124882-74-2Relevant articles and documents
Action of Serine Carboxypeptidases on Endopeptidase Substrates, N-Acyldipeptideamides
Kunugi, Shigeru,Tanabe, Kazuo,Yamashita, Kouji,Fukuda, Mitsuhiro
, p. 1399 - 1402 (1987)
Action patterns of two serine carboxypeptidases, one from yeast (Y) and the other from wheat bran (W), on N--(Fua-)-dipeptideamide substrates were examined by HPLC and amino acid analysis.In the reaction of the wheat enzyme the substrates were hydrolyzed to Fua-amino acid and no sufficient amount of Fua-dipeptides were detected on HPLC in the product mixtures.Very few or no free amino acids were observed by amino acid analysis.This indicates that the wheat enzyme exhibited carboxamidopeptidase activity on these substrates.On the contrary, carboxypeptidase Y gave Fua-amino acids and Fua-dipeptides as products, depending on the structure of the substrates.Accordingly, liberations of free amino acids were detected in some cases.This result shows that the yeast enzyme acts on some of the substrates in a two step manner: First by amidase and second by a carboxypeptidase activity.Based on these results the substrate binding mechanisms of these enzymes are discussed.
Transition-State Structural Features for the Thermolysin-Catalyzed Hydrolysis of N-(3-acryloyl)-Gly-LeuNH2
Stein, Ross L.
, p. 7907 - 7908 (1988)
-
Preparation and synthetic applications of N-(α,β-unsaturated acyl)-α-amino acid derivatives
Katritzky, Alan R.,Gyanda, Reena,Meher, Nabin K.,Song, Yuming
experimental part, p. 1249 - 1259 (2010/10/03)
N-(α,β-Unsaturated acyl)-α-amino acids, amides and esters are structural motifs of many biologically active natural products. An alternate and advantageous approach for the synthesis of N-(α,β-unsaturated acyl)-α-amino acid derivatives is developed via ac
Protease-Catalyzed Peptide Formation under High Pressure
Kunugi, Shigeru,Tanabe, Kazuo,Yamashita, Kouji,Morikawa, Yoshio,Ito, Takanobu,et al.
, p. 514 - 518 (2007/10/02)
The effect of high pressure on peptide formation by the catalysis of carboxypeptidase Y (substitution of ester or peptide by amino acid derivative) or by thermolysin (condensation of N-acylamino acid and amino acid amide) was studied.The carboxypeptidase Y-catalyzed substitution reaction of N-phenylalanine ethyl ester with glycinamide or phenylalaninamide showed a six-fold higher total peptide yield at 200 MPa than at atmospheric pressure.In the case of the reaction of N-acyldipeptide and amino acid amide, both the peptide yield and substitution efficiency were improved at elevated pressure and the wasteful hydrolysis of the substrate was highly depressed by increasing pressure.The pressure was also effective to get rid of the substrate inhibition by the amino acid ester inthe reaction between the N-acylamino acid ester and the amino acid ester and to yield much dipeptide ester at high pressure.An improvement of the peptide yield by pressure for the reaction of thermolysin was observed in a combination of less specific substrates, N-benzyloxycarbonyl-L-aspartic acid and phenylalanine methyl ester, since the high catalytic activity of this enzyme under elevated pressure was significant only in the case that the peptide yield was kinetic-controlled.
