Literature DB >> 901754

Oxidation of corticosteroids to steroidal carboxylic acids by an enzyme preparation from hamster liver.

H J Lee, C Monder.   

Abstract

Enzyme activity which catalyzes the oxidation of 11-deoxycorticosterone to 21-oic acids accompanies the "detritiating" enzyme (isomerase) of hamster liver recently isolated by Martin, K. O., et al. ((1977) Biochemistry 16 (preceding paper in this issue)). The metabolites isolated were 20alpha- and 20beta-hydroxy-3-oxo-pregn-4-en-21-oic acid and 3,20-dioxo-pregn-4-en-21-oic acid. When 21-hydroxy[4-14C, 21-3H]pregn-4-en-3,20-dione was the substrate, about half of the tritium was retained in position 20 of the hydroxy acids. The system which catalyzes the conversion of the ketol side chain of corticosteroids to acid metabolites appears to be a cluster of closely related enzymes. As a result of these studies, we believe that the hamster liver enzyme preparation provides a useful model system for studies on the biosynthesis of acid metabolites of the corticosteroids in man.

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Year:  1977        PMID: 901754     DOI: 10.1021/bi00636a014

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


  1 in total

1.  Expanded substrate screenings of human and Drosophila type 10 17beta-hydroxysteroid dehydrogenases (HSDs) reveal multiple specificities in bile acid and steroid hormone metabolism: characterization of multifunctional 3alpha/7alpha/7beta/17beta/20beta/21-HSD.

Authors:  Naeem Shafqat; Hanns-Ulrich Marschall; Charlotta Filling; Erik Nordling; Xiao-Qiu Wu; Lars Björk; Johan Thyberg; Eva Mårtensson; Samina Salim; Hans Jörnvall; Udo Oppermann
Journal:  Biochem J       Date:  2003-11-15       Impact factor: 3.857

  1 in total

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