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: Oncorhynchus mykiss

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
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
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
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the enzyme participates in the biosynthesis of the sialic acid 3-deoxy-D-glycero-D-galacto-nononate
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?
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
3.66
D-mannose 6-phosphate
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pH 7.0, 25°C
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
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE