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.
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
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
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
A combined experimental matrix-isolation FT-IR and theoretical study has been performed to investigate the conformational behavior of N-acetylproline. The conformational landscape of N-acetylproline was explored using successively higher computational methods, i.e. HF, DFT(B3LYP) and finally MP2. The exploration resulted in
The journal of physical chemistry. B, 112(11), 3441-3450 (2008-02-26)
The structure and properties of (s)-N-acetylproline amide (NAP) in aqueous solution are studied by exploiting a continuum solvation model. The conformational preference of NAP as a function of the environment is discussed as well as data for a number of
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