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Literature summary for 1.14.18.2 extracted from

  • Schlenzka, W.; Shaw, L.; Schneckenburger, P.; Schauer, R.
    Purification and characterization of CMP-N-acetylneuraminic acid hydroxylase from pig submandibular glands (1994), Glycobiology, 4, 675-683.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline
-
Sus scrofa
ferrozine
-
Sus scrofa
KCN
-
Sus scrofa
Tiron
-
Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.003
-
CMP-N-acetylneuraminate pH 7.4, 37°C, reconstituted system consisting of purified hydroxylase, cytochrome b5, cytochrome b5 reductase and catalase Sus scrofa
0.011
-
CMP-N-acetylneuraminate pH 7.4, 37°C, purified hydroxylase in presence of Triton X-100 solubilized microsomes Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
60000
-
gel filtration Sus scrofa
65000
-
1 * 65000, SDS-PAGE Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
submandibular gland
-
Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.816
-
-
Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CMP-N-acetylneuraminate + NADH + O2
-
Sus scrofa CMP-N-glycoloylneuraminate + NAD+ + H2O
-
?

Subunits

Subunits Comment Organism
monomer 1 * 65000, SDS-PAGE Sus scrofa

Cofactor

Cofactor Comment Organism Structure
NADH
-
Sus scrofa