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Sirtuin 4, also known as SIRT4, is a mitochondrial protein which in humans is encoded by the SIRT4 gene. [ 5 ] [ 6 ] SIRT4 is member of the mammalian sirtuin family of proteins, which are homologs to the yeast Sir2 protein.
The first sirtuin was identified in yeast (a lower eukaryote) and named sir2. In more complex mammals, there are seven known enzymes that act in cellular regulation, as sir2 does in yeast. These genes are designated as belonging to different classes (I-IV), depending on their amino acid sequence structure. [20]
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.
Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes, and the protein encoded by this gene is included in class I of the sirtuin family. [5] The human sirtuins have a range of molecular functions and have emerged as important proteins in aging, stress resistance, and metabolic regulation.
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 ...
Cytochrome c has an amino acid sequence that is highly conserved in eukaryotes, varying by only a few residues. In more than thirty species tested in one study, 34 of the 104 amino acids were conserved (identical at their characteristic position). [11] For example, human cytochrome oxidase reacted with wheat cytochrome c, in vitro; which held ...
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.
This simple correspondence between amino acids in TAL effectors and DNA bases in their target sites makes them useful for protein engineering applications. Numerous groups have designed artificial TAL effectors capable of recognizing new DNA sequences in a variety of experimental systems.