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Kjell Wikvall - One of the best experts on this subject based on the ideXlab platform.

  • sterol 27 hydroxylase in bile acid biosynthesis mechanism of oxidation of 5 beta Cholestane 3 alpha 7 alpha 12 alpha 27 tetrol into 3 alpha 7 alpha 12 alpha trihydroxy 5 beta cholestanoic acid
    Journal of Biological Chemistry, 1993
    Co-Authors: I Holmbergbetsholtz, Ingemar Björkhem, Erik G Lund, Kjell Wikvall
    Abstract:

    Abstract The sequence of reactions catalyzed by sterol 27-hydroxylase (CYP27) in the oxidation of 5 beta-Cholestane-3 alpha,7 alpha,12 alpha,27-tetrol into 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestanoic acid was studied with apparently homogeneous preparations of the cytochrome P-450 from rabbit liver mitochondria. Conditions are described for the formation and characterization of 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-Cholestane-27-al as an enzymatically generated intermediate in the oxidation process. Incubation of 5 beta-Cholestane-3 alpha,7 alpha,12 alpha-triol or 5 beta-Cholestane-3 alpha,7 alpha,12 alpha,27-tetrol with sterol 27-hydroxylase in 18O2 atmosphere resulted in the incorporation of one or two 18O atoms in the carboxyl group of 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestanoic acid. Similar incubations with 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-Cholestane-27-al resulted in the incorporation of one 18O atom in the 27-carboxyl group. The results strongly indicate that the sterol 27-hydroxylase performs multiple monooxygenations in the conversion of 5 beta-Cholestane-3 alpha,7 alpha,12 alpha-triol into 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestanoic acid. The following reaction sequence (Reaction 1) at carbon 27 is proposed. [formula: see text] Reaction 1.

Usein M Dzhemilev - One of the best experts on this subject based on the ideXlab platform.

I Holmbergbetsholtz - One of the best experts on this subject based on the ideXlab platform.

  • sterol 27 hydroxylase in bile acid biosynthesis mechanism of oxidation of 5 beta Cholestane 3 alpha 7 alpha 12 alpha 27 tetrol into 3 alpha 7 alpha 12 alpha trihydroxy 5 beta cholestanoic acid
    Journal of Biological Chemistry, 1993
    Co-Authors: I Holmbergbetsholtz, Ingemar Björkhem, Erik G Lund, Kjell Wikvall
    Abstract:

    Abstract The sequence of reactions catalyzed by sterol 27-hydroxylase (CYP27) in the oxidation of 5 beta-Cholestane-3 alpha,7 alpha,12 alpha,27-tetrol into 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestanoic acid was studied with apparently homogeneous preparations of the cytochrome P-450 from rabbit liver mitochondria. Conditions are described for the formation and characterization of 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-Cholestane-27-al as an enzymatically generated intermediate in the oxidation process. Incubation of 5 beta-Cholestane-3 alpha,7 alpha,12 alpha-triol or 5 beta-Cholestane-3 alpha,7 alpha,12 alpha,27-tetrol with sterol 27-hydroxylase in 18O2 atmosphere resulted in the incorporation of one or two 18O atoms in the carboxyl group of 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestanoic acid. Similar incubations with 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-Cholestane-27-al resulted in the incorporation of one 18O atom in the 27-carboxyl group. The results strongly indicate that the sterol 27-hydroxylase performs multiple monooxygenations in the conversion of 5 beta-Cholestane-3 alpha,7 alpha,12 alpha-triol into 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestanoic acid. The following reaction sequence (Reaction 1) at carbon 27 is proposed. [formula: see text] Reaction 1.

Erik G Lund - One of the best experts on this subject based on the ideXlab platform.

  • sterol 27 hydroxylase in bile acid biosynthesis mechanism of oxidation of 5 beta Cholestane 3 alpha 7 alpha 12 alpha 27 tetrol into 3 alpha 7 alpha 12 alpha trihydroxy 5 beta cholestanoic acid
    Journal of Biological Chemistry, 1993
    Co-Authors: I Holmbergbetsholtz, Ingemar Björkhem, Erik G Lund, Kjell Wikvall
    Abstract:

    Abstract The sequence of reactions catalyzed by sterol 27-hydroxylase (CYP27) in the oxidation of 5 beta-Cholestane-3 alpha,7 alpha,12 alpha,27-tetrol into 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestanoic acid was studied with apparently homogeneous preparations of the cytochrome P-450 from rabbit liver mitochondria. Conditions are described for the formation and characterization of 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-Cholestane-27-al as an enzymatically generated intermediate in the oxidation process. Incubation of 5 beta-Cholestane-3 alpha,7 alpha,12 alpha-triol or 5 beta-Cholestane-3 alpha,7 alpha,12 alpha,27-tetrol with sterol 27-hydroxylase in 18O2 atmosphere resulted in the incorporation of one or two 18O atoms in the carboxyl group of 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestanoic acid. Similar incubations with 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-Cholestane-27-al resulted in the incorporation of one 18O atom in the 27-carboxyl group. The results strongly indicate that the sterol 27-hydroxylase performs multiple monooxygenations in the conversion of 5 beta-Cholestane-3 alpha,7 alpha,12 alpha-triol into 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestanoic acid. The following reaction sequence (Reaction 1) at carbon 27 is proposed. [formula: see text] Reaction 1.

Ingemar Björkhem - One of the best experts on this subject based on the ideXlab platform.

  • sterol 27 hydroxylase in bile acid biosynthesis mechanism of oxidation of 5 beta Cholestane 3 alpha 7 alpha 12 alpha 27 tetrol into 3 alpha 7 alpha 12 alpha trihydroxy 5 beta cholestanoic acid
    Journal of Biological Chemistry, 1993
    Co-Authors: I Holmbergbetsholtz, Ingemar Björkhem, Erik G Lund, Kjell Wikvall
    Abstract:

    Abstract The sequence of reactions catalyzed by sterol 27-hydroxylase (CYP27) in the oxidation of 5 beta-Cholestane-3 alpha,7 alpha,12 alpha,27-tetrol into 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestanoic acid was studied with apparently homogeneous preparations of the cytochrome P-450 from rabbit liver mitochondria. Conditions are described for the formation and characterization of 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-Cholestane-27-al as an enzymatically generated intermediate in the oxidation process. Incubation of 5 beta-Cholestane-3 alpha,7 alpha,12 alpha-triol or 5 beta-Cholestane-3 alpha,7 alpha,12 alpha,27-tetrol with sterol 27-hydroxylase in 18O2 atmosphere resulted in the incorporation of one or two 18O atoms in the carboxyl group of 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestanoic acid. Similar incubations with 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-Cholestane-27-al resulted in the incorporation of one 18O atom in the 27-carboxyl group. The results strongly indicate that the sterol 27-hydroxylase performs multiple monooxygenations in the conversion of 5 beta-Cholestane-3 alpha,7 alpha,12 alpha-triol into 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestanoic acid. The following reaction sequence (Reaction 1) at carbon 27 is proposed. [formula: see text] Reaction 1.