Side chain removal from corticosteroids by unspecific peroxygenase

Two unspecific peroxygenases (UPO, EC 1.11.2.1) from the basidiomycetous fungi Marasmius rotula and Marasmius wettsteinii oxidized steroids with hydroxyacetyl and hydroxyl functionalities at C17 - such as cortisone, Reichstein's substance S and prednisone - via stepwise oxygenation and final fi...

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Bibliographic Details
Published in:Journal of Inorganic Biochemistry
Main Authors: Ullrich, René, Hofrichter, Martin, Poraj-Kobielska, Marzena, Pecyna, Marek, Scheibner, Katrin, Scholze, Steffi, Sandvoss, Martin, Halbout, Claire
Format: Article in Journal/Newspaper
Language:English
Published: Elsevier 2018
Subjects:
info:eu-repo/classification/ddc/540
ddc:540
info:eu-repo/classification/ddc/570
ddc:570
Peroxygenierung
Peroxide shunt
P450
Häm-Thiolat
Deacylierung
Geminaler Alkohol
Peroxygenation
Heme-thiolate
Deacylation
Geminal alcohol
Carbonic acid
Online Access:https://nbn-resolving.org/urn:nbn:de:bsz:14-qucosa-235595
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Description
Summary:Two unspecific peroxygenases (UPO, EC 1.11.2.1) from the basidiomycetous fungi Marasmius rotula and Marasmius wettsteinii oxidized steroids with hydroxyacetyl and hydroxyl functionalities at C17 - such as cortisone, Reichstein's substance S and prednisone - via stepwise oxygenation and final fission of the side chain. The sequential oxidation started with the hydroxylation of the terminal carbon (C21) leading to a stable geminal alcohol (e.g. cortisone 21-gem-diol) and proceeded via a second oxygenation resulting in the corresponding α-ketocarboxylic acid (e.g. cortisone 21-oic acid). The latter decomposed under formation of adrenosterone (4-androstene-3,11,17-trione) as well as formic acid and carbonic acid (that is in equilibrium with carbon dioxide); fission products comprising two carbon atoms such as glycolic acid or glyoxylic acid were not detected. Protein models based on the crystal structure data of MroUPO (Marasmius rotula unspecific peroxygenase) revealed that the bulky cortisone molecule suitably fits into the enzyme's access channel, which enables the heme iron to come in close contact to the carbons (C21, C20) of the steroidal side chain. ICP-MS analysis of purified MroUPO confirmed the presence of magnesium supposedly stabilizing the porphyrin ring system.

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