OB fold (Dihydrolipoamide Acetyltransferase, E2P)
glycine:lipoylprotein oxidoreductase (decarboxylating andacceptor-aminomethylating)
S-aminomethyldihydrolipoylprotein:(6S)-tetrahydrofolateaminomethyltransferase (ammonia-forming)
[protein]-8-S-aminomethyldihydrolipoyllysine:tetrahydrofolateaminomethyltransferase (ammonia-forming)
protein-6-N-(dihydrolipoyl)lysine:NAD+ oxidoreductase
Glycine, serine and threonine metabolism
Valine, leucine and isoleucine degradation
The mitochondrial glycine cleavage system. Unique features of the glycine decarboxylation.
Crystallographic data for H-protein from the glycine decarboxylase complex.
X-ray structure determination at 2.6-A resolution of a lipoate-containing protein: the H-protein of the glycine decarboxylase complex from pea leaves.
Refined structures at 2 and 2.2 A resolution of two forms of the H-protein, a lipoamide-containing protein of the glycine decarboxylase complex.
The lipoamide arm in the glycine decarboxylase complex is not freely swinging.
Specific induction by glycine of the gene for the P-subunit of glycine decarboxylase from Saccharomyces cerevisiae.
Structural studies of the glycine decarboxylase complex from pea leaf mitochondria.
Crystal structure of eucaryotic E3, lipoamide dehydrogenase from yeast.
Investigation of the local structure and dynamics of the H subunit of the mitochondrial glycine decarboxylase using heteronuclear NMR spectroscopy.
Biochemical dissection of photorespiration.
Structural and functional characterization of H protein mutants of the glycine decarboxylase complex.
Backbone and sequence-specific assignment of three forms of the lipoate-containing H-protein of the glycine decarboxylase complex.
Theoretical study of the conformation of the H-protein lipoamide arm as a function of its terminal group.
Combined structural and biochemical analysis of the H-T complex in the glycine decarboxylase cycle: evidence for a destabilization mechanism of the H-protein.
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.
Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system. 1. Biochemical studies.
Theoretical study of the conformation of the lipoamide arm in a mutant H protein.
The glycine decarboxylase system: a fascinating complex.
Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations.
Crystal structure of human T-protein of glycine cleavage system at 2.0 A resolution and its implication for understanding non-ketotic hyperglycinemia.
The glycine cleavage system, which catalyzes three distinct reactions (EC 1.4.4.2, 2.1.2.10, 1.8.1.4) is a protein comprex composed of the four proteins: P chain is responsible for the cleavage of glycine (EC 1.4.4.2). T chain is responsible for the transfer of aminomethyl group (EC 2.1.2.10). H chain transports methylamine group from the P chain to the T chain, with the lysine residue (Lys63) covalently-bound to lipoyl group. L chain is responsible for the oxidation of dihydrolipoyl group (EC 1.8.1.4). This enzyme is homologous to the counterpart enzyme (T00017 in EzCatDB). Although the structures of T, H and L chain have been determined, those of the other chain have not been solved yet. As for the reaction by T chain (EC 2.1.2.10), the two consecutive transfer reactions might be involved (see [20]).