Electrocatalytic Hydroxylation of Sterols by Steroid C25 Dehydrogenase from Sterolibacterium denitrificans.
Kalimuthu, Palraj; Wojtkiewicz, Agnieszka M; Szaleniec, Maciej; Bernhardt, Paul V.
; 24(30): 7710-7717, 2018 May 28.
Artigo em Inglês | MEDLINE | ID: mdl-29573289
Asymmetric reduction of ketones and ß-keto esters by (S)-1-phenylethanol dehydrogenase from denitrifying bacterium Aromatoleum aromaticum.
Structure of an integral membrane sterol reductase from Methylomicrobium alcaliphilum.
Reductive dehalogenase structure suggests a mechanism for B12-dependent dehalogenation.
Regioselective hydroxylation of cholecalciferol, cholesterol and other sterol derivatives by steroid C25 dehydrogenase.
Substrate uptake and subcellular compartmentation of anoxic cholesterol catabolism in Sterolibacterium denitrificans.
Structural determinants of reductive terpene cyclization in iridoid biosynthesis.
Biochemistry of Catabolic Reductive Dehalogenation.
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Deletion of the gene encoding the reductase component of 3-ketosteroid 9α-hydroxylase in Rhodococcus equi USA-18 disrupts sterol catabolism, leading to the accumulation of 3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid and 1,4-androstadiene-3,17-dione.
Activation and reduction of carbon dioxide by nitrogenase iron proteins.