PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2554286-11 1989 The testis enzyme contains the second of the two putative metal-binding sites (His-Glu-Met-Gly-His) identified in endothelial ACE. Histidine 79-82 angiotensin I converting enzyme Homo sapiens 126-129 2554286-11 1989 The testis enzyme contains the second of the two putative metal-binding sites (His-Glu-Met-Gly-His) identified in endothelial ACE. Histidine 95-98 angiotensin I converting enzyme Homo sapiens 126-129 32945658-6 2020 The interactions inhibiting heme dissociation were then seen to be (i) either a direct or a water molecule mediated interaction between distal histidine and heme iron; and (ii) stacking between heme and the alphaCE1/betaCD1 phenylalanine residue. Histidine 143-152 angiotensin I converting enzyme Homo sapiens 207-223 2983326-5 1985 ACE also released the COOH-terminal tripeptide, Arg-Pro-Gly-NH2, and then sequentially the dipeptides Gly-Leu and Ser-Try, leaving less than Glu-His-Trp intact. Histidine 145-148 angiotensin I converting enzyme Homo sapiens 0-3 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. Histidine 34-37 angiotensin I converting enzyme Homo sapiens 227-230 28339746-5 2017 The ACE-inhibitory activity was determined using the cleavage of a chromogenic substrate -Hip-His-Leu. Histidine 94-97 angiotensin I converting enzyme Homo sapiens 4-7 22199132-8 2011 The newly developed IQF substrate, Nma-Phe-His-Lys(Dnp), is a valuable tool for ACE and carboxypeptidase studies. Histidine 43-46 angiotensin I converting enzyme Homo sapiens 80-83 18085519-6 2008 The use of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS) coupled with the (18)O-labeled internal standard approach has allowed us to show that (i) the N-domain of ACE (N-ACE), but not the C-domain, selectively cleaves the Arg-5-His-6 bond in both peptides, and that (ii) N-ACE hydrolyzes the isoAsp-7 analogue more efficiently than the non-modified one. Histidine 273-276 angiotensin I converting enzyme Homo sapiens 208-211 20467653-2 2010 Herein, we advanced the concept of moving affinity boundary (MAB) using metal ion Ni(II) and histidine (His) as the model inorganic ion and ligand, respectively, developed the simple method of MAB affinity capillary electrophoresis (MAB-ACE), and carried out the relative experiments. Histidine 93-102 angiotensin I converting enzyme Homo sapiens 237-240 20467653-2 2010 Herein, we advanced the concept of moving affinity boundary (MAB) using metal ion Ni(II) and histidine (His) as the model inorganic ion and ligand, respectively, developed the simple method of MAB affinity capillary electrophoresis (MAB-ACE), and carried out the relative experiments. Histidine 104-107 angiotensin I converting enzyme Homo sapiens 237-240 20467653-3 2010 The experiments manifested that (a) an MAB could be created with the model metal ion and ligand; (b) the MAB-ACE could specifically capture His rather than other amino acids, or numerous metabolites in human urine; and (c) the capture had the merits of simultaneous focusing and separation to the target metabolite of His. Histidine 140-143 angiotensin I converting enzyme Homo sapiens 109-112 20467653-5 2010 The analyses of His in raw urine by the MAB-ACE are in agreement with those via the standard amino acid analyzer, indicating the reliability of the developed method. Histidine 16-19 angiotensin I converting enzyme Homo sapiens 44-47 18853057-6 2008 RESULTS: The purified ACE (MM = 140 kDa), releases angiotensin II, hydrolyses bradykinin and the Hip-His-Leu substrate. Histidine 101-104 angiotensin I converting enzyme Homo sapiens 22-25 14595564-5 2004 Supine ACE levels were dependent upon ACE genotype [24.8 (5.7), 26.9 (4.5), 45.5 (6.4) nmol His-Leu ml(-1) min(-1); II, ID, DD, respectively; P<0.00005] and thereafter. Histidine 92-95 angiotensin I converting enzyme Homo sapiens 7-10 16033330-4 2005 We demonstrate here that a 1:1 stoichiometry for the binding of the common ACE inhibitors, captopril and lisinopril, to human s-ACE is enough to abolish enzymatic activity towards FA {N-[3-(2-furyl)acryloyl]}-Phe-GlyGly, Cbz (benzyloxycarbonyl)-Phe-His-Leu or Hip (N-benzoylglycyl)-His-Leu. Histidine 249-252 angiotensin I converting enzyme Homo sapiens 75-78 16033330-4 2005 We demonstrate here that a 1:1 stoichiometry for the binding of the common ACE inhibitors, captopril and lisinopril, to human s-ACE is enough to abolish enzymatic activity towards FA {N-[3-(2-furyl)acryloyl]}-Phe-GlyGly, Cbz (benzyloxycarbonyl)-Phe-His-Leu or Hip (N-benzoylglycyl)-His-Leu. Histidine 249-252 angiotensin I converting enzyme Homo sapiens 128-131 16033330-6 2005 Kinetic analysis of the simultaneous hydrolysis of two substrates, Hip-His-Leu (S1) and Cbz-Phe-His-Leu (S2), with a common product (His-Leu) by s-ACE at different values for the ratio of the initial concentrations of these substrates (i.e. sigma=[S2]0/[S1]0) demonstrated competition of these substrates for binding to the s-ACE molecule, i.e. binding of a substrate at one active site makes the other site unavailable for either the same or a different substrate. Histidine 71-74 angiotensin I converting enzyme Homo sapiens 147-150 15453706-0 2004 ACE-inhibitory activity and structural properties of peptide Asp-Lys-Ile-His-Pro [beta-CN f(47-51)]. Histidine 73-76 angiotensin I converting enzyme Homo sapiens 0-3 14595564-5 2004 Supine ACE levels were dependent upon ACE genotype [24.8 (5.7), 26.9 (4.5), 45.5 (6.4) nmol His-Leu ml(-1) min(-1); II, ID, DD, respectively; P<0.00005] and thereafter. Histidine 92-95 angiotensin I converting enzyme Homo sapiens 38-41 11067854-3 2001 Multiple sequence alignment was used to predict His(1089) as the catalytic residue in human ACE C-domain that, by analogy with the prototypical gluzincin, thermolysin, stabilizes the scissile carbonyl bond through a hydrogen bond during transition state binding. Histidine 48-51 angiotensin I converting enzyme Homo sapiens 92-95 11067854-8 2001 H1089A has a pH optimum of 5.5 with no pH dependence of its catalytic activity in the range 6.5-10.5, indicating that the His(1089) side chain allows ACE to function as an alkaline peptidyl-dipeptidase. Histidine 122-125 angiotensin I converting enzyme Homo sapiens 150-153 11067854-9 2001 Since transition state mutants of other gluzincins show pH optima shifts toward the alkaline, this effect of His(1089) on the ACE pH optimum and its ability to influence transition state binding of the sulfhydryl inhibitor captopril indicate that the catalytic mechanism of ACE is distinct from that of other gluzincins. Histidine 109-112 angiotensin I converting enzyme Homo sapiens 126-129 11067854-9 2001 Since transition state mutants of other gluzincins show pH optima shifts toward the alkaline, this effect of His(1089) on the ACE pH optimum and its ability to influence transition state binding of the sulfhydryl inhibitor captopril indicate that the catalytic mechanism of ACE is distinct from that of other gluzincins. Histidine 109-112 angiotensin I converting enzyme Homo sapiens 274-277 7923904-6 1994 Genotyping for the I/D polymorphism was performed by polymerase chain reaction and plasma DCP1 activity was measured by rate of hydrolysis of both [3H]-Hip-Gly-Gly and Hip-His-Leu. Histidine 172-175 angiotensin I converting enzyme Homo sapiens 90-94 8817875-1 1996 Angiotensin-converting enzyme (ACE; EN 3.4.15.1) is a peptidyl dipeptide hydrolase that removes the carboxyl terminal His-Leu from angiotensin I to produce the octapeptide angiotensin II. Histidine 118-121 angiotensin I converting enzyme Homo sapiens 0-29 8817875-1 1996 Angiotensin-converting enzyme (ACE; EN 3.4.15.1) is a peptidyl dipeptide hydrolase that removes the carboxyl terminal His-Leu from angiotensin I to produce the octapeptide angiotensin II. Histidine 118-121 angiotensin I converting enzyme Homo sapiens 31-34 7683654-2 1993 Angiotensin I-converting enzyme (ACE, E.C.3.4.15.1) has been recently shown to contain two very similar domains, each of which bears a functional active site hydrolyzing Hip-His-Leu or angiotensin I (AI). Histidine 174-177 angiotensin I converting enzyme Homo sapiens 0-31 7961923-1 1994 Angiotensin I-converting enzyme (ACE) contains two zinc-dependent catalytic domains (N and C domains) each bearing the motif HEXXH where the two histidines form two of the three amino acid zinc ligands. Histidine 145-155 angiotensin I converting enzyme Homo sapiens 0-31 7961923-1 1994 Angiotensin I-converting enzyme (ACE) contains two zinc-dependent catalytic domains (N and C domains) each bearing the motif HEXXH where the two histidines form two of the three amino acid zinc ligands. Histidine 145-155 angiotensin I converting enzyme Homo sapiens 33-36 7683654-2 1993 Angiotensin I-converting enzyme (ACE, E.C.3.4.15.1) has been recently shown to contain two very similar domains, each of which bears a functional active site hydrolyzing Hip-His-Leu or angiotensin I (AI). Histidine 174-177 angiotensin I converting enzyme Homo sapiens 33-36 7683654-3 1993 The substrate specificity of the two active sites of ACE was compared using wild-type recombinant ACE and mutants, where one active site is suppressed by deletion or inactivated by mutations of 2 histidines coordinating an essential zinc atom. Histidine 196-206 angiotensin I converting enzyme Homo sapiens 53-56 1316850-1 1992 Angiotensin-I-converting enzyme (ACE) is a peptidyl-dipeptide hydrolase which splits off the dipeptide His-Leu from the decapeptide angiotensin I and thus converts it to angiotensin II. Histidine 103-106 angiotensin I converting enzyme Homo sapiens 0-31 1316850-1 1992 Angiotensin-I-converting enzyme (ACE) is a peptidyl-dipeptide hydrolase which splits off the dipeptide His-Leu from the decapeptide angiotensin I and thus converts it to angiotensin II. Histidine 103-106 angiotensin I converting enzyme Homo sapiens 33-36