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A codon table can be used to translate a genetic code into a sequence of amino acids. [1] [2] The standard genetic code is traditionally represented as an RNA codon table, because when proteins are made in a cell by ribosomes, it is messenger RNA (mRNA) that directs protein synthesis.
Lysine is commonly used as a treatment; however, in a 2015 systematic review, the authors investigated all clinical trials with cats as well as in vitro studies and concluded that lysine supplementation is likely not effective for the treatment or prevention of feline herpesvirus 1 infection. [15]
Pages for logged out editors learn more. Contributions; Talk; ... Print/export Download as PDF; ... (DL-Lysine) ^a CID 5962 from PubChem (L-Lysine)
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]
An equianalgesic chart is a conversion chart that lists equivalent doses of analgesics (drugs used to relieve pain). Equianalgesic charts are used for calculation of an equivalent dose (a dose which would offer an equal amount of analgesia) between different analgesics. [1]
The precursor amino acid lysine contains two amino groups, one at the α-carbon and one at the ε-carbon. Either can be the location of polymerization , resulting in α-polylysine or ε-polylysine. Polylysine is a homopolypeptide belonging to the group of cationic polymers : at pH 7, polylysine contains a positively charged hydrophilic amino group.
In enzymology, a lysine N-acetyltransferase (EC 2.3.1.32) is an enzyme that catalyzes the chemical reaction. acetyl phosphate + L-lysine phosphate + N 6-acetyl-L-lysine. Thus, the two substrates of this enzyme are acetyl phosphate and L-lysine, whereas its two products are phosphate and N6-acetyl-L-lysine.
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.