Amino-acid residues arginine

Conserved amino acid residues Arginine residue (binding site to CO2H group)... 

Is and PBPRP1 may then represent an OBP-1 type of protein defined by key residues that may underlie specific functions. The ABPX/PBPRP-specific amino acid residues arginine at position 16, lysine at position 47, proline at position 76, threonine at position 92 are replaced respectively by leucine, glycine, lysine and lysine residues that are conserved in the different types of binding protein from B. mori (Krieger et al., 1993 Picimbon, 2001). These replacements may be relevant to support the function of ABPX. Based on the crystal structure of the bombykol-PBP complex, the tryptophane at position 101 and the valine 105 have been shown to contact the molecule of Bombykol (Sandler et al., 2000). These are replaced by two threonine residues characteristic of OBP-1. Therefore, the threonine residues characteristic of OBP Is may be of crucial importance for the binding specificities of these proteins. 

Figure 6. Binding site region of Protoporphyrinogen IX Oxidase 2 [Protox, pdb code ISEZ) with the co-crystallized inhibitor /NH (ball and sticks representation), the critical amino acid residue arginine (Arg) and the co-factor FAD. Re-docked solutions are indicated inside (int) and outside (ext) of the detected binding pocket.

ENZYMATIC ANALYSIS WITH CARBOXYPEPTIDASES. Carboxypeptidases are enzymes that cleave amino acid residues from the C-termini of polypeptides in a successive fashion. Four carboxypeptidases are in general use A, B, C, and Y. Carboxypeptidase A (from bovine pancreas) works well in hydrolyzing the C-terminal peptide bond of all residues except proline, arginine, and lysine. The analogous enzyme from hog pancreas, carboxypeptidase B, is effective only when Arg or Lys are the C-terminal residues. Thus, a mixture of carboxypeptidases A and B liberates any C-terminal amino acid except proline. Carboxypeptidase C from citrus leaves and carboxypeptidase Y from yeast act on any C-terminal residue. Because the nature of the amino acid residue at the end often determines the rate at which it is cleaved and because these enzymes remove residues successively, care must be taken in interpreting results. Carboxypeptidase Y cleavage has been adapted to an automated protocol analogous to that used in Edman sequenators. 

It is a peptide containing 27 amino acid residues containing the amino acids L-histidine (His) L-aspartic acid (Asp) L-serine (Ser) glycine (Gly) L-threonine (Thr) L-phenyl-alanine (Phe) L-glutamic acid (Glu) L-glutamine [Glu(NHj)] L-leucine (Leu) L-arginine (Arg) L-alanine (Ala) and L-valinamide (Va -NHj). 

Note The amino acid residues of lysine (K) and arginine (R) which may be responsible for the binding of POs to polysaccharides are in bold. According to Demand et al. (2002), the mutual substitution of these amino acids has no influence on the sorption properties of the ATg08770 PO of Arabidopsis with pectins, and the deletion of the fragment results in the loss of this function. 

Neurotoxins present in sea snake venoms are summarized. All sea snake venoms are extremely toxic, with low LD5Q values. Most sea snake neurotoxins consist of only 60-62 amino acid residues with 4 disulOde bonds, while some consist of 70 amino acids with 5 disulfide bonds. The origin of toxicity is due to the attachment of 2 neurotoxin molecules to 2 a subunits of an acetylcholine receptor that is composed of a2 6 subunits. The complete structure of several of the sea snake neurotoxins have been worked out. Through chemical modification studies the invariant tryptophan and tyrosine residues of post-synaptic neurotoxins were shown to be of a critical nature to the toxicity function of the molecule. Lysine and arginine are also believed to be important. Other marine vertebrate venoms are not well known. 

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