Disease relevance of ECs3774

• Inhibitors of the P protein of GDC block its NO synthase (NOS)-like activity, and variant P produced in E. coli or insect cells displays NOS activity [1].
• Thermus thermophilus (Tth) HB8 glycine decarboxylase (P-protein) is an alpha(2)beta(2) tetrameric enzyme with a total molecular mass of 200 kDa [2].

High impact information on ECs3774

• Here, we demonstrate that the pathogen-induced, NO-synthesizing enzyme is a variant form of the P protein of glycine decarboxylase (GDC) [1].
• Backbone and sequence-specific assignment of three forms of the lipoate-containing H-protein of the glycine decarboxylase complex [3].
• Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system. 1. Biochemical studies [4].
• Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system 2. Crystal structures of H- and L-proteins [5].
• A synthetic gene encoding the entire mature H protein of the glycine decarboxylase complex from pea (Pisum sativum L.) was constructed and expressed in Escherichia coli [6].

Chemical compound and disease context of ECs3774

• Coexpression, purification, crystallization and preliminary X-ray characterization of glycine decarboxylase (P-protein) of the glycine-cleavage system from Thermus thermophilus HB8 [2].

Biological context of ECs3774

• In marked contrast, these analogues strongly and competitively inhibited the decarboxylation of the glycine molecule catalysed by the P-protein component of the glycine decarboxylase system [4].

Other interactions of ECs3774

• The pathogen-inducible nitric oxide synthase (iNOS) in plants is a variant of the P protein of the glycine decarboxylase complex [1].

References