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In enzymology, a lysine—tRNA ligase (EC 6.1.1.6) is an enzyme that catalyzes the chemical reaction. ATP + L-lysine + tRNALys AMP + diphosphate + L-lysyl-tRNALys. The 3 substrates of this enzyme are ATP, L-lysine, and tRNA(Lys), whereas its 3 products are AMP, diphosphate, and L-lysyl-tRNA(Lys).
Lysine (symbol Lys or K) [2] is an α-amino acid that is a precursor to many proteins.Lysine contains an α-amino group (which is in the protonated −NH + 3 form when the lysine is dissolved in water at physiological pH), an α-carboxylic acid group (which is in the deprotonated −COO − form when the lysine is dissolved in water at physiological pH), and a side chain (CH 2) 4 NH 2 (which ...
Double-stranded DNA phage lysins tend to lie within the 25 to 40 kDa range in terms of size. A notable exception is the streptococcal PlyC endolysin, which is 114 kDa. PlyC is not only the biggest and most potent lysin, but also structurally unique since it is composed of two different gene products, PlyCA and PlyCB, with a ratio of eight PlyCB subunits for each PlyCA in its active conformation.
The 3 substrates of this enzyme are ATP, L-lysine, and tRNA(Pyl), whereas its 3 products are AMP, diphosphate, and L-lysyl-tRNA(Pyl). This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-lysine:tRNAPyl ligase (AMP ...
Shown on the right is the three-dimensional structure of the Lysine 2,3-aminomutase protein. The structure was determined by X-ray crystallography to 2.1 Angstrom resolution and was seen to crystallize as a homotetramer. [2] KAM was first purified and characterized in Clostridium subterminale for studies of Lysine metabolism.
Lysine riboswitch are most abundant in Bacillota and Gammaproteobacteria where they are found upstream of a number of genes involved in lysine biosynthesis, transport and catabolism. [2] [3] [4] The lysine riboswitch has also been identified independently and called the L box. [5] The lysine riboswitch controls metabolic pathways of lysine ...
This pathway is a part of the glutamate family of amino acid biosynthetic pathways. [2] The reaction steps in the pathway are similar to the citric acid cycle. The first step in the pathway is condensation of acetyl-CoA with α-ketoglutarate, which gives homocitrate. This reaction is catalyzed by homocitrate synthase.
Alpha-aminoadipic semialdehyde synthase is an enzyme encoded by the AASS gene in humans and is involved in their major lysine degradation pathway. It is similar to the separate enzymes coded for by the LYS1 and LYS9 genes in yeast, and related to, although not similar in structure, the bifunctional enzyme found in plants.