Publication: Avances en el estudio de la enzimas implicadas en la ruta de degradación del anillo esteroideo en "Rodococcus ruber Chol-4"
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2018-05-31
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Universidad Complutense de Madrid
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Abstract
Rhodococcus ruber Chol-4 es una actinobacteria aislada a partir de una muestra de lodos de depuradora. Esta cepa es capaz de crecer en medio mínimo suplementado con esteroides y compuestos aromáticos, mostrando una gran capacidad catabólica. La degradación de compuestos aromáticos y esteroides ayuda a mantener el ciclo global del carbono, además de tener un número creciente de aplicaciones biotecnológicas que van desde la biodegradación de contaminantes hasta la producción de compuestos farmacéuticos. El género rhodococci contiene múltiples genes homólogos, lo que le confiere una amplia y versátil capacidad catabólica. Sin embargo, la redundancia de genes en los genomas actinobacterianos resulta una seria complicación para obtener intermediarios de interés industrial mediante ingeniería metabólica. La actividad de la enzima 3-cetosteroide-Δ1-deshidrogenasa (KstD) en combinación con la 3-cetosteroide-9α-hidroxilasa (KshAB) es clave en el esquema general del catabolismo bacteriano de esteroides, ambas son responsables de la rotura del núcleo esteroide A/B. KshAB inicia la apertura del anillo de esteroides mediante la 9α-hidroxilación del carbono C9 de 4-eno-3-oxosteroides (p. ej. AD) o 1,4-dieno-3-oxosteroides (p. ej. ADD), transformándolos en 9α-hidroxi-4-androsten-3,17-diona (9OHAD) o 9α-hidroxi-1,4-androstadien-3,17-diona (9OHADD), respectivamente. KstD convierte 4-eno-3-oxoesteroides (p. ej. AD) o 9-hidroxi-4-eno-3-oxoesteroides (p. ej. 9OH-AD) a 1,4-dieno-3-oxoesteroides (p. ej. ADD) o 9-hidroxi-1,4-dieno-3-oxoesteroides (p. ej. 9OH-ADD) por eliminación transaxial de los átomos de hidrógeno C-1 (α) y C-2 (β)...
Rhodococcus ruber strain Chol-4 is an actinobacteria isolated from a sewage sludge sample. It is able to grow in minimal medium supplemented with steroids and aromatic compounds, showing a large catabolic capacity. The degradation of aromatic compounds and steroids helps to maintain the global carbon cycle, and it also has an increasing number of biotechnological applications from biodegradation of pollutants to production of pharmaceutical compounds. The genus rhodococci contains multiple homologues of catabolic genes, which may be the reason of their wide and versatile catabolic capabilities. However, the redundancy of genes in the actinobacterial genomes results in a serious complication for metabolic engineering to obtain intermediates of industrial interest. The 3-ketosteroid-Δ1-deydrogenase activity (KstD) is a key enzyme in the general scheme of the bacterial steroid catabolism in combination with the 3-Ketosteroid-9α-Hydroxylase (KshAB), being both responsible of the steroid nucleus (rings A/B) breakage. KshAB initiates the opening of the steroid ring by the 9α-hydroxylation of the C9 carbon of 4-ene-3-oxosteroids (e.g. AD) or 1,4-diene-3-oxosteroids (e.g. ADD), transforming them into 9α-hydroxy-4-androsten-3,17-dione (9OHAD) or 9α-hydroxy-1,4-androstadiene-3,17-dione (9OHADD) respectively. KstD converts 4-ene-3-oxosteroids (e.g. AD) or 9-hydroxy-4-ene-3-oxosteroids (9OH-AD) to 1,4-diene-3-oxosteroids (e.g. ADD) or 9-hydroxy-1,4-diene-3-oxosteroids (e.g. 9OH-ADD) by trans-axial elimination of the C-1(α) and C-2(β) hydrogen atoms...
Rhodococcus ruber strain Chol-4 is an actinobacteria isolated from a sewage sludge sample. It is able to grow in minimal medium supplemented with steroids and aromatic compounds, showing a large catabolic capacity. The degradation of aromatic compounds and steroids helps to maintain the global carbon cycle, and it also has an increasing number of biotechnological applications from biodegradation of pollutants to production of pharmaceutical compounds. The genus rhodococci contains multiple homologues of catabolic genes, which may be the reason of their wide and versatile catabolic capabilities. However, the redundancy of genes in the actinobacterial genomes results in a serious complication for metabolic engineering to obtain intermediates of industrial interest. The 3-ketosteroid-Δ1-deydrogenase activity (KstD) is a key enzyme in the general scheme of the bacterial steroid catabolism in combination with the 3-Ketosteroid-9α-Hydroxylase (KshAB), being both responsible of the steroid nucleus (rings A/B) breakage. KshAB initiates the opening of the steroid ring by the 9α-hydroxylation of the C9 carbon of 4-ene-3-oxosteroids (e.g. AD) or 1,4-diene-3-oxosteroids (e.g. ADD), transforming them into 9α-hydroxy-4-androsten-3,17-dione (9OHAD) or 9α-hydroxy-1,4-androstadiene-3,17-dione (9OHADD) respectively. KstD converts 4-ene-3-oxosteroids (e.g. AD) or 9-hydroxy-4-ene-3-oxosteroids (9OH-AD) to 1,4-diene-3-oxosteroids (e.g. ADD) or 9-hydroxy-1,4-diene-3-oxosteroids (e.g. 9OH-ADD) by trans-axial elimination of the C-1(α) and C-2(β) hydrogen atoms...
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Tesis inédita de la Universidad Complutense de Madrid, Facultad de Ciencias Químicas, Departamento de Bioquímica y Biología Molecular I, leída el 23-06-2017