GCSH Human
Description
GCSH is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Glycine Cleavage System Protein H (GCSH) is a crucial component of the glycine cleavage system (GCS), a highly conserved protein complex responsible for the oxidative cleavage of glycine. This system is essential for glycine catabolism, which involves the release of carbon dioxide (CO₂) and ammonia (NH₃), and the transfer of a methylene group to tetrahydrofolate, with the concomitant reduction of NAD⁺ to NADH .
The glycine cleavage system consists of four main proteins: glycine decarboxylase (GLDC), aminomethyltransferase (AMT), dehydrolipamide dehydrogenase (DLD), and the H-protein (GCSH). The H-protein acts as a shuttle, interacting with the other three proteins via a lipoyl swinging arm . This interaction is crucial for the proper functioning of the GCS, enabling the decarboxylation of glycine and the subsequent metabolic processes.
GCSH is located at the mitochondrial membrane in eukaryotes and plays a significant role in the major route of glycine catabolism. The glycine cleavage system is part of the most prominent glycine and serine catabolism pathway in humans and most vertebrates . This pathway is vital for the formation of 5,10-methylenetetrahydrofolate, a crucial C₁ donor in biosynthesis .
Mutations in the genes encoding the components of the glycine cleavage system, such as AMT or GLDC, can lead to severe metabolic disorders. These include neural tube defects (NTDs) and ventriculomegaly, as well as a post-natal life-limiting neurometabolic disorder known as Non-Ketotic Hyperglycinemia . However, the specific role of GCSH mutations in these conditions is less clear. Studies have shown that loss of function in GCSH can cause embryonic death prior to mid-gestation, indicating its essential role in embryonic development .
Recent research suggests that GCSH may have additional roles beyond its function in the glycine cleavage system. It is hypothesized that GCSH may act in the lipoylation of 2-oxoacid dehydrogenase proteins, a function reported in bacteria . This potential additional role highlights the importance of GCSH in various metabolic processes.
