Information on EC 3.1.4.40 - CMP-N-acylneuraminate phosphodiesterase

for references in articles please use BRENDA:EC3.1.4.40
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.1.4.40
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RECOMMENDED NAME
GeneOntology No.
CMP-N-acylneuraminate phosphodiesterase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
CMP-N-acylneuraminate + H2O = CMP + N-acylneuraminate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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SYSTEMATIC NAME
IUBMB Comments
CMP-N-acylneuraminate N-acylneuraminohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
55326-41-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
calf
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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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
CMP-N-acylneuraminate + H2O
?
show the reaction diagram
CMP-N-acylneuraminate + H2O
CMP + N-acylneuraminate
show the reaction diagram
deoxythymidine-5'-p-nitrophenyl phosphate + H2O
deoxythymidine + 4-nitrophenol
show the reaction diagram
UDP-galactose + H2O
UDP + D-galactose
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
CMP-N-acylneuraminate + H2O
?
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Divalent cations
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required, monovalent metal ions without or little stimulatory effect
Mn2+
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increased activity at higher concentrations
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
5,5'-dithiobis(2-nitrobenzoic acid)
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16.3% inhibition at 25 mM
cAMP
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19% inhibition at 0.86 mM
carrageen
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reduced activity of the enzyme after 8 h and 3 days after injection, mostly normal by 7 days
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CDP
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64% inhibition at 0.86 mM
CTP
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84% inhibition at 0.86 mM
Cu2+
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38% reduction of enzyme activity at 10 mM
cysteine
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80% inhibition at 25 mM
cytidine
diphosphate
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41% inhibition at 0.86 mM, 82% inhibition at 6.5
dithiothreitol
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84% inhibition by 25 mM reduced dithiothreitol, 0% inhibition by 25 mM oxidized dithiotreitol
GDPglucose
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competitive, 83% inhibition
GDPmannose
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competitive, 85% inhibition
glutathione
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62% inhibition by 25 mM reduced glutathione, 15% inhibition by 25 mM oxidized glutathione
Mn2+
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slight inhibition at lower concentrations
N-ethylmaleimide
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5.8% inhibition at 25 mM
N-methyl-nitro-N-nitrosugoanidine
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carcinogen, induces gastric tumors, reduces enzyme activity
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p-chloromercuribenzoate
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7.2% inhibition at 25 mM
TDPglucose
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competitive, 70% inhibition
Trypsin
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UDP
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76% inhibition at 0.86 mM
UDP-N-acetylglucosamine
UDPgalactose
UDPgalacturonic acid
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competitive, 79% inhibition
UDPglucose
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competitive, 70% inhibition
UDPglucuronic acid
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competitive, 76% inhibition
UDPmannose
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competitive, 61% inhibition
Urate
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reduced activity of the enzyme after 8 h and 3 days after injection, mostly normal by 7 days
uridine
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7.5% inhibition at 0.86 mM
UTP
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83% inhibition at 0.86 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Alkaline phosphatase
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stimulation
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azoxymethane
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carcinogen, elevated enzyme activity in tumour cells
Triton X-100
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increase of enzyme activity
UMP
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slight stimulation at 0.4-1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00088 - 0.6
CMP-N-acylneuraminate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2
EDTA
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.8 - 9
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9
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in Tris-HCl buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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from skin of normal individuals and patients with salla disease
Manually annotated by BRENDA team
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skeletal
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 1 mM Tris-HCl buffer, pH 8, membrane preparations
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-20°C, for at least 5 months, no loss of activity
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-20°C, plasma membranes, 1 year, microsomes, 3 months, no loss of activity
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0-4°C, different sucrose concentrations, for several days, no inactivation
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0-4°C, for at several days, no loss of activity
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0°C, for several days no loss of activity, by the 25th day 42% of initial activity remains
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repeated freezing and thawing, no influence of enzyme activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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