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Literature summary 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

Localization

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

Organism

EC Number Organism UniProt Comment Textmining
1.14.18.2 Mus musculus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.18.2 liver
-
 Mus musculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.18.2 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
-
 ?
1.14.18.2 CMP-N-acetylneuraminate + NADH + O2
-
 Mus musculus CMP-N-glycoloylneuraminate + NAD+ + H2O
-
 ?
1.14.18.2 CMP-N-acetylneuraminate + NADPH + O2
-
 Mus musculus CMP-N-glycoloylneuraminate + NADP+ + H2O
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.18.2 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
1.14.18.2 NADH NADH is much more effective than NADPH Mus musculus
1.14.18.2 NADPH NADH is much more effective than NADPH Mus musculus