EC Number   |
General Information |
Reference  |
|---|
    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 | metabolism |
liver mitochondria actively catalyze the cleavage of glycine into methylene-THF, CO2, and ammonia, but fail to appreciably catalyze CO2 formation from the alpha-carbon of glycine. The one-carbon compound derived from glycine in the avian livers is utilized largely for the synthesis of uric acid. The yields of 14C-hypoxanthine from 14C-glycine, especially from glycine-2-14C, are significantly increased by the addition of mitochondria to the soluble liver fraction, and under these conditions the ratio of the yields of 14C-hypoxanthine from glycine-l-14C and 2-14C rises to 1:2.3 |
758693 |
| 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 |
| 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 |
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 | metabolism |
isotopic labeling to explore the in vitro and in vivo metabolic fate of the 2-carbon from [2-13C]glycine and [2-13C]serine. As the 2-carbon of glycine and serine is decarboxylated and catabolized via the GCS, the original 13C-labeled 2-carbon is transferred to tetrahydrofolate and yields methylene-tetrahydrofolate in the mitochondria. In hepatoma cell-lines, 2-carbon from glycine is incorporated into deoxythymidine, species of purines (deoxyadenine and deoxyguanine), and methionine |
759374 |
| 1.4.1.27 | metabolism |
isotopic labeling to explore the in vitro and in vivo metabolic fate of the 2-carbon from [2-13C]glycine and [2-13C]serine. In healthy mice, incorporation of GCS-derived formate from glycine 2-carbon is found in serine, methionine, dTMP, and methylcytosine in bone marrow DNA. Labeled glycine 2-carbon directly incorporates into serine, adenine and guanine (at C2 and C8 of purine) in the cytosol |
759374 |
| 1.4.1.27 | physiological function |
in an LpdA deletion mutant, inducible GCV enzyme activity is not detected. A D-3-phosphoglycerate dehydrogenase SerA/LpdA double mutant is unable to utilize glycine as a serine source and lacks detectable GCV enzyme activity |
759421 |
| 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 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 |
