Information on EC 2.5.1.132 - 3-deoxy-D-glycero-D-galacto-nononate 9-phosphate synthase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
2.5.1.132
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RECOMMENDED NAME
GeneOntology No.
3-deoxy-D-glycero-D-galacto-nononate 9-phosphate synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
phosphoenolpyruvate + D-mannose 6-phosphate + H2O = 3-deoxy-D-glycero-D-galacto-nononate 9-phosphate + phosphate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
CMP-2-keto-3-deoxy-D-glycero-D-galacto-nononate biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
phosphoenolpyruvate:D-mannose-6-phosphate 1-(2-carboxy-2-oxoethyl)transferase
The enzyme participates in the biosynthesis of the sialic acid 3-deoxy-D-glycero-D-galacto-nononate (KDN). The human sialic acid synthase (EC 2.5.1.57) is also able to catalyse the reaction. KDN is abundant in extracellular glycoconjugates of lower vertebrates such as fish and amphibians, but is also found in the capsular polysaccharides of bacteria that belong to the Bacteroides genus.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
phosphoenolpyruvate + D-mannose 6-phosphate + H2O
3-deoxy-D-glycero-D-galacto-nononate 9-phosphate + phosphate
show the reaction diagram
phosphoenolpyruvate + N-acetyl-D-mannose 6-phosphate + H2O
? + phosphate
show the reaction diagram
the enzyme prefers N-acetyl-D-mannose 6-phosphate over D-mannose 6-phosphate in the production of phosphorylated forms of N-acetylneuraminic acid and 2-dehydro-3-deoxy-D-glycero-D-galacto-nononic acid
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-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
phosphoenolpyruvate + D-mannose 6-phosphate + H2O
3-deoxy-D-glycero-D-galacto-nononate 9-phosphate + phosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
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maximal activity in presence of Mn2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
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the enzyme is active in the absence of exogenously added divalent cations but lost all activity when incubated before assay with 5 mM EDTA. The lost enzyme activity is restored to 2.4–3 times higher levels of the original one by the addition of 1 mM MnCl2, CoCl2, or NiCl2 and to one-third the original activity by 1 mM MgCl2. The other cations (Ca2+, Fe2+, Cu2+, and Zn2+) do not restore enzyme activity
NaCl
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activity is reduced by about 50% in the presence of 150 mM NaCl compared with the activity without added NaCl
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.4 - 5
D-mannose 6-phosphate
0.11
phosphoenolpyruvate
pH 7.5, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0011 - 0.017
D-mannose 6-phosphate
0.017
phosphoenolpyruvate
Bacteroides thetaiotaomicron
Q8A711
pH 7.5, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000327 - 0.012
D-mannose 6-phosphate
700
0.15
phosphoenolpyruvate
Bacteroides thetaiotaomicron
Q8A711
pH 7.5, 25°C
51
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0009
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pH 7.0, 25°C, the 50fold purified enzyme from testis is unstable, preventing further purification of this enzyme activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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specific activity is 33fold lower than in testis
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 40308, calculated from sequence
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
glutathione agarose column chromatography
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nickel affinity column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) Gold cells
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expressed in Escherichia coli BL21-AI cells
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the gene partially restores sialic acid synthase activity in a neuB-negative mutant of Escherichia coli and results in N-acetylneuraminic acid (Neu5Ac) and 2-dehydro-3-deoxy-D-glycero-D-galacto-nononic acid production in insect cells upon recombinant baculovirus infection
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
M42L
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the M42L mutant of N-acetylneuraminic acid-9-phosphate synthase, like the wild type enzyme, shows the additional 2-keto-3-deoxy-D-glycero-D-galacto-nonulosonic acid-9-phosphate synthase activity
M42T
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the mutation of N-acetylneuraminic acid-9-phosphate synthase abolishes its 2-keto-3-deoxy-D-glycero-D-galacto-nonulosonic acid-9-phosphate synthase activity
R96K/R100S/E103Q/V105I/V195A
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the mutant of N-acetylneuraminic acid-9-phosphate synthase has significant 2-keto-3-deoxy-D-glycero-D-galacto-nonulosonic acid-9-phosphate synthase activity
additional information
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replacement of the antifreeze-like domain of human N-acetylneuraminic acid phosphate synthase with the mouse antifreeze-like domain impacts both N-acetylneuraminic acid 9-phosphate synthase and 2-keto-3-deoxy-D-glycero-D-galacto-nonulosonic acid 9-phosphate synthase activities