Part of the book: Protein Engineering
The so-called dye-linked dehydrogenases catalyze the oxidation of various biomolecules in the presence of an artificial electron acceptor, in which several unique compounds related to plants as substrates such as opine(s) and L-hydroxyproline are contained. Opines including nopaline and octopine are produced from nutrients of plant by pathogenic agrobacteria species in a crown gall tumor and subsequently degraded for their nutrients by (hypothetical) opine dehydrogenase(s) (OpnDH). The homologous proteins of Pseudomonas putida and Bradyrhizobium japonicum (isozymes 1 and 2) function as nopaline- and octopine-specific dye-linked dehydrogenases, to yield α-ketoglutarate + L-arginine and pyruvate + L-arginine, respectively. L-Hydroxyproline is detected in such hydroxyproline-rich glycoprotein of plant cell walls. In the degradation pathway of bacteria, D-hydroxyproline dehydrogenase (HypDH) catalyzes the dehydrogenation reaction of cis-4-hydroxy-D-proline, and is classified into two types: homomeric and heteromeric enzymes. Both OpnDH and heteromeric HypDH commonly consist of three different subunits (αβγ), in which 2 FAD, 1 FMN, [2Fe-2S] and [4Fe-4S] clusters are contained as prosthetic groups. In D-amino acid dehydrogenase superfamily, these enzymes are physiologically related to L-proline dehydrogenase from archaea and hydrogen cyanide synthase from bacteria, whereas isozyme 2 of OpnDH from B. japonicum and other OpnDHs had appeared by convergent evolution.
Part of the book: Symbiosis