BRENDA - Enzyme Database
show all sequences of 2.5.1.101

Biosynthesis of CMP-N,N-diacetyllegionaminic acid from UDP-N,N-diacetylbacillosamine in Legionella pneumophila

Glaze, P.A.; Watson, D.C.; Young, N.M.; Tanner, M.E.; Biochemistry 47, 3272-3282 (2008) View publication on PubMed

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
gene lpg0752 or neuB, DNA and amino acid sequence determination and analysis, overexpression of the inactive C- and N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3), functional expression as MalE-NeuB fusion protein
Legionella pneumophila
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
additional information
the synthase activity is dependent on the presence of a divalent metal ion
Legionella pneumophila
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + phosphoenolpyruvate + H2O
Legionella pneumophila
-
N,N'-diacetyllegionaminate + phosphate
-
-
?
2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + phosphoenolpyruvate + H2O
Legionella pneumophila ATCC 33152D
-
N,N'-diacetyllegionaminate + phosphate
-
-
?
additional information
Legionella pneumophila
the enzyme condenses 2,4-diacetamido-2,4,6-trideoxymannose with phosphoenolpyruvate, the reaction proceeded via a C-O bond cleavage process
?
-
-
?
additional information
Legionella pneumophila ATCC 33152D
the enzyme condenses 2,4-diacetamido-2,4,6-trideoxymannose with phosphoenolpyruvate, the reaction proceeded via a C-O bond cleavage process
?
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Legionella pneumophila
-
subsp. pneumophila, gene lpg0752 or neuB homologue, clustered with the neuC and neuA homologues
-
Legionella pneumophila ATCC 33152D
-
subsp. pneumophila, gene lpg0752 or neuB homologue, clustered with the neuC and neuA homologues
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant C- and N-terminally and inactive His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal chelating chromatography, recombinant active MalE-NeuB fusion protein by amylose affinity chromatography to high yields, the MalE protein is removed by thrombin treatment
Legionella pneumophila
Reaction
Reaction
Commentary
Organism
Reaction ID
2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + phosphoenolpyruvate + H2O = N,N'-diacetyllegionaminate + phosphate
C-O bond cleavage process reaction via a oxocarbenium ion intermediate generated by an initial attack of C-3 of phosphoenolpyruvate on the aldehyde of 2,4-diacetamido-2,4,6-trideoxymannose. This attack is facilitated by the divalent cation that serves as an electrophilic catalyst and polarizes the carbonyl of the aldehyde. Water then adds to the oxocarbenium ion intermediate to give a tetrahedral intermediate that subsequently collapses to generate phosphate and the product 2-oxo acid, overview
Legionella pneumophila
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + phosphoenolpyruvate + H2O
-
718850
Legionella pneumophila
N,N'-diacetyllegionaminate + phosphate
-
-
-
?
2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + phosphoenolpyruvate + H2O
-
718850
Legionella pneumophila
N,N'-diacetyllegionaminate + phosphate
NMR spectroscopic product identification
-
-
?
2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + phosphoenolpyruvate + H2O
-
718850
Legionella pneumophila ATCC 33152D
N,N'-diacetyllegionaminate + phosphate
-
-
-
?
2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + phosphoenolpyruvate + H2O
-
718850
Legionella pneumophila ATCC 33152D
N,N'-diacetyllegionaminate + phosphate
NMR spectroscopic product identification
-
-
?
additional information
the enzyme condenses 2,4-diacetamido-2,4,6-trideoxymannose with phosphoenolpyruvate, the reaction proceeded via a C-O bond cleavage process
718850
Legionella pneumophila
?
-
-
-
?
additional information
the enzyme does not show measurable activity with ManNAc
718850
Legionella pneumophila
?
-
-
-
?
additional information
the enzyme condenses 2,4-diacetamido-2,4,6-trideoxymannose with phosphoenolpyruvate, the reaction proceeded via a C-O bond cleavage process
718850
Legionella pneumophila ATCC 33152D
?
-
-
-
?
additional information
the enzyme does not show measurable activity with ManNAc
718850
Legionella pneumophila ATCC 33152D
?
-
-
-
?
Synonyms
Synonyms
Commentary
Organism
N,N'-diacetyllegionaminic acid synthase
-
Legionella pneumophila
NeuB
-
Legionella pneumophila
NeuB homologue
-
Legionella pneumophila
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Legionella pneumophila
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.4
-
assay at
Legionella pneumophila
Cloned(Commentary) (protein specific)
Commentary
Organism
gene lpg0752 or neuB, DNA and amino acid sequence determination and analysis, overexpression of the inactive C- and N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3), functional expression as MalE-NeuB fusion protein
Legionella pneumophila
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
additional information
the synthase activity is dependent on the presence of a divalent metal ion
Legionella pneumophila
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + phosphoenolpyruvate + H2O
Legionella pneumophila
-
N,N'-diacetyllegionaminate + phosphate
-
-
?
2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + phosphoenolpyruvate + H2O
Legionella pneumophila ATCC 33152D
-
N,N'-diacetyllegionaminate + phosphate
-
-
?
additional information
Legionella pneumophila
the enzyme condenses 2,4-diacetamido-2,4,6-trideoxymannose with phosphoenolpyruvate, the reaction proceeded via a C-O bond cleavage process
?
-
-
?
additional information
Legionella pneumophila ATCC 33152D
the enzyme condenses 2,4-diacetamido-2,4,6-trideoxymannose with phosphoenolpyruvate, the reaction proceeded via a C-O bond cleavage process
?
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant C- and N-terminally and inactive His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal chelating chromatography, recombinant active MalE-NeuB fusion protein by amylose affinity chromatography to high yields, the MalE protein is removed by thrombin treatment
Legionella pneumophila
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + phosphoenolpyruvate + H2O
-
718850
Legionella pneumophila
N,N'-diacetyllegionaminate + phosphate
-
-
-
?
2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + phosphoenolpyruvate + H2O
-
718850
Legionella pneumophila
N,N'-diacetyllegionaminate + phosphate
NMR spectroscopic product identification
-
-
?
2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + phosphoenolpyruvate + H2O
-
718850
Legionella pneumophila ATCC 33152D
N,N'-diacetyllegionaminate + phosphate
-
-
-
?
2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + phosphoenolpyruvate + H2O
-
718850
Legionella pneumophila ATCC 33152D
N,N'-diacetyllegionaminate + phosphate
NMR spectroscopic product identification
-
-
?
additional information
the enzyme condenses 2,4-diacetamido-2,4,6-trideoxymannose with phosphoenolpyruvate, the reaction proceeded via a C-O bond cleavage process
718850
Legionella pneumophila
?
-
-
-
?
additional information
the enzyme does not show measurable activity with ManNAc
718850
Legionella pneumophila
?
-
-
-
?
additional information
the enzyme condenses 2,4-diacetamido-2,4,6-trideoxymannose with phosphoenolpyruvate, the reaction proceeded via a C-O bond cleavage process
718850
Legionella pneumophila ATCC 33152D
?
-
-
-
?
additional information
the enzyme does not show measurable activity with ManNAc
718850
Legionella pneumophila ATCC 33152D
?
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Legionella pneumophila
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.4
-
assay at
Legionella pneumophila
General Information
General Information
Commentary
Organism
evolution
the gene encoding the enzyme shows homology to known sialic acid biosynthetic gene neuB
Legionella pneumophila
metabolism
the three enzymes, UDP-N,N'-diacetylbacillosamine 2-epimerase, N,N'-diacetyllegionaminic acid synthase, and CMP-N,N'-diacetyllegionaminic acid synthetase, constitute a pathway that converts a UDP-linked bacillosamine derivative into a CMP-linked legionaminic acid derivative, the activated form of legionaminic acid used in lipopolysaccharide biosynthesis, overview
Legionella pneumophila
General Information (protein specific)
General Information
Commentary
Organism
evolution
the gene encoding the enzyme shows homology to known sialic acid biosynthetic gene neuB
Legionella pneumophila
metabolism
the three enzymes, UDP-N,N'-diacetylbacillosamine 2-epimerase, N,N'-diacetyllegionaminic acid synthase, and CMP-N,N'-diacetyllegionaminic acid synthetase, constitute a pathway that converts a UDP-linked bacillosamine derivative into a CMP-linked legionaminic acid derivative, the activated form of legionaminic acid used in lipopolysaccharide biosynthesis, overview
Legionella pneumophila
Other publictions for EC 2.5.1.101
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
719563
Schoenhofen
The CMP-legionaminic acid path ...
Campylobacter jejuni, Campylobacter jejuni 11168
Glycobiology
19
715-725
2009
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1
-
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-
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2
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5
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1
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2
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1
1
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1
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1
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2
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1
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1
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1
1
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718850
Glaze
Biosynthesis of CMP-N,N-diacet ...
Legionella pneumophila, Legionella pneumophila ATCC 33152D
Biochemistry
47
3272-3282
2008
-
-
1
-
-
-
-
-
-
1
-
4
-
4
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1
1
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8
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3
1
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1
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1
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1
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4
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1
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8
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1
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1
-
-
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2
2
-
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718948
Knirel
Identification of a homopolyme ...
Legionella pneumophila
Biochemistry
66
1035-1041
2001
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1
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1
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1
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1
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1
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1
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1
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2
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1
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1
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2
2
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