N-Acetyl-L-proline, an analog of the COOH-terminal dipeptide portion of preferred angiotensin-converting enzyme substrates, is use to probe the active site of angiotensin-converting enzyme(s). N-Acetyl-L-proline may be used to to identify, differentiate and characterized N-acyl-amino acid amidohydrolase(s)/aminoacylase(s). N-Acetyl-L-proline is used to study the physicochemical parameters of prolines.
N-acetyl-L-proline is an analog of the COOH-terminal dipeptide portion of preferred substrates of angiotensin-converting enzyme (ACE). It may be used in studies of the binding of substrates and inhibitors by ACE and to differentiate the specificities of various aminoacylases.
Journal of medicinal chemistry, 31(6), 1148-1160 (1988-06-01)
Analogues of captopril, enalaprilat, and the phosphinic acid [hydroxy(4-phenylbutyl)phosphinyl]acetyl]-L-proline incorporating 4-substituted proline derivatives have been synthesized and evaluated as inhibitors of angiotensin-converting enzyme (ACE) in vitro and in vivo. The 4-substituted prolines, incorporating alkyl, aryl, alkoxy, aryloxy, alkylthio, and arylthio
The journal of physical chemistry. B, 111(50), 14034-14042 (2007-11-22)
The results of the ring conformational analysis of L-proline, N-acetyl-L-proline, and trans-4-hydroxy-L-proline by NMR combined with calculations using density functional theory (DFT) and molecular dynamics (MD) are reported. Accurate values of 1H-1H J-couplings in water and other solvents have been
Bioscience, biotechnology, and biochemistry, 69(10), 1914-1922 (2005-10-26)
A novel aminoacylase was purified to homogeneity from culture broth of Streptomyces mobaraensis, as evidenced by SDS-polyacrylamide gel electrophoresis (PAGE). The enzyme was a monomer with an approximate molecular mass of 100 kDa. The purified enzyme was inhibited by the
The journal of physical chemistry. B, 110(38), 18834-18843 (2006-09-22)
A few experimental and theoretical studies on the molecular structure of N-acetylproline amide (AP) in D2O solution have been reported recently. However, there is no consensus of the precise structure of AP in D2O because spectroscopically determined structures and a
The Journal of biological chemistry, 263(9), 4056-4058 (1988-03-25)
We have investigated the interaction of ligands in the active site of the angiotensin-converting enzyme from rabbit lung by monitoring the concurrent effects of two inhibitors on enzyme activity. A strong synergism is found in the binding of N-acetyl-L-proline (an
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