
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EC 4.1.3.19
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formerly
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N-acetylneuraminate lyase synthase
N-acetylneuraminate pyruvate-lyase (pyruvate-phosphorylating)
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N-acetylneuraminic acid condensing enzyme
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NANA condensing enzyme
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NANA synthase
NANAS
NANS
NeuAc synthase
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-
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NeuB
NeuB1
NmeNANAS
sialic acid synthase
synthase, N-acetylneuraminate
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O = phosphate + N-acetylneuraminate
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phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O = phosphate + N-acetylneuraminate
mechanism, essential role for divalent metal ion as an electrophilic catalyst that activates the N-acetylmannosamine carbonyl prior to the addition of phosphoenolpyruvate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
condensation
condensation
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-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
phosphoenolpyruvate:N-acetyl-D-mannosamine C-(1-carboxyvinyl)transferase (phosphate-hydrolysing, 2-carboxy-2-oxoethyl-forming)
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CAS REGISTRY NUMBER
COMMENTARY
37290-66-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
?
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15% of the activity with N-acetyl-D-mannosamine
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-
?
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
N-acetylneuraminate + phosphate
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-
-
?
phosphoenolpyruvate + N-butanoyl-D-mannosamine + H2O
phosphate + N-butanoylneuraminate
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-
-
-
?
phosphoenolpyruvate + N-pentanoyl-D-mannosamine + H2O
phosphate + N-pentanoylneuraminate
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-
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?
phosphoenolpyruvate + N-propanoyl-D-mannosamine + H2O
phosphate + N-propanoylneuraminate
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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
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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
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-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
?
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the neuB genes appear to be involved in the biosynthesis of at least two distinct surface structures: lipooligosaccharide and flagella
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?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
?
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the neuB genes appear to be involved in the biosynthesis of at least two distinct surface structures: lipooligosaccharide and flagella
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?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
?
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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
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?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
?
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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
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-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
?
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the enzyme is involved in sialic acid synthesis
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?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
?
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the enzyme is involved in sialic acid synthesis
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?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
?
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the enzyme is involved in sialic acid synthesis
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?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
N-acetylneuraminate + phosphate
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?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
N-acetylneuraminate + phosphate
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-
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
N-acetylneuraminate + phosphate
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-
-
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
N-acetylneuraminate + phosphate
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-
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
N-acetylneuraminate + phosphate
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specific for
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?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
N-acetylneuraminate + phosphate
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specific for
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?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
N-acetylneuraminate + phosphate
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-
-
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
N-acetylneuraminate + phosphate
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-
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-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
N-acetylneuraminate + phosphate
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specific for
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ir
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
N-acetylneuraminate + phosphate
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the reaction strongly favors the formation of N-acetylneuraminic acid and appears to be irreversible
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ir
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
N-acetylneuraminate + phosphate
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-
-
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
N-acetylneuraminate + phosphate
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-
-
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
N-acetylneuraminate + phosphate
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-
-
-
?
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
phosphate + N-acetylneuraminate
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-
-
-
?
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
phosphate + N-acetylneuraminate
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-
-
-
?
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
phosphate + N-acetylneuraminate
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-
-
-
?
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
phosphate + N-acetylneuraminate
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-
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ir
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
phosphate + N-acetylneuraminate
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-
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ir
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
phosphate + N-acetylneuraminate
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-
-
?
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
phosphate + N-acetylneuraminate
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-
-
?
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
phosphate + N-acetylneuraminate
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-
-
-
?
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
phosphate + N-acetylneuraminate
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?
additional information
?
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enzyme catalyzes the condensation of the si face of phosphoenolpyruvate with the aldehyde sugar
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?
additional information
?
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the enzyme shows activity towards 2-acetamido-4-O-acetyl-2-deoxy-D-mannopyranose resulting in formation of 4-O-acetyl-ManNAc
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?
additional information
?
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the enzyme shows activity towards 2-acetamido-4-O-acetyl-2-deoxy-D-mannopyranose resulting in formation of 4-O-acetyl-ManNAc
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?
additional information
?
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the enzyme shows activity towards 2-acetamido-4-O-acetyl-2-deoxy-D-mannopyranose resulting in formation of 4-O-acetyl-ManNAc
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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arginine residues are present in the active site and are involved in substrate recognition and binding
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
N-acetylneuraminate + phosphate
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?
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
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-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
?
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the enzyme is involved in sialic acid synthesis
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-
?
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
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-
-
ir
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O
phosphate + N-acetylneuraminate
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-
-
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
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mn2+
Co2+
activates and stabilizes at low and inhibits at higher concentrations
Co2+
-
1 mM stimulates around 2fold, the enzyme is dependent on the presence of metal ions such as Mg2+, Mn2+ or Co2+
Mg2+
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the enzyme is dependent on the presence of metal ions such as Mg2+, Mn2+ or Co2+
Mn2+
required, increases the enzyme stability, binding of Mn2+ is associated with a change in the average conformation of enzyme NmeNANAS
Mn2+
-
1 mM stimulates around 2fold, the enzyme is dependent on the presence of metal ions such as Mg2+, Mn2+ or Co2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-(carboxyamino)-3,5-dideoxy-2-O-phosphono-D-erythro-L-manno-nononic acid
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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
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
additional information
no or poor effect by Mg2+ and Ca2+ at 1 mM
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Cloning and expression of the human N-acetylneuraminic acid phosphate synthase gene with 2-keto-3-deoxy-D-glycero- D-galacto-nononic acid biosynthetic ability.
Intellectual Disability
The fate of orally administered sialic acid: First insights from patients with N-acetylneuraminic acid synthase deficiency and control subjects.
Meningococcal Infections
Design, synthesis, and structural elucidation of novel NmeNANAS inhibitors for the treatment of meningococcal infection.
n-acetylneuraminate synthase deficiency
The fate of orally administered sialic acid: First insights from patients with N-acetylneuraminic acid synthase deficiency and control subjects.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11.6
N-acetyl-D-mannosamine
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the reaction mixture contains 1 mM MgCl2 in 50 mM Tris-acetate buffer, pH 7.5, at 37°C
0.157
phosphoenolpyruvate
37°C, 100 mM Tris-HCl buffer, pH 7.0, 1 mM MnCl2, 50 microM to 1 mM phosphoenolpyruvate, His-tagged enzyme, purine nucleoside phosphorylase, 200 mircoM 2-amino-6-mercapto-7-methylpurine ribonucleoside
additional information
additional information
-
coupled assay to monitor enzyme kinetics
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additional information
additional information
Michaelis-Menten kinetics, overview
-
additional information
additional information
-
Michaelis-Menten kinetics, overview
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additional information
additional information
kinetic analysis of wild-ype and mutant enzymes, no kinetic activity can be observed for mutant G272Term with phosphoenolpyruvate, binding constants for wild-type, overview
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additional information
additional information
-
kinetic analysis of wild-ype and mutant enzymes, no kinetic activity can be observed for mutant G272Term with phosphoenolpyruvate, binding constants for wild-type, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.83
N-acetyl-D-mannosamine
-
the reaction mixture contains 1 mM MgCl2 in 50 mM Tris-acetate buffer, pH 7.5, at 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0031
5-acetamido-4,6,7,8,9-pentahydroxy-2-phosphorylnonanoic acid ditriethylammonium salt
4.5/1 mixture of 2S-inhibitor/2R-inhibitor, a 1.2/1 mixture of 2S-inhibitor/2R-inhibitor requires a 2.5-fold lower total inhibitor concentration, 37°C, 100 mM Tris-HCl buffer, pH 7.0, 1 mM MnCl2, 50 microM to 1 mM phosphoenolpyruvate, His-tagged enzyme, purine nucleoside phosphorylase, 200 mircoM 2-amino-6-mercapto-7-methylpurine ribonucleoside
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 12
-
pH 4.0: about 50% of maximal activity, pH 12.0: about 40% of maximal activity
6.5 - 10
-
pH 6.5: about 40% of maximal activity, pH 10.0: about 60% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 50
the relative enzyme activity is approximately 20% at 5°C, and increasing to a maximum at around 30°C, and decreases rapidly above 30°C, no activity remains at 55°C. The enzyme from a psychrophilic bacterium, MvNeuB, is less stable at higher temperature and has a high catalytic activity at lower temperature compared to mesophilic counterparts. MvNeuB is a typical cold adapted enzyme
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE