2.5.1.56: N-acetylneuraminate synthase
This is an abbreviated version!
For detailed information about N-acetylneuraminate synthase, go to the full flat file.
Word Map on EC 2.5.1.56
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2.5.1.56
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n-acetylmannosamine
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antifreeze
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mannac
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meningitidis
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polysialic
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neunacs
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neuroinvasive
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synthesis
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cmp-sialic
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2-epimerase
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ice-binding
- 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
Reaction
Synonyms
(NANA) condensing enzyme, EC 4.1.3.19, N-acetylneuraminate lyase synthase, N-acetylneuraminate pyruvate-lyase (pyruvate-phosphorylating), N-acetylneuraminic acid condensing enzyme, N-acetylneuraminic acid synthase, NANA condensing enzyme, NANA synthase, NANAS, NANS, NeuAc synthase, NeuB, NeuB1, NeuNAc synthase, NmeNANAS, sialic acid synthase, synthase, N-acetylneuraminate
ECTree
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Substrates Products
Substrates Products on EC 2.5.1.56 - N-acetylneuraminate synthase
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REACTION DIAGRAM
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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?
phosphoenolpyruvate + N-propanoyl-D-mannosamine + H2O
phosphate + N-propanoylneuraminate
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-
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?
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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?
?
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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-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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?
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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?
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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ir
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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?
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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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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?