Arginyl

L-Asperaginyl-L-arginyl-L-velyl-L-tyrosyl-L-velyl-L-hlstIdyl-L-prolyl-L-phenylelenine methyl ester trihydrochloride Sodium hydroxide... 

Benzylmercaptopropionyl-L-tyrosyl-L-phenyalanyl-L-glutaminyl-L-asparaginyl-S-benzyl-L-cysteinyl-L-prolyl-N-tosyl-D-arginyl glycinamide Sodium Ammonia Acetic acid... 

L-Asparaginyl-L-arginyl-L-valyl-L-tyrosyl-L-valyl-L-histidyl-L-prolyl-L-phenylalanine methyl ester trihydrochloride Angiotensin amide Atropic acid ethyl ester Tilidine HCI Atropine... 

PA S1 S01.281 Arginyl peptidase Potential drug target in corneal infection by Pseudomonas aeruginosa... 

Trypsin-like proteinases are serine proteinases that recognized peptide residues with positively charged side chains (arginyl or lysyl residues) and that effect... 

R Schwyzer, CH Li. A new synthesis of the pentapeptide L-histidinyl-L-phenylalanyl-L-arginyl-L-tryptophyl-glycine and its melanocyte-stimulating activity. (/Moluene-sulfonyl) Nature (London) 182, 1669, 1958. 

M. J. Muller, B. Samuelsson, J. Z. Haeggstrom, Chemical Modification of Leukotriene A4 Hydrolase. Indications for Essential Tyrosyl and Arginyl Residues at the Active Site , Biochemistry 1995, 34, 3536 - 3543. 

A. An essential role of N-terminal arginylation in cardovascular development. Science 2002, 297, 96-99. 

The L-aminoadipic acid 2 side chain fits into subsite -F 1 in roughly the same way as one side of the GlcNAc + 1 pyranosyl ring. Its carboxylate group does not hydrogen bond to the protein, but rather to the arginyl tail these two long side chains extend into subsite + 2. 

This enzyme [EC 3.4.14.1], also called cathepsin C and cathepsin J, catalyzes the hydrolysis of a peptide bond resulting in the release of an N-terminal dipeptide, XaaXbb-Xcc, except when Xaa is an arginyl or a lysyl residue, or Xbb or Xcc is a prolyl residue. This enzyme, a member of the peptidase family Cl, is a CF-dependent lysosomal cysteine-type peptidase. 

This calcium-activated enzyme [EC 3.4.21.75] catalyzes the hydrolysis of peptide bonds in protein precursors that results in the release of mature proteins from their proproteins by hydrolysis of ArgXaaYaaArg—Zaa bonds, where Xaa can be any amino acid and Yaa is an arginyl or a lysyl residue. Albumin, complement component C3, and von Willebrand factor are thus released from their respective precursors. Furin is a member of the peptidase family S8. 

This zinc-dependent enzyme [EC 3.4.11.1], also referred to as cytosol aminopeptidase, leucyl aminopeptidase, and peptidase S, catalyzes the hydrolysis of a terminal peptide bond such that there is a release of an N-terminal amino acid, Xaa-Xbb-, in which Xaa is preferably a leucyl residue, but may be other aminoacyl residues including prolyl (although not arginyl or lysyl). Xbb may be prolyl. In addition, amino acid amides and methyl esters are also readily hydrolyzed, but the rates with arylamides are exceedingly slow. The enzyme is activated by heavy metal ions. 

This serine-protease [EC 3.4.21.87] catalyzes the hydrolysis of peptide bonds at Xaa—Yaa in which there is a preference for arginyl or lysyl residues at Xaa and Yaa. 

Leuprolide Leuprolide, 5-oxo-L-prolyl-L-histadyl-L-tryptophyl-L-seryl-L-tyrosyl-D-leu-cil-L-leucil-L-arginyl-iV-ethyl-L-prolinamide (30.5.9), is made synthetically [136-139]. 

Isolation of alkaline phosphatase from Escherichia coli in which 85% of the proline residues were replaced by 3,4-dehydro-proline affected the heat lability and ultraviolet spectrum of the protein but the important criteria of catalytic function such as the and were unaltered (12). Massive replacement of methionine by selenomethionine in the 0-galactosidase of E. coli also failed to influence the catalytic activity. Canavanine facilely replaced arginine in the alkaline phosphatase of this bacterium at least 13 and perhaps 20 to 22 arginyl residues were substituted. This replacement by canavanine caused subunit accumulation since the altered subunits did not dimerize to yield the active enzyme (21). Nevertheless, these workers stated "There was also formed, however, a significant amount of enzymatically active protein in which most arginine residues had been replaced by canavanine." An earlier study in which either 7-azatryptophan or tryptazan replaced tryptophan resulted in active protein comparable to the native enzyme (14). 

Examination of this question with the tobacco hornworm, an insect known to be canavanine-sensitive (this insect normally feeds on canavanine-free plants) revealed that it readily incorporates [ C]canavanine into its newly synthesized proteins. Caryedes brasiliensis. however, very effectively avoids the production of such radiolabeled proteins. When the arginyl- RNA synthetase activity of these insects was compared, tobacco hornworm larvae readily activated canavanine while the larvae of the bruchid beetle possess an arginyl- tRNA synthetase with a marked ability to discriminate between arginine and its structural analogue (22). 

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