Biochemistry published new progress about Enzyme functional sites, active. 77215-54-4 belongs to class esters-buliding-blocks, and the molecular formula is C12H24N2O4, Recommanded Product: (S)-tert-Butyl 3-amino-2-((tert-butoxycarbonyl)amino)propanoate.
Moali, Catherine; Brollo, Maurice; Custot, Julien; Sari, Marie-Agnes; Boucher, Jean-Luc; Stuehr, Dennis J.; Mansuy, Daniel published the artcile< Recognition of α-Amino Acids Bearing Various C:NOH Functions by Nitric Oxide Synthase and Arginase Involves Very Different Structural Determinants>, Recommanded Product: (S)-tert-Butyl 3-amino-2-((tert-butoxycarbonyl)amino)propanoate, the main research area is hydroxyguanidine amino acid preparation arginase recognition; amidoxime amino acid preparation nitric oxide synthase recognition; amino acid recognition arginase nitric oxide synthase.
Several α-amino acids bearing a C:NOH function separated from the Cα carbon by two to five atoms have been synthesized and tested as substrates or inhibitors of recombinant nitric oxide synthases (NOS) I and II and as inhibitors of rat liver arginase (RLA). These include four N-hydroxyguanidines, Nω-hydroxy-L-arginine (NOHA) and its analogs homo-NOHA, nor-NOHA, and dinor-NOHA, two amidoximes bearing the -NH-C(CH3):NOH group, and two amidoximes bearing the -CH2-C(NH2):NOH group. Their behavior toward NOS and RLA was compared to that of the corresponding compounds bearing a C:NH function instead of the C:NOH function. The results obtained clearly show that efficient recognition of these α-amino acids by NOS and RLA involves very different structural determinants. NOS favors mols. bearing a -NH-C(R):NH motif separated from Cα by three or four CH2 groups – such as arginine itself – with the necessary presence of δ-NH and ω-NH groups and a more variable R substituent. The corresponding mols. with a C:NOH function exhibit a much lower affinity for NOS. On the contrary, RLA best recognizes mols. bearing a C:NOH function separated from Cα by three or four atoms, the highest affinity being observed in the case of three atoms. The presence of two ω-nitrogen atoms is important for efficient recognition, as in the two best RLA inhibitors, Nω-hydroxynorarginine and Nω-hydroxynorindospicine, which exhibit IC50 values at the micromolar level. However, contrary to what was observed in the case of NOS, the presence of a δ-NH group is not important. These different structural requirements of NOS and RLA may be directly linked to the position of crucial residues that have been identified from crystallog. data in the active sites of both enzymes. Thus, binding of arginine analogs to NOS particularly relies on strong interactions of their δ-NH and ω-NH2 groups with glutamate 371 (of NOS II), whereas binding of C:NOH mols. to RLA is mainly based on interactions of their terminal OH group with the binuclear Mn(II)···Mn(II) cluster of the enzyme and on possible addnl. bonds between their ω-NH2 group with histidine 141, glutamate 277, and one Mn(II) ion. The different modes of interaction displayed by both enzymes depend on their different catalytic functions and provide interesting opportunities to design useful mols. for selective regulation of NOS and arginase.
Biochemistry published new progress about Enzyme functional sites, active. 77215-54-4 belongs to class esters-buliding-blocks, and the molecular formula is C12H24N2O4, Recommanded Product: (S)-tert-Butyl 3-amino-2-((tert-butoxycarbonyl)amino)propanoate.
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Ester – Wikipedia,
Ester – an overview | ScienceDirect Topics