http://www.cnr.it/ontology/cnr/individuo/prodotto/ID17632
One-pot multienzymatic synthesis of 12-ketoursodeoxycholic acid: subtle cofactor specificities rule the reaction equilibria of five biocatalysts working in a row (Articolo in rivista)
- Type
- Label
- One-pot multienzymatic synthesis of 12-ketoursodeoxycholic acid: subtle cofactor specificities rule the reaction equilibria of five biocatalysts working in a row (Articolo in rivista) (literal)
- Anno
- 2009-01-01T00:00:00+01:00 (literal)
- Alternative label
Monti D., Ferrandi E.E., Zanellato I., Hua L., Polentini F., Carrea G., Riva S. (2009)
One-pot multienzymatic synthesis of 12-ketoursodeoxycholic acid: subtle cofactor specificities rule the reaction equilibria of five biocatalysts working in a row
in Advanced synthesis & catalysis (Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Monti D., Ferrandi E.E., Zanellato I., Hua L., Polentini F., Carrea G., Riva S. (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Istituto di Chimica del Riconoscimento Molecolare, C.N.R., Via Mario Bianco 9, 20131 Milano, Italy. Department of Chemistry, Southern Methodist University, Dallas, TX 75275, USA. Prodotti Chimici e Alimentari S. p. A., Via Novi 78, 15060 Basaluzzo (AL), Italy (literal)
- Titolo
- One-pot multienzymatic synthesis of 12-ketoursodeoxycholic acid: subtle cofactor specificities rule the reaction equilibria of five biocatalysts working in a row (literal)
- Abstract
- The hydroxysteroid dehydrogenases
(HSDHs)-catalyzed one-pot enzymatic synthesis of
12-ketoursodeoxycholic acid (3a,7b-dihydroxy-12-
oxo-5b-cholanoic acid), a key intermediate for the
synthesis of ursodeoxycholic acid, from cholic acid
has been investigated. This goal has been achieved
by alternating oxidative and reductive steps in a one-
pot system employing HSDHs with different cofactor
specificity, namely NADH-dependent HSDHs in the
oxidative step and an NADPH-dependent 7b-HSDH
in the reductive one. Coupled in situ regeneration
systems have been exploited not only to allow the
use of catalytic amounts of the cofactors, but also to
provide the necessary driving force to opposite reac-
tions (i.e., oxidation and reduction) acting on differ-
ent sites of the substrate molecule. Biocatalysts suita-
ble for the set-up of this process have been selected
and their kinetic behaviour in respect of the reac-
tions of interest has been evaluated. Finally, the pro-
cess has been studied employing the enzymes both in
free and compartmentalized form. (literal)
- Prodotto di
- Autore CNR
Incoming links:
- Autore CNR di
- Prodotto
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi