EC Number   |
General Information |
Reference |
|---|
    1.4.1.27 | physiological function |
in tobacco plants overexpressing the Arabidopsis thaliana H-protein, under controlled environment conditions an increase in biomass is evident. Targeted overexpression of the H-protein using the leaf-specific promoter ST-LS1 has a positive impact on biomass, but higher levels of overexpression of this protein driven by the constitutive CaMV 35S promoter result in a reduction in the growth of the plants. In the constitutive overexpressor plants, carbon allocation between soluble carbohydrates and starch is altered, as is the protein lipoylation of the pyruvate dehydrogenase and 2-oxoglutarate complexes |
759926 |
| 1.4.1.27 | physiological function |
mutations in Gldc result in severe or mild elevations of plasma glycine and model non-ketotic hyperglycinemia. Liver of Gldc-deficient mice accumulates glycine and numerous glycine derivatives, including multiple acylglycines. Levels of dysregulated metabolites increase with age and are normalised by liver-specific rescue of Gldc expression. Brain tissue exhibits increased abundance of glycine, as well as derivatives including guanidinoacetate. Elevation of brain tissue glycine occurs even in the presence of only mildly elevated plasma glycine in mice carrying a missense allele of Gldc. Treatment with benzoate enhances hepatic glycine conjugation thereby lowering plasma and tissue glycine. Administration of glycine conjugation pathway intermediate, cinnamate, similarly achieves normalisation of liver glycine derivatives and circulating glycine |
759585 |
| 1.4.1.27 | physiological function |
structure-based dynamic analysis of the induced release of the lipoate arm of protein H. Four major steps of the release process can be distinguished showing significantly different energy barriers and time scales. Mutations of key residue, Ser67 in protein H, leads to a bidirectional tuning of the release process |
759080 |
| 1.4.1.27 | physiological function |
T-protein knock out parasites do not show any growth defect in asexual, sexual and liver stages. T-protein is dispensable for parasite survival in vertebrate and invertebrate hosts |
743266 |
| 1.4.1.27 | physiological function |
the component T-protein catalyzes the degradation of the protein-bound intermediate (-CH2NH2 moiety of glycine) to a 1-carbon unit and NH3. The reaction is dependent on tetrahydrofolate. T-protein associates with H-protein forming a complex of one molecule each of T-protein and H-protein |
759448 |
| 1.4.1.27 | physiological function |
the glycine cleavage system CGS is highly activated to promote stem cell pluripotency and during somatic cell reprogramming. The expression of glycine dehydrogenase GldC, regulated by Sox2 and Lin28A, facilitates this activation. The activated GCS catabolizes glycine to fuel histone H3K4me3 modification, promoting the expression of pluripotency genes. The activated GCS helps to cleave excess glycine and prevents methylglyoxal accumulation, which stimulates senescence in stem cells and during reprogramming |
759700 |
| 1.4.1.27 | physiological function |
the isolated component P-protein can bind glycine and catalyze glycine decarboxylation but at extremely low rate. The product of glycine decarboxylation is methylamine. Methylamine can bind to P-protein, inhibiting the glycine decarboxylation. P-protein alone can also slightly catalyze the exchange of carboxyl carbon of glycine with CO2 and the exchange obeys a pingpong mechanism |
759446 |
| 1.4.1.27 | physiological function |
the lipoamide dehydrogenase component, cf. EC 1.8.1.4, is an indistinguishable constituent among alpha-keto acid dehydrogenase complexes and the glycine cleavage system in mitochondria in nature, and lipoamide dehydrogenase-mediated transfer of reducing equivalents might regulate alpha-keto acid oxidation as well as glycine oxidation |
758695 |
| 1.4.1.27 | physiological function |
the reversible glycine cleavage system in liver mitochondria involves four enzyme proteins designated as P-protein (a pyridoxal phosphate requiring protein), H-protein (a hydrogen carrier protein), L-protein (exhibiting a lipoamide dehydrogenase activity) and T-protein (a H4-folate requiring protein). All three protein fractions obtained during purification are essential for the overall reactions of glycine cleavage and glycine synthesis, while only P-, L-protein and H-protein are required for the glycine-14CO2 exchange |
759438 |
| 1.4.1.27 | physiological function |
the reversible glycine cleavage system is composed of four protein components named as P-, H-, L-, and T-protein, respectively. P-protein catalyzes the decarboxylation of glycine or its reverse reaction in the presence of H-protein, and T-protein participates in the formation of one carbon unit and ammonia or the reverse reaction |
758694 |
