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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 ...
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.
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).
In pathway A, both acetate and butyrate are generated from C 2-C 3 cleavage of D-lysine. Unlike pathway A, pathway B involves C 5-C 4 degradation, producing the same products. D-lysine 5,6-aminomutase (5,6-LAM) is responsible for the first conversion in pathway B to convert D-α-lysine into 2,5-diaminohexanoate. Unlike other members of the ...
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.
LysE appears to catalyze unidirectional efflux of L-lysine (and other basic amino acids such as L-arginine), and it provides the sole route for L-lysine excretion. The energy source is believed to be the proton motive force (H + antiport). The E. coli ArgO homologue (TC# 2.A.75.1.2) effluxes arginine and possibly lysine and canavanine as well. [5]
In enzymology, a lysine-pyruvate 6-transaminase (EC 2.6.1.71) is an enzyme that catalyzes the chemical reaction L-lysine + pyruvate ⇌ L-2-aminoadipate 6-semialdehyde + L-alanine Thus, the two substrates of this enzyme are L-lysine and pyruvate , whereas its two products are L-2-aminoadipate 6-semialdehyde and L-alanine .
ALAS is a homodimer with similarly sized sub units and the active sites consisting of amino acid side chains such as arginine, threonine, and lysine exist at a subunity interface. [1] The protein when extracted from R. spheroids contains 1600-folds and weighs about 80,000 daltons. [3] Enzymatic activity varies for different sources of the ...