Structural and functional features of dimeric dihydrodiol dehydrogenase

Vincenzo Carbone, Akira Hara, Ossama El-Kabbani

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24 Citations (Scopus)

Abstract

Dimeric dihydrodiol dehydrogenase ( DD) catalyzes the NADP(+)- dependent oxidation of trans-dihydrodiols of aromatic hydrocarbons to their corresponding catechols. The tertiary structure of dimeric DD concists of a classical dinucleotide binding domain comprising two beta alpha beta alpha beta motifs at the N-terminus, and an eight-stranded, predominantly antiparallel sheet, forming the C-terminal domain The aim of this reviewis to summarize the biochemical and structural properties of dimeric DD, compare it to enzymes that are structurally similar, and provide an insight into its catalytic mechanism and membership amongst a unique family of monomeric/oligomeric proteins that most likely share a common ancestry.
Original languageEnglish
Pages (from-to)1464 - 1474
Number of pages11
JournalCellular and Molecular Life Sciences
Volume65
Issue number10
Publication statusPublished - 2008

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