Lipoamide is a lipid of Fatty Acyls (FA) class. Lipoamide is associated with abnormalities such as Wiskott-Aldrich Syndrome. The involved functions are known as Phosphorylation, Protonation, Mutagenesis, Site-Directed, Oxidants and Acetylation. Lipoamide often locates in Mitochondria, Mitochondrial matrix, nucleocapsid location and Chloroplasts. The associated genes with lipoamide are Mutant Proteins, Recombinant Proteins, mycothione reductase, alanylproline and Genes, Mitochondrial.
To understand associated biological information of lipoamide, we collected biological information of abnormalities, associated pathways, cellular/molecular locations, biological functions, related genes/proteins, lipids and common seen animal/experimental models with organized paragraphs from literatures.
lipoamide is suspected in and other diseases in descending order of the highest number of associated sentences.
| Disease | Cross reference | Weighted score | Related literature |
|---|
We collected disease MeSH terms mapped to the references associated with lipoamide
| MeSH term | MeSH ID | Detail |
|---|---|---|
| Body Weight | D001835 | 333 associated lipids |
| Liver Cirrhosis, Biliary | D008105 | 12 associated lipids |
| Nerve Degeneration | D009410 | 53 associated lipids |
| Prostatic Neoplasms | D011471 | 126 associated lipids |
| Hyperglycinemia, Nonketotic | D020158 | 2 associated lipids |
There are no associated biomedical information in the current reference collection.
Associated locations are in red color. Not associated locations are in black.
| Location | Cross reference | Weighted score | Related literatures |
|---|
| Function | Cross reference | Weighted score | Related literatures |
|---|
There are no associated biomedical information in the current reference collection.
| Gene | Cross reference | Weighted score | Related literatures |
|---|
There are no associated biomedical information in the current reference collection.
| Authors | Title | Published | Journal | PubMed Link |
|---|---|---|---|---|
| Park YH et al. | Amino-terminal residues 1-45 of the Escherichia coli pyruvate dehydrogenase complex E1 subunit interact with the E2 subunit and are required for activity of the complex but not for reductive acetylation of the E2 subunit. | 2004 | Biochemistry | pmid:15518552 |
| Bryk R et al. | Lipoamide channel-binding sulfonamides selectively inhibit mycobacterial lipoamide dehydrogenase. | 2013 | Biochemistry | pmid:24251446 |
| Argyrou A et al. | The lipoamide dehydrogenase from Mycobacterium tuberculosis permits the direct observation of flavin intermediates in catalysis. | 2002 | Biochemistry | pmid:12463758 |
| Bryk R et al. | Triazaspirodimethoxybenzoyls as selective inhibitors of mycobacterial lipoamide dehydrogenase . | 2010 | Biochemistry | pmid:20078138 |
| Nemeria N et al. | Histidine 407, a phantom residue in the E1 subunit of the Escherichia coli pyruvate dehydrogenase complex, activates reductive acetylation of lipoamide on the E2 subunit. An explanation for conservation of active sites between the E1 subunit and transketolase. | 2002 | Biochemistry | pmid:12501174 |
| Reed GH et al. | Radical reactions of thiamin pyrophosphate in 2-oxoacid oxidoreductases. | 2012 | Biochim. Biophys. Acta | pmid:22178227 |
| Jocelyn PC and Cronshaw AD | The reduction of disulphides by rat liver mitochondria. | 1984 | Biochim. Biophys. Acta | pmid:6421329 |
| Jacobia SJ et al. | Characterization of a missense mutation at histidine-44 in a pyruvate dehydrogenase-deficient patient. | 2002 | Biochim. Biophys. Acta | pmid:11781147 |
| Chan M et al. | A relevant in vitro eukaryotic live-cell system for the evaluation of plasmodial protein localization. | 2006 | Biochimie | pmid:16839657 |
| Tam TK et al. | In situ regeneration of NADH via lipoamide dehydrogenase-catalyzed electron transfer reaction evidenced by spectroelectrochemistry. | 2012 | Bioelectrochemistry | pmid:22497727 |