From this literature《Side reactions in enzymic peptide synthesis in organic media: effects of enzyme, solvent, and substrate concentrations》,we know some information about this compound(10466-61-2)Name: H-Leu-NH2.HCl, but this is not all information, there are many literatures related to this compound(10466-61-2).
Name: H-Leu-NH2.HCl. Aromatic heterocyclic compounds can also be classified according to the number of heteroatoms contained in the heterocycle: single heteroatom, two heteroatoms, three heteroatoms and four heteroatoms. Compound: H-Leu-NH2.HCl, is researched, Molecular C6H15ClN2O, CAS is 10466-61-2, about Side reactions in enzymic peptide synthesis in organic media: effects of enzyme, solvent, and substrate concentrations. Author is Gololobov, Mikhail Yu.; Stepanov, Valentin M.; Voyushina, Tatjana L.; Morozova, Irina P.; Adlercreutz, Patrick.
The progress of enzymic peptide synthesis catalyzed by α-chymotrypsin and subtilisin from Bacillus subtilis strain 72 (subtilisin 72) in low water systems was studied. The initial reaction mixture consisted of the solvent, the acyl-group donor (Mal-Ala-Ala-Phe-OMe or Z-Ala-Ala-PheO-Me; Mal = maleyl, Z = benzyloxycarbonyl), the nucleophile H-Xaa-NH2 (Xaa = Phe, Leu, Ala), and the enzyme adsorbed on porous silica material. All amino acid residues were of the L-configuration. The solvent consisted of acetonitrile, DMF and 4% (volume/volume) of water. The DMF/acetonitrile ratio was varied between 0 and 1/1. At high concentration of the acyl-group donor, quant. formation of Mal-Ala-Ala-Phe-Xaa-NH2 or Z-Ala-Ala-Phe-Xaa-NH2 occurred. As a result, a method for the synthesis of peptide amides was developed. At low concentration of the acyl group donor and excess of the nucleophile, condensation byproducts with two and three nucleophile mols. were found in the reaction mixtures The data obtained provided evidence that organic solvents affected the S1′-specificity of α-chymotrypsin and the S1-specificity of subtilisin 72, while the S1-specificity of α-chymotrypsin and the S1′-specificity of subtilisin 72 were not affected. When the DMF content was increased, the rate of the α-chymotrypsin-catalyzed reactions decreased. In contrast to this, an increase in DMF content accelerated the subtilisin 72-catalyzed reactions. Hydrolysis of the acyl group donor did not occur in the α-chymotrypsin-catalyzed reactions. Significant (up to 50%) formation of Mal-Ala-Ala-Phe-OH was observed at the early stage of the subtilisin 72-catalyzed reactions. Later, Mal-Ala-Ala-Phe-OH underwent synthesis.
From this literature《Side reactions in enzymic peptide synthesis in organic media: effects of enzyme, solvent, and substrate concentrations》,we know some information about this compound(10466-61-2)Name: H-Leu-NH2.HCl, but this is not all information, there are many literatures related to this compound(10466-61-2).
Reference:
Chiral Catalysts,
Chiral catalysts – SlideShare