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Literature summary for 1.14.18.2 extracted from

  • Schneckenburger, P.; Shaw, L.; Schauer, R.
    Purification, characterization and reconstitution of CMP-N-acetylneuraminate hydroxylase from mouse liver (1994), Glycoconjugate J., 11, 194-203.
    View publication on PubMed
Search for more literature for 1.14.18.2

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.005
-
 CMP-N-acetylneuraminate pH 7.4, 37°C, amphiphilic system Mus musculus
0.013
-
 CMP-N-acetylneuraminate pH 7.4, 37°C, soluble system Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
 Mus musculus
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
58000
-
 gel filtration Mus musculus
64000
-
 1 * 64000, SDS-PAGE Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
CMP-N-acetylneuraminate + NADH + O2 Mus musculus a regulation of CMP-N-acetylneuraminate hydroxylation and thus the ratio of glycoconjugate-bound N-acetylneuraminate and N-acetylglycoloylneuraminate might occur by varying the amount of hydroxylase protein within the cell, possibly by controlling the expression of the hydroxylase gene CMP-N-glycoloylneuraminate + NAD+ + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Mus musculus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.126
-
-
 Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CMP-N-acetylneuraminate + ferrocytochrome b5 + O2
-
 Mus musculus CMP-N-glycoloylneuraminate + ferricytrochrome b5 + H2O
-
 ?
CMP-N-acetylneuraminate + NADH + O2
-
 Mus musculus CMP-N-glycoloylneuraminate + NAD+ + H2O
-
 ?
CMP-N-acetylneuraminate + NADH + O2 a regulation of CMP-N-acetylneuraminate hydroxylation and thus the ratio of glycoconjugate-bound N-acetylneuraminate and N-acetylglycoloylneuraminate might occur by varying the amount of hydroxylase protein within the cell, possibly by controlling the expression of the hydroxylase gene Mus musculus CMP-N-glycoloylneuraminate + NAD+ + H2O
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 64000, SDS-PAGE Mus musculus

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Mus musculus