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Literature summary extracted from

  • Takematsu, H.; Kawano, T.; Koyama, S.; Kozutsumi, Y.; Suzuki, A.; Kawasaki, T.
    Reaction mechanism underlying CMP-N-acetylneuraminic acid hydroxylation in mouse liver: formation of a ternary complex of cytochrome b5, CMP-N-acetylneuraminic acid, and a hydroxylation enzyme (1994), J. Biochem., 115, 381-386.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.18.2 CMP-N-acetylneuraminate + NADH + O2 Mus musculus binding of CMP-N-acetylneuraminate to CMP-N-acetylneuraminate hydroxylase changes conformation of the enzyme so as to construct a recognition site for cytochrome b5, followed by the formation of a ternary complex through this domain. Then the transport of electrons from NAD(P)H to the enzyme through cytochrome b5 takes place, CMP-N-acetylneuraminate is converted to CMP-N-glycoloylneuraminic acid and finally the ternary complex dissociates into its components to release CMP-N-glycoloylneuraminic acid CMP-N-glycoloylneuraminate + NAD+ + H2O
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 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.18.2 Mus musculus
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Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.18.2 liver
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 Mus musculus
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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 binding of CMP-N-acetylneuraminate to CMP-N-acetylneuraminate hydroxylase changes conformation of the enzyme so as to construct a recognition site for cytochrome b5, followed by the formation of a ternary complex through this domain. Then the transport of electrons from NAD(P)H to the enzyme through cytochrome b5 takes place, CMP-N-acetylneuraminate is converted to CMP-N-glycoloylneuraminic acid and finally the ternary complex dissociates into its components to release CMP-N-glycoloylneuraminic acid Mus musculus CMP-N-glycoloylneuraminate + ferricytrochrome b5 + H2O
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 ?
1.14.18.2 CMP-N-acetylneuraminate + NADH + O2 binding of CMP-N-acetylneuraminate to CMP-N-acetylneuraminate hydroxylase changes conformation of the enzyme so as to construct a recognition site for cytochrome b5, followed by the formation of a ternary complex through this domain. Then the transport of electrons from NAD(P)H to the enzyme through cytochrome b5 takes place, CMP-N-acetylneuraminate is converted to CMP-N-glycoloylneuraminic acid and finally the ternary complex dissociates into its components to release CMP-N-glycoloylneuraminic acid Mus musculus CMP-N-glycoloylneuraminate + NAD+ + H2O
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 ?
1.14.18.2 CMP-N-acetylneuraminate + NADPH + O2 binding of CMP-N-acetylneuraminate to CMP-N-acetylneuraminate hydroxylase changes conformation of the enzyme so as to construct a recognition site for cytochrome b5, followed by the formation of a ternary complex through this domain. Then the transport of electrons from NAD(P)H to the enzyme through cytochrome b5 takes place, CMP-N-acetylneuraminate is converted to CMP-N-glycoloylneuraminic acid and finally the ternary complex dissociates into its components to release CMP-N-glycoloylneuraminic acid Mus musculus CMP-N-glycoloylneuraminate + NADP+ + H2O
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 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.18.2 ferrocytochrome b5 binding of CMP-N-acetylneuraminate to CMP-N-acetylneuraminate hydroxylase changes conformation of the enzyme so as to construct a recognition site for cytochrome b5, followed by the formation of a ternary complex through this domain. Then the transport of electrons from NAD(P)H to the enzyme through cytochrome b5 takes place, CMP-N-acetylneuraminate is converted to CMP-N-glycoloylneuraminic acid and finally the ternary complex dissociates into its components to release CMP-N-glycoloylneuraminic acid Mus musculus