Arginine from protein hydrolysis

M.p. 207°C. The naturally occurring substance is dextrorotatory. Arginine is one of the essential amino-acids and one of the most widely distributed products of protein hydrolysis. It is obtained in particularly high concentration from proteins belonging to the prolamine and histone classes. It plays an important role in the production of urea as an excretory product. 

In proteins, targets for methylation include lysine, arginine, and residues containing free carboxyl groups. Histones (chromatin proteins), for example, become methylated at specific arginine and lysine residues at particular times in the cell cycle (see here). s-N-Trimethyllysine, which is derived specifically from the hydrolysis of methylated proteins, is a precursor of carnitine, which transports fatty acyl moieties across membranes (see here). 

It is noteworthy that there is another limiting factor in the choice of amino acid types at the junction sites which affect the enzymatic process of the intein. For example, in the case of SceVMA (also called PI-Seel) from the IMPACT system, proline, cysteine, asparagine, aspartic acid, and arginine cannot be at the C-terminus of the N-terminal target protein just before the intein sequence. The presence of these residues at this position would either slow down the N-S acyl shift dramatically or lead to immediate hydrolysis of the product from the N-S acyl shift [66]. The compatibility of amino acid types at the proximal sites depends on the specific inteins and needs to be carefully considered during the design of the required expression vectors. The specific amino acid requirements at a particular splicing site depends on the specific intein used and is thus a crucial point in this approach. 

This zinc-dependent enzyme [EC 3.4.17.1], a member of the peptidase family M14, catalyzes the hydrolysis of peptide bonds at the C-terminus of polypeptides. Little hydrolytic action occurs if the C-terminal amino acid is aspartate, glutamate, arginine, lysine, or proline. Car-boxypeptidase A is formed from a precursor protein, procarboxypeptidase A. 

This toxin subunit is an enzyme, an ADP-ribo-syltransferase which catalyzes transfer of ADP-ribosyl units from the coenzyme NAD+ to specific arginine side chains to form N-ADP-ribosyl derivatives of various proteins. Of the proteins modified by cholera toxin, the most significant is the guanyl nucleotide regulatory protein Gs of the adenylate cyclase system.C/f/h ADP ribosylation of arginine 201 of the a subunit of protein Gs inhibits the GTP hydrolysis that normally allows the protein to relax to an unactivated form.e The ADP-ribosylated Gs keeps adenylate cyclase activated continuously and... 

Amino acids can be obtained by hydrolysis of proteins, chemical synthesis, fermentation (e.g. of sugars), and enzymatic processes [32], They serve similar purposes as proteins, but in addition, aspartic acid and glutamic acid were rated as top value-added chemicals, which can be converted to further fine chemicals [8]. Another example is the production of building blocks like ethylenediamine and butanediamine from serine and arginine, respectively [6],... 

Figure 4 Residues within Ga that are critical to the GTP hydrolysis mechanism include arginine-178 and threonine-181 from switch I and glutamine-204 from switch II (colored as in Fig. 2 and numbered as in Ga i coordinates are from PDB record IGFI). Magnesium ion is highlighted in yellow. The planar anion aluminum tetrafluoride, which mimics the y-phosphate leaving group in the hydrolysis reaction, is depicted in metallic red. Note the position of serine-47, the target of phosphorylation by the Y. pestis protein kinase YpkA.

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