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Literature summary for 1.14.18.2 extracted from

  • Kozutsumi, Y.; Kawano, T.; Yamakawa, T.; Suzuki, A.
    Participation of cytochrome b5 in CMP-N-acetylneuraminic acid hydroxylation in mouse liver cytosol (1990), J. Biochem., 108, 704-706.
    View publication on PubMed
Search for more literature for 1.14.18.2

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Mus musculus 5829
-

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CMP-N-acetylneuraminate + ferrocytochrome b5 + O2 2 electrons are donated by either NADH or NADPH are transported via cytochrome b5 in the CMP-NeuAc hydroxylation system of mouse liver cytosol Mus musculus CMP-N-glycoloylneuraminate + ferricytrochrome b5 + H2O
-
 ?
CMP-N-acetylneuraminate + NADH + O2
-
 Mus musculus CMP-N-glycoloylneuraminate + NAD+ + H2O
-
 ?
CMP-N-acetylneuraminate + NADPH + O2
-
 Mus musculus CMP-N-glycoloylneuraminate + NADP+ + H2O
-
 ?

Cofactor

Cofactor Comment Organism Structure
ferrocytochrome b5 2 electrons are donated by either NADH or NADPH are transported via cytochrome b5 in the CMP-NeuAc hydroxylation system of mouse liver cytosol Mus musculus
NADH NADH is much more effective than NADPH Mus musculus
NADPH NADH is much more effective than NADPH Mus musculus