Poly synthetase domain structure

The Domain Structure of Poly(ADP-Ribose) Synthetase and Its Role in Accurate Transcription Initiation... 

Fig. 7A-C. The domain structure of poly(ADP-ribose) synthetase. The chymotryptic and papain cleavage sites on the enzyme molecule are indicated by arrows...

Deletion of the fabi gene can also be appUed in other malonyl-CoA based pathways, such as pathway 8, in order to increase the malonyl-CoA pool for 3-HP production. This malonyl-CoA mediated pathway was also used for the development of novel metabolic pathways for the production of P(3HB-co-3HP) from a structurally unrelated carbon source in Cupriavidus necator, in which malonyl-CoA reductase and the 3-HP-CoA synthetase domain of propionyl-CoA synthase from C. aurantiacus were employed [36]. Recombinant C. necator with malonyl-CoA mediated 3-HP synthetic activity could produce poly(3-hydroxybutyrate-co-3-hydroxypropionate) (P(3HB-co-3HP)), in which 3-HP monomer could be incorporated into copolymer up to 2.1 mol%, from fructose or even alkanoic acids [36]. 

Poly(ADP-ribose) synthetase is a chromatin-bound enzyme which, in the presence of DNA, catalyzes polymerization of the ADP-ribose moiety of NAD to form a protein-bound homopolymer, poly(ADP-ribose) (1). The enzyme is automodified during the reaction. It has been shown that the enzyme consists of three functional domains for DNA-binding, automodification, and NAD-binding (2-4). The enzyme has recently been purified from human placenta and characterized (4, 5). To study the structure and function of the enzyme in more detail we have prepared monoclonal antibodies to the placental enzyme (6, 7). The present study defines three monoclonal antibodies to human poly(ADP-ribose) synthetase and shows that one of the antibodies which binds to the NAD binding domain inhibits the enzyme activity. 

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