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L-alanine is second only to L-leucine in rate of occurrence, accounting for 7.8% of the primary structure in a sample of 1,150 proteins. [5] The right-handed form, D -alanine, occurs in peptides in some bacterial cell walls [ 6 ] : 131 (in peptidoglycan ) and in some peptide antibiotics , and occurs in the tissues of many crustaceans and ...
Glycine N-carboxyanhydride is the parent member of the amino acid N-carboxyanhydrides.. NCAs are typically prepared by phosgenation of amino acids: [4]. They were first synthesized by Hermann Leuchs by heating an N-ethoxycarbonyl or N-methoxycarbonyl amino acid chloride in a vacuum at 50-70 °C: [5] [6]
[citation needed] During cell culture, L-alanyl-L-glutamine is broken down into L-glutamine which is an essential nutrient for the cells. Because the chemical compound L-alanyl-L-glutamine is broken down a little at a time, the cells have time to use the L-glutamine that is formed before it is broken down into ammonia and pyrrolidine carboxylic ...
L-aspartate L-alanine + CO 2. Hence, this enzyme has one substrate, L-aspartate, and two products, L-alanine and CO 2. This reaction is the basis of the industrial synthesis of L-alanine. [1] This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds.
Cysteic acid also known as 3-sulfo-l-alanine is the organic compound with the formula HO 3 SCH 2 CH(NH 2)CO 2 H. It is often referred to as cysteate, which near neutral pH takes the form − O 3 SCH 2 CH(NH 3 +)CO 2 −. It is an amino acid generated by oxidation of cysteine, whereby a thiol group is fully oxidized to a sulfonic acid/sulfonate ...
Thus, the two substrates of this enzyme are L-arginine and pyruvate, whereas its two products are 5-guanidino-2-oxopentanoate and L-alanine. This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-arginine:pyruvate aminotransferase.
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