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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.
[2] [3] They are ancient in animal evolution and appear to possess a highly conserved structure throughout all kingdoms of life. [2] Chemically, sirtuins are a class of proteins that possess either mono- ADP-ribosyltransferase or deacylase activity, including deacetylase, desuccinylase , demalonylase , demyristoylase and depalmitoylase activity.
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 ...
Norvaline (abbreviated as Nva) is an amino acid with the formula CH 3 (CH 2) 2 CH(NH 2)CO 2 H. The compound is a structural analog of valeric acid and also an isomer of the more common amino acid valine. [2] Like most other α-amino acids, norvaline is chiral. It is a white, water-soluble solid.
Diaminopimelic acid (DAP) is an amino acid, representing an epsilon-carboxy derivative of lysine. meso-α,ε-Diaminopimelic acid is the last intermediate in the biosynthesis of lysine and undergoes decarboxylation by diaminopimelate decarboxylase to give the final product. [1] DAP is a characteristic of certain cell walls [2] of some
A string is defined as a contiguous sequence of code units terminated by the first zero code unit (often called the NUL code unit). [1] This means a string cannot contain the zero code unit, as the first one seen marks the end of the string. The length of a string is the number of code units before the zero code unit. [1]
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.
Sirtuin 1, also known as NAD-dependent deacetylase sirtuin-1, is a protein that in humans is encoded by the SIRT1 gene. [5] [6] [7]SIRT1 stands for sirtuin (silent mating type information regulation 2 homolog) 1 (S. cerevisiae), referring to the fact that its sirtuin homolog (biological equivalent across species) in yeast (Saccharomyces cerevisiae) is Sir2.