Recombinant Desulfovibrio vulgaris Glycine cleavage system H protein (gcvH)
Description
Introduction to Recombinant Desulfovibrio vulgaris Glycine Cleavage System H Protein (gcvH)
The glycine cleavage system H protein (gcvH) in Desulfovibrio vulgaris is a crucial component of the glycine cleavage system (GCS), which plays a significant role in the metabolism of glycine. This system is essential for the oxidative cleavage of glycine, resulting in the release of carbon dioxide, ammonia, and the transfer of a methylene group to tetrahydrofolate, with the concomitant reduction of NAD+ to NADH . The recombinant form of this protein, derived from Desulfovibrio vulgaris, is of particular interest due to its potential roles in both glycine metabolism and as a lipoyl-donor for other enzymes.
Structure and Function of gcvH
The glycine cleavage system H protein (gcvH) is a lipoic acid-containing protein that acts as a carrier in the glycine cleavage reaction. It transfers the methylamine group from the P-protein (glycine decarboxylase) to the T-protein (aminomethyltransferase) . This process is critical for the degradation of glycine in various organisms, including bacteria like Desulfovibrio vulgaris.
| Protein Component | Function |
|---|---|
| P-protein | Glycine decarboxylase, transfers methylamine group to H-protein |
| H-protein (gcvH) | Transfers methylamine group from P-protein to T-protein, contains lipoic acid |
| T-protein | Aminomethyltransferase, catalyzes release of ammonia and transfer of methylene group to tetrahydrofolate |
| L-protein | Dihydrolipoamide dehydrogenase, oxidizes dihydrolipoyl residue of H-protein |
Recombinant Expression and Applications
Recombinant expression of Desulfovibrio vulgaris gcvH allows for the study of its biochemical properties and potential applications. This includes understanding its role as a lipoyl-donor for other enzymes, such as those involved in the pyruvate dehydrogenase complex . The ability of Desulfovibrio vulgaris gcvH to substitute for its human counterpart in certain biochemical pathways highlights its functional conservation across species .
Research Findings and Implications
Recent studies have shown that the ortholog of gcvH in Bacillus subtilis can act as a lipoyl-moiety donor for other lipoic acid-requiring enzymes, suggesting a similar potential role for Desulfovibrio vulgaris gcvH . This function is crucial for the activity of several key metabolic enzymes, including those involved in the tricarboxylic acid cycle.
| Organism | gcvH Function | Implication |
|---|---|---|
| B. subtilis | Lipoyl-moiety donor | Essential for metabolic enzyme activity |
| D. vulgaris | Potential lipoyl-donor | Could support metabolic pathways in anaerobic conditions |
Product Specs
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Target Background
KEGG: dvu:DVU1426
STRING: 882.DVU1426
