PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15453706-0 2004 ACE-inhibitory activity and structural properties of peptide Asp-Lys-Ile-His-Pro [beta-CN f(47-51)]. Proline 77-80 angiotensin I converting enzyme Homo sapiens 0-3 15922781-1 2005 Pyroglutamyl, proline-rich oligopeptides, classically referred to as bradykinin-potentiating peptides (BPPs) are found in Bothrops jararaca venom, and are naturally occurring inhibitors of the somatic angiotensin-converting enzyme (ACE). Proline 14-21 angiotensin I converting enzyme Homo sapiens 232-235 15453706-2 2004 Some of the most potent ACE-inhibitory peptides described in food have a proline at the end of their sequence, a characteristic that can cause problems in the synthesis procedures. Proline 73-80 angiotensin I converting enzyme Homo sapiens 24-27 15337510-2 2004 The compounds, known collectively as angiotensin-converting enzyme (ACE) inhibitors, all share the amino acid residue proline or some variant thereof, as a common structural element. Proline 118-125 angiotensin I converting enzyme Homo sapiens 68-71 2539165-3 1989 Angiotensin-converting enzyme was an effective kininase in mixtures with carboxypeptidase N at physiologic concentration and digested bradykinin to the dipeptides Phe- Arg and Ser-Pro plus the pentapeptide Arg-Pro-Pro-Gly-Phe. Proline 180-183 angiotensin I converting enzyme Homo sapiens 0-29 15236580-2 2004 Here we report the high-resolution crystal structures of testis ACE (tACE) in complex with the first successfully designed ACE inhibitor captopril and enalaprilat, the Phe-Ala-Pro analogue. Proline 176-179 angiotensin I converting enzyme Homo sapiens 64-67 15236580-2 2004 Here we report the high-resolution crystal structures of testis ACE (tACE) in complex with the first successfully designed ACE inhibitor captopril and enalaprilat, the Phe-Ala-Pro analogue. Proline 176-179 angiotensin I converting enzyme Homo sapiens 70-73 9461491-7 1998 The low Km and high kcat values (Km 7.3 and 5.0 microM, kcat 226 and 207 s-1 for the hydrolysis of Phe-Ser-Pro-Arg-Leu-Gly-Lys-Arg and Phe-Ser-Pro-Arg-Leu-Gly-Arg-Arg, respectively) obtained for the hydrolysis of these two peptides by insect ACE means that these peptides, along with mammalian bradykinin, are the most favoured in vitro ACE substrates so far identified. Proline 107-110 angiotensin I converting enzyme Homo sapiens 242-245 9461491-7 1998 The low Km and high kcat values (Km 7.3 and 5.0 microM, kcat 226 and 207 s-1 for the hydrolysis of Phe-Ser-Pro-Arg-Leu-Gly-Lys-Arg and Phe-Ser-Pro-Arg-Leu-Gly-Arg-Arg, respectively) obtained for the hydrolysis of these two peptides by insect ACE means that these peptides, along with mammalian bradykinin, are the most favoured in vitro ACE substrates so far identified. Proline 107-110 angiotensin I converting enzyme Homo sapiens 337-340 8868112-0 1996 Synthesis and biological evaluation of proline derivatives as potential angiotensin converting enzyme inhibitor. Proline 39-46 angiotensin I converting enzyme Homo sapiens 72-101 1320881-5 1992 The beta-casomorphins, beta-casein derived opioid peptides, with a proline residue at their C-terminus also showed inhibitory action on ACE activity, without being cleaved by the enzyme. Proline 67-74 angiotensin I converting enzyme Homo sapiens 136-139 2485059-5 1987 Several newer ACE inhibitors have increased potency and/or improved pharmacokinetic properties due to modifications such as substitution of the proline ring or replacement of the methyl side chain analogous to Ala by an aminobutyl residue analogous to Lys. Proline 144-151 angiotensin I converting enzyme Homo sapiens 14-17 3035180-1 1987 The synthesis of a series of novel, potent angiotensin converting enzyme (ACE) inhibitors containing saturated bicyclic amino acids in place of proline is described. Proline 144-151 angiotensin I converting enzyme Homo sapiens 43-72 3035180-1 1987 The synthesis of a series of novel, potent angiotensin converting enzyme (ACE) inhibitors containing saturated bicyclic amino acids in place of proline is described. Proline 144-151 angiotensin I converting enzyme Homo sapiens 74-77 3035180-2 1987 Octahydroindole-2-carboxylic acid, octahydroisoindole-1-carboxylic acid, and octahydro-3-oxoisoindole-1-carboxylic acid can replace proline in both sulfhydryl and non-sulfhydryl ACE inhibitors to give compounds equipotent to captopril and enalapril both in vitro and in vivo. Proline 132-139 angiotensin I converting enzyme Homo sapiens 178-181 6274413-5 1981 These data indicate that kininase II can release C-terminal tripeptides of substrates having a proline residue in the penultimate position such as des-Arg9-bradykinin and its analogues, and that this enzyme is able not only to act as a dipeptidyl carboxypeptidase but also acts as a tripeptidyl carboxy-peptidase. Proline 95-102 angiotensin I converting enzyme Homo sapiens 25-36 28317757-3 2017 Sequences of ACE-inhibitory peptides are composed of hydrophobic (proline) and aliphatic amino acids (isoleucine and leucine) at the N-terminus. Proline 66-73 angiotensin I converting enzyme Homo sapiens 13-16 33171852-5 2020 The main feature of ACE inhibitory peptides is the location of the hydrophobic residue, usually Proline, at the C-terminus. Proline 96-103 angiotensin I converting enzyme Homo sapiens 20-23 28810191-1 2017 The vasoactive proline-rich oligopeptide termed BPP-BrachyNH2 (H-WPPPKVSP-NH2) induces in vitro inhibitory activity of angiotensin I-converting enzyme (ACE) in rat blood serum. Proline 15-22 angiotensin I converting enzyme Homo sapiens 119-150 28810191-1 2017 The vasoactive proline-rich oligopeptide termed BPP-BrachyNH2 (H-WPPPKVSP-NH2) induces in vitro inhibitory activity of angiotensin I-converting enzyme (ACE) in rat blood serum. Proline 15-22 angiotensin I converting enzyme Homo sapiens 152-155 28810191-9 2017 Thus, the removal of C-terminal proline residue was able to markedly decrease both the BPP-BrachyNH2-induced ACE inhibitory and cytotoxic effects assessed by in vitro and in silico approaches. Proline 32-39 angiotensin I converting enzyme Homo sapiens 109-112 28573254-3 2017 RESULTS: The presence of proline at the C-terminal tripeptide of ACE inhibitor can competitively inhibit the ACE activity. Proline 25-32 angiotensin I converting enzyme Homo sapiens 65-68 28573254-3 2017 RESULTS: The presence of proline at the C-terminal tripeptide of ACE inhibitor can competitively inhibit the ACE activity. Proline 25-32 angiotensin I converting enzyme Homo sapiens 109-112 24596454-4 2014 PURPOSE: We focused on the cis/trans configurations of the peptide bonds in proline-containing tripeptides in order to discover whether the different structural properties of these peptides influence their activity in ACE-1 inhibition. Proline 76-83 angiotensin I converting enzyme Homo sapiens 218-223 25181455-2 2014 This study was conducted to identify the most potent ACE-inhibitory tripeptides with a proline C-terminus, using a novel three-step (tautomerization-docking-ADME simulation) virtual screening process and in vitro assays. Proline 87-94 angiotensin I converting enzyme Homo sapiens 53-56 24516103-2 2014 Dipeptidyl peptidase-4 degrades other peptides with a penultimate proline or alanine, including bradykinin and substance P, which are also substrates of angiotensin-converting enzyme (ACE). Proline 66-73 angiotensin I converting enzyme Homo sapiens 153-182 24516103-2 2014 Dipeptidyl peptidase-4 degrades other peptides with a penultimate proline or alanine, including bradykinin and substance P, which are also substrates of angiotensin-converting enzyme (ACE). Proline 66-73 angiotensin I converting enzyme Homo sapiens 184-187 24596454-9 2014 Based on molecular docking studies, we propose that in ACE-1 inhibition IPP and VPP share a similar cis configuration between the first aliphatic (isoleucine or valine) and the second (proline) amino acid residues and more different configurations between two proline residues. Proline 185-192 angiotensin I converting enzyme Homo sapiens 55-60 24596454-9 2014 Based on molecular docking studies, we propose that in ACE-1 inhibition IPP and VPP share a similar cis configuration between the first aliphatic (isoleucine or valine) and the second (proline) amino acid residues and more different configurations between two proline residues. Proline 260-267 angiotensin I converting enzyme Homo sapiens 55-60 22199132-4 2011 The k(cat)/K(m) values of Nma-Phe-His-Lys(Dnp), Nma-His-Pro-Phe-Lys(Dnp)-Pro, and Hip-His-Leu were 5.12, 1.90, and 0.80 microM(-1) s(-1) for rabbit lung ACE, and 16.0, 7.36, and 0.30 microM(-1) s(-1) for recombinant human (rh)-ACE, respectively. Proline 56-59 angiotensin I converting enzyme Homo sapiens 227-230 22199132-4 2011 The k(cat)/K(m) values of Nma-Phe-His-Lys(Dnp), Nma-His-Pro-Phe-Lys(Dnp)-Pro, and Hip-His-Leu were 5.12, 1.90, and 0.80 microM(-1) s(-1) for rabbit lung ACE, and 16.0, 7.36, and 0.30 microM(-1) s(-1) for recombinant human (rh)-ACE, respectively. Proline 73-76 angiotensin I converting enzyme Homo sapiens 227-230 21923188-6 2011 Especially, the proline residue in the C-terminal end strongly enhanced ACE inhibition. Proline 16-23 angiotensin I converting enzyme Homo sapiens 72-75 19267429-3 2009 We studied the cis-trans isomerization of the proline dipeptide (Ace-Pro-NMe) in explicit water by molecular dynamics simulations using a combined potential derived from ab initio quantum mechanics and empirical molecular mechanics. Proline 46-53 angiotensin I converting enzyme Homo sapiens 65-68 21629912-7 2011 This study reveals that both the selenol or thiol moiety and proline residues are essential for ACE inhibition. Proline 61-68 angiotensin I converting enzyme Homo sapiens 96-99 19884823-2 2010 Research has mainly focused on isoleucine-proline-proline and valine-proline-proline (IPP + VPP), two lactotripeptides that can inhibit the angiotensin-converting enzyme (ACE) in vitro. Proline 42-49 angiotensin I converting enzyme Homo sapiens 140-169 19884823-2 2010 Research has mainly focused on isoleucine-proline-proline and valine-proline-proline (IPP + VPP), two lactotripeptides that can inhibit the angiotensin-converting enzyme (ACE) in vitro. Proline 42-49 angiotensin I converting enzyme Homo sapiens 171-174 18598727-1 2008 The first naturally occurring angiotensin-converting enzyme (ACE) inhibitors described are pyroglutamyl proline-rich oligopeptides, found in the venom of the viper Bothrops jararaca, and named as bradykinin-potentiating peptides (BPPs). Proline 104-111 angiotensin I converting enzyme Homo sapiens 61-64