Anagram & Information om | Engelska ordet LIPOAMIDE
LIPOAMIDE
Antal bokstäver
9
Är palindrom
Nej
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Exempel på hur man kan använda LIPOAMIDE i en mening
- Illustrative of the biochemical role of lipoamide is in the conversion of pyruvate to acetyl lipoamide.
- In humans, arsenite inhibits pyruvate dehydrogenase (PDH complex) in the pyruvate-acetyl CoA reaction, by binding to the –SH group of lipoamide, a participant coenzyme.
- This intermediate is taken up by dihydrolipoyl transacetylase and reacted with a second lipoamide cofactor to generate an acetyl-dihydrolipoyl intermediate, releasing TPP in the process.
- The oxidative decarboxylation reaction is catalyzed by pyruvate dehydrogenase system, which includes three different enzymes: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2), dihydrolipoamide dehydrogenase (E3), six cofactors: thiamine pyrophosphate (TPP), lipoamide, coenzyme A (CoA), flavin adenine dinucleotide (FAD), magnesium ion, and one co-substrate: nicotinamide adenine dinucleotide (NAD+).
- Pyruvate dehydrogenase is an enzyme that catalyzes the reaction of pyruvate and a lipoamide to give the acetylated dihydrolipoamide and carbon dioxide.
- Dihydrolipoamide is a molecule oxidized by dihydrolipoyl dehydrogenase in order to produce lipoamide.
- Degradation of glycine is brought about by the glycine cleavage system, which is composed of four mitochondrial protein components: P protein (a pyridoxal phosphate-dependent glycine decarboxylase), H protein (a lipoic acid-containing protein), T protein (a tetrahydrofolate-requiring enzyme), and L protein (a lipoamide dehydrogenase).
- The T-protein catalyzes the release of ammonia and transfer of the one-carbon fragment from the intermediate lipoyl residue to tetrahydrofolate, while the L-protein, a lipoamide dehydrogenase, catalyzes the oxidation of the dihydrolipoyl residue of H-protein and reduction of NAD.
- The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor, carbon dioxide is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
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