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SIRT4 is a mitochondrial ADP-ribosyltransferase that inhibits mitochondrial glutamate dehydrogenase 1 activity, thereby downregulating insulin secretion in response to amino acids. [7] A deacetylation of malonyl-CoA decarboxylase enzyme by SIRT4 represses the enzyme activity, inhibiting fatty acid oxidation in muscle and liver cells.
SIRT3, a mitochondrial protein deacetylase, plays a role in the regulation of multiple metabolic proteins like isocitrate dehydrogenase of the TCA cycle. It also plays a role in skeletal muscle as a metabolic adaptive response. Since glutamine is a source of a-ketoglutarate used to replenish the TCA cycle, SIRT4 is involved in glutamine metabolism.
RNA and DNA contain only right-handed sugars; proteins are exclusively composed of left-handed amino acids, although many bacteria and fungi are able to synthesise non-ribosomal peptides containing right-handed amino acids, as the example of peptidoglycan synthesis shows. This phenomenon is known as homochirality. [11]
S-Aminoethyl-l-cysteine, also known as thialysine, is a toxic analog of the amino acid lysine in which the second carbon of the amino acid's R-group (side chain) has been replaced with a sulfur atom. Strictly speaking, L-thialysine is actually considered an S-(2-aminoethyl) analogue of L-cysteine.
These compounds are structural analogues of amino acids in which a carboxylic moiety is replaced by phosphonic acid or related groups. [1] Acting as antagonists of amino acids, they inhibit enzymes involved in amino acid metabolism and thus affect the physiological activity of the cell.
Mono-N-protected amino acid (MPAA) is a bifunctional ligand that plays a key role in C–H functionalizations by accelerating the reaction rate and imparting specified chirality into the product. [1] Amino acids are ideal building blocks for chiral ligand synthesis due to the cost, accessibility, large variety, solubility, and inherent ...
Seven of 12 amino acids surrounding tryptophan are the same in C- and N-domain, the biggest difference is that 2 bulky and hydrophobic amino acids in the C-domain have been replaced with 2 smaller and polar amino acids in the N-domain.
In molecular biology, pseudo amino acid composition (PseACC) is a method introduced by Kuo-Chen Chou to convert the protein sequence into a numerical vector for enhancing pattern recognition techniques, such as during discrimination between classes of proteins based on their sequences (e.g. between membrane proteins, transmembrane proteins, cytosolic proteins, and other types). [1]