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TIP. Revista especializada en ciencias químico-biológicas
versión impresa ISSN 1405-888X
TIP vol.8 no.1 Ciudad de México jun. 2005
Artículos de revisión
Las quinoproteínas alcohol deshidrogenasas en los sistemas bacterianos: distribución, clasificación, estructura y función
The alcohol quinoproteins dehydrogenases in the bacterial systems: distribution, classification, structure and function
1Depto. de Bioquímica, Instituto de Fisiología Celular, UNAM. Apdo. Postal 70-242, México, D.F.
2Instituto de Química, UNAM. Apdo. Postal 70-242, México, D.F.
Existe una gran diversidad de alcohol deshidrogenasas (ADHs) microbianas; las cuales son divididas en tres grandes grupos: (a) Las que son dependientes de las coenzimas NAD o NADP, (b) Las que son independientes de estas coenzimas; sin embargo, utilizan pirroloquinolina quinona (PQQ) y hemo tipo C como grupo prostético y (c) Las oxidasas dependientes de FAD que catalizan la reacción irreversible de alcoholes. Las ADHs que utilizan el PQQ, se encuentran a su vez divididas en tres tipos. Las ADHs tipo I que contienen sólo PQQ como grupo prostético y se les conoce como quinoproteínas; mientras que las ADHs tipo II y tipo III además del PQQ contienen hemo tipo C y se les conoce como quinohemoproteínas. Las ADHs tipo II son enzimas solubles que se encuentran en el espacio periplásmico y están presentes en proteobacterias como Pseudomonas putida, Ralstonia eutropha y Comamonas testosteroni. Las ADHs tipo Ill son enzimas que se encuentran ancladas a la membrana y trabajan orientadas hacia el espacio periplásmico. se les ha identificado y caracterizado únicamente en bacterias ácido acéticas. Las ADH tipo III, por lo general contienen tres subunidades. El transporte intramolecular de electrones en las ADHs tipo II y IIII se propone que es del PQQ al hemo C de la primera subunidad y de ahí, de hemo en hemo en la segunda subunidad hasta llegar a la quinona endógena. Los tres tipos de PQQ-ADHs son discutidas en esta revisión.
Palabras clave: Alcohol deshidrogenasas (ADHs); pirrolo-quinolina-quinona (PQQ); quinohemoproteína alcohol deshidrogenasa (qhADH); quinohemoproteína etanol deshidrogenasa (qhEDH); quinoproteína etanol deshidrogenasa (QEDH); quinoproteína metanol deshidrogenasa (QMDH)
Microbial alcohol oxidoreductases constitute a very diverse group. They can be divided into three major categories. (a) NAD(P)-dependent dehydrogenases. (b) NAD(P)-independent enzymes that use pirroloquinoline quinone (PQQ), heme C as cofactor. (c) FAD-dependent oxidases that catalyze an essentially irreversible oxidation of alcohols. The ADHs that have PQQ as the prosthetic group are divided into 3 groups; types I, II and III. Type I ADH is a simple quinoprotein having PQQ as the prosthetic group; while type II and type III ADHs are quinohemoprotein having heme C as well as PQQ. Type II are soluble periplasmic enzymes and are widely distributed in Proteobacterias such as Pseudomonas putida, Ralstonia eutropha and Comamonas testosteroni. Type III ADHs are membrane-bound enzymes and oriented towards the periplasmic surface. They have been identified and characterized solely in acetic acid bacteria. Type III ADH consists of three subunits. The intramolecular electron transfer in the type II and III ADHs is the PQQ to heme C of the first subunit and there, from heme to heme in the second subunit until arriving at ubiquinone. The three types of PQQ-ADHs are discussed in this paper.
Key Words: Alcohol dehydrogenases (ADHs); pyrroloquinoline-quinone (PQQ); quinohemeprotein alcohol dehydrogenase (qhADH); quinohemeprotein ethanol deshydrogenase (qhEDH); quinoprotein ethanol dehydrogenase (QEDH); quinoprotein methanol dehydrogenase (QMDH)
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Recibido: 28 de Enero de 2005; Aprobado: 01 de Abril de 2005
Este es un artículo publicado en acceso abierto bajo una licencia Creative Commons
