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hjq 5.32 mod crackGlycine utilization is an attractive mode for the industrial production of amino acids, as it gives high product yields, does not necessitate the use of expensive and toxic reagents and is relatively environmentally friendly. Glycine is produced by fermentation of glucose or from hydrolysis of biomass. These fermentation processes do not allow for economy of scale and can lead to the production of byproducts such as acetic acid, a feature that can be disadvantageous. In view of the high energy cost of hydrolysis of biomass, a need exists for a process for producing glycine that is more energy efficient and does not produce byproducts.
Biosynthetic pathways involving glycine are attractive as the starting material is inexpensive and abundant. Various glycine and diamine biosynthetic pathways have been described, including the valine, leucine and isoleucine biosynthetic pathways, the lysine, histidine and ornithine biosynthetic pathways, the citrulline and arginine biosynthetic pathways and the diamine biosynthetic pathways, see FIG. 1. The most studied pathway is the pathway responsible for the biosynthesis of glycine from 2-ketoglutarate. The biosynthetic pathway in this system is shown in FIG. 2 and is conventionally referred to as the classical pathway. In the classical pathway, the glycine/diamine (Put, Ser, Thr, Lys, Arg, Hcit, or Orn) moiety is formed by transamination of the corresponding a-amino acid (Val, Leu, Ile, Cit, Arg, Hcit, Orn) by a pyruvoyl-dependent transaminase (GadA, B or C) and then ligated to the a-keto acid (α-KG) by a pyruvate-dependent glycine dehydrogenase (GdcA, B or C). The pyruvate-dependent glycine dehydrogenase has been shown to