Enzymatic Formation of Testololactone

Richard L. Prairie; Paul Talalay

doi:10.1021/bi00901a039

Enzymatic Formation of Testololactone

Richard L. Prairie, Paul Talalay

Research output: Contribution to journal › Article › peer-review

47 Scopus citations

Abstract

The conversion of testosterone to testololactone has been studied in soluble and partially purified enzyme systems derived from Penicillium lilacinum. This transformation is carried out by two steroid-induced enzyme systems: a diphosphopyridine nucleotide-linked 17β-hydroxysteroid dehydrogenase that catalyzes the reversible interconversion of testosterone and 4-androstene-3,17-dione; and a lactonizing enzyme system that converts 4-androstene-3,17-dione to testololactone. The lactonization reaction shows an absolute requirement for reduced triphosphopyridine nucleotide and for molecular oxygen. Tracer studies with oxygen have shown that the single oxygen atom incorporated during the formation of the lactone is derived from molecular oxygen and is located in the ethereal and not the carbonyl group linked to C-17.

Original language	English (US)
Pages (from-to)	203-208
Number of pages	6
Journal	Biochemistry
Volume	2
Issue number	1
DOIs	https://doi.org/10.1021/bi00901a039
State	Published - Jan 1 1963
Externally published	Yes

ASJC Scopus subject areas

Biochemistry

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title = "Enzymatic Formation of Testololactone",

abstract = "The conversion of testosterone to testololactone has been studied in soluble and partially purified enzyme systems derived from Penicillium lilacinum. This transformation is carried out by two steroid-induced enzyme systems: a diphosphopyridine nucleotide-linked 17β-hydroxysteroid dehydrogenase that catalyzes the reversible interconversion of testosterone and 4-androstene-3,17-dione; and a lactonizing enzyme system that converts 4-androstene-3,17-dione to testololactone. The lactonization reaction shows an absolute requirement for reduced triphosphopyridine nucleotide and for molecular oxygen. Tracer studies with oxygen have shown that the single oxygen atom incorporated during the formation of the lactone is derived from molecular oxygen and is located in the ethereal and not the carbonyl group linked to C-17.",

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AU - Talalay, Paul

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N2 - The conversion of testosterone to testololactone has been studied in soluble and partially purified enzyme systems derived from Penicillium lilacinum. This transformation is carried out by two steroid-induced enzyme systems: a diphosphopyridine nucleotide-linked 17β-hydroxysteroid dehydrogenase that catalyzes the reversible interconversion of testosterone and 4-androstene-3,17-dione; and a lactonizing enzyme system that converts 4-androstene-3,17-dione to testololactone. The lactonization reaction shows an absolute requirement for reduced triphosphopyridine nucleotide and for molecular oxygen. Tracer studies with oxygen have shown that the single oxygen atom incorporated during the formation of the lactone is derived from molecular oxygen and is located in the ethereal and not the carbonyl group linked to C-17.

AB - The conversion of testosterone to testololactone has been studied in soluble and partially purified enzyme systems derived from Penicillium lilacinum. This transformation is carried out by two steroid-induced enzyme systems: a diphosphopyridine nucleotide-linked 17β-hydroxysteroid dehydrogenase that catalyzes the reversible interconversion of testosterone and 4-androstene-3,17-dione; and a lactonizing enzyme system that converts 4-androstene-3,17-dione to testololactone. The lactonization reaction shows an absolute requirement for reduced triphosphopyridine nucleotide and for molecular oxygen. Tracer studies with oxygen have shown that the single oxygen atom incorporated during the formation of the lactone is derived from molecular oxygen and is located in the ethereal and not the carbonyl group linked to C-17.

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Enzymatic Formation of Testololactone

Abstract

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