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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. SIRT4 exhibits NAD+-dependent deacetylase activity.
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]
A conservative replacement (also called a conservative mutation or a conservative substitution or a homologous replacement) is an amino acid replacement in a protein that changes a given amino acid to a different amino acid with similar biochemical properties (e.g. charge, hydrophobicity and size). [1] [2]
Serine (symbol Ser or S) [3] [4] is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated − NH +3 form under biological conditions), a carboxyl group (which is in the deprotonated − COO −
1-Aminocyclopropane-1-carboxylic acid (ACC) is a disubstituted cyclic α-amino acid in which a cyclopropane ring is fused to the C α atom of the amino acid. It is a white solid. Many cyclopropane-substituted amino acids are known, but this one occurs naturally. [2] [verification needed] Like glycine, but unlike most α-amino acids, ACC is not ...
Ionization and Brønsted character of N-terminal amino, C-terminal carboxylate, and side chains of amino acid residues The common natural forms of amino acids have a zwitterionic structure, with −NH + 3 ( −NH + 2 − in the case of proline) and −CO − 2 functional groups attached to the same C atom, and are thus α-amino acids, and are ...
Homoserine (also called isothreonine) is an α-amino acid with the chemical formula HO 2 CCH(NH 2)CH 2 CH 2 OH. L-Homoserine is not one of the common amino acids encoded by DNA.It differs from the proteinogenic amino acid serine by insertion of an additional -CH 2 - unit into the backbone.
Peptide bonds to proline, and to other N-substituted amino acids (such as sarcosine), are able to populate both the cis and trans isomers. Most peptide bonds overwhelmingly adopt the trans isomer (typically 99.9% under unstrained conditions), chiefly because the amide hydrogen ( trans isomer) offers less steric repulsion to the preceding C α ...