[Enzymes involved in modification of the steroid nucleus of industrial mycobacterial strains: isolation, functions, and properties]

Autor:	M V, Donova, V M, Nikolaeva, O V, Egorova
Rok vydání:	2005
Předmět:	Sterols 3-Hydroxysteroid Dehydrogenases Culture Media Conditioned Hydroxysteroid Dehydrogenases Testosterone Hydroxylation Oxidation-Reduction Sitosterols Mycobacterium
Zdroj:	Prikladnaia biokhimiia i mikrobiologiia. 41(5)
ISSN:	0555-1099
Popis:	The key enzymes involved in modification of the steroid nucleus of sterol-transforming mycobacteria--3beta-hydroxysteroid oxidase (3-OH-SO, EC 1.13.1.2) and 17beta-hydroxysteroid dehydrogenase (17-OH-SDH, EC 1.1.1)--were isolated and characterized. It is shown that 3-OH-SO is a multifunctional enzyme catalyzing oxidation of the 3beta-OH group, delta5 --delta4 isomerization, and 6-hydroxylation. Two forms of intracellular 17-OH-SDH that catalyze redox reactions at C17 were found, and their properties were determined. The presence of an extracellular 17-OH-SDH in Mycobacterium spp. (VKM Ac-1815 D and Et1) was demonstrated for the first time.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::fb1c7cf5a793e52b0f24ddedc7905782 https://pubmed.ncbi.nlm.nih.gov/16240648 Zobrazit plný text záznamu