3-Keto-5alpha-steroid Delta(1)-dehydrogenase from Rhodococcus erythropolis SQ1 and its orthologue in Mycobacterium tuberculosis H37Rv are highly specific enzymes that function in cholesterol catabolism.
作者： Jan Knol , Karin Bodewits , Gerda I. Hessels , Lubbert Dijkhuizen , Robert van der Geize
DOI: 10.1042/BJ20071130
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摘要: The Rhodococcus erythropolis SQ1 kstD3 gene was cloned, heterologously expressed and biochemically characterized as a KSTD3 (3-keto-5alpha-steroid Delta(1)-dehydrogenase). Upstream of kstD3, an ORF (open reading frame) with similarity to Delta(4) KSTD Delta(4)-dehydrogenase) found, tentatively designated kst4D. Biochemical analysis revealed that the Delta(1) has clear preference for 3-ketosteroids saturated A-ring, displaying highest activity on 5alpha-AD (5alpha-androstane-3,17-dione) 5alpha-T (5alpha-testosterone; also known 17beta-hydroxy-5alpha-androstane-3-one). KSTD1 KSTD2 enzymes, other hand, clearly prefer (9alpha-hydroxy-)4-androstene-3,17-dione substrates. Phylogenetic putative amino acid sequences showed R. proteins cluster into four distinct groups. Interestingly, from clustered Rv3537, only present in Mycobacterium tuberculosis H37Rv, protein involved cholesterol catabolism pathogenicity. substrate range Rv3537 enzyme nearly identical KSTD3, indicating these are orthologous enzymes. results imply newly identified intermediates catabolic pathway, important steroids respect
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