Literature DB >> 2833663

Hydroxysteroid dehydrogenase of Cochliobolus lunatus.

A Plemenitas1, M Zakelj-Mavric, R Komel.   

Abstract

Cochliobolus lunatus is known to be able to hydroxylate steroids at position 11 beta. Besides this inducible enzyme, we found a constitutive hydroxysteroid dehydrogenase activity which is strongly regioselective with the highest activity at position 17, and the best substrate was found to be androstenedione. Using different substrates, no such activities were observed at positions 3 or 11. The enzyme is membrane bound and NADH or NADPH dependent. The protoplasts of Cochliobolus lunatus show the same activity as intact cells, which means that the cell wall does not influence the reaction.

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Year:  1988        PMID: 2833663     DOI: 10.1016/0022-4731(88)90041-6

Source DB:  PubMed          Journal:  J Steroid Biochem        ISSN: 0022-4731            Impact factor:   4.292


  3 in total

1.  A novel 17beta-hydroxysteroid dehydrogenase in the fungus Cochliobolus lunatus: new insights into the evolution of steroid-hormone signalling.

Authors:  T Lanisnik Rizner; G Moeller; H H Thole; M Zakelj-Mavric; J Adamski
Journal:  Biochem J       Date:  1999-02-01       Impact factor: 3.857

2.  Altered expression of the steroid bioconverting pathway in pAN 7-1 transformants of Cochliobolus lunatus.

Authors:  D Rozman; R Komel
Journal:  Curr Genet       Date:  1991-11       Impact factor: 3.886

3.  Engineering Mycobacterium smegmatis for testosterone production.

Authors:  Lorena Fernández-Cabezón; Beatriz Galán; José L García
Journal:  Microb Biotechnol       Date:  2016-11-17       Impact factor: 5.813

  3 in total

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