PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10388847-0 1999 Catalytic role of the active site histidine of porcine pancreatic phospholipase A2 probed by the variants H48Q, H48N and H48K. Histidine 34-43 phospholipase A2 group IB Homo sapiens 66-82 19003116-0 2002 Possible involvement of phospholipase A(2) and cyclooxygenase in stimulatory action of L-histidine on protein synthesis in L6 myotubes. Histidine 87-98 phospholipase A2 group IB Homo sapiens 24-61 19003116-4 2002 These results suggest an involvement of phospholipase A(2) and cyclooxygenase in the stimulatory action of L-histidine on protein synthesis in L6 myotubes. Histidine 107-118 phospholipase A2 group IB Homo sapiens 40-77 12609879-2 2003 A snake-venom PLA(2) was completely inhibited by covalent modification of the catalytic histidine 48 by p-bromophenacyl bromide. Histidine 88-97 phospholipase A2 group IB Homo sapiens 14-20 7929350-5 1994 We have examined by site-specific mutagenesis of a recombinant PLA2 that is identical to an enzyme in human synovial fluid (containing His-6, Arg-7, Lys-10, and Lys-15 and a global net charge of +15) the role of basic residues in this region in PLA2 action against PLA-deficient (pldA-) E. coli. Histidine 135-138 phospholipase A2 group IB Homo sapiens 63-67 8605210-0 1996 Active site of bee venom phospholipase A2: the role of histidine-34, aspartate-64 and tyrosine-87. Histidine 55-64 phospholipase A2 group IB Homo sapiens 25-41 8605210-1 1996 In bee venom phospholipase A2, histidine-34 probably functions as a Bronsted base to deprotonate the attacking water. Histidine 31-40 phospholipase A2 group IB Homo sapiens 13-29 2555283-15 1989 The mechanisms by which arginine- and histidine-rich polyelectrolytes activate the respiratory burst in neutrophils might involve interaction with G-proteins, the activation of arachidonic acid metabolism and phospholipase A2, or the interaction with myeloperoxidase. Histidine 38-47 phospholipase A2 group IB Homo sapiens 209-225 1567910-8 1992 In the present study we investigated the interaction of native PLA2 and of an inactive PLA2 in which the active site residue His-48 has been modified by alkylation with 1-bromo-2-octanone, with pure micelles of several of these inhibitors in both enantiomeric forms by means of ultraviolet difference absorption spectroscopy. Histidine 125-128 phospholipase A2 group IB Homo sapiens 87-91 1898340-7 1991 This might accompany a change in the configuration around His-48 of the phospholipase A2 subunit. Histidine 58-61 phospholipase A2 group IB Homo sapiens 72-88 3103690-4 1987 We now confirm the involvement of serine and histidine in catalysing the phospholipase A2 action of lecithin-cholesterol acyltransferase by demonstrating the inhibition of this activity by phenylboronic acid (Ki = 1.23 mM) and m-aminophenylboronic acid (Ki = 2.32 mM), inhibitors of known serine/histidine hydrolases. Histidine 45-54 phospholipase A2 group IB Homo sapiens 73-89 3700425-5 1986 Modification of 1 serine residue with phenylmethanesulfonyl fluoride or 1 histidine residue with diethyl pyrocarbonate inhibited cholesteryl ester formation and phospholipase A2 activity. Histidine 74-83 phospholipase A2 group IB Homo sapiens 161-177 6848515-8 1983 Similar His-Asp pairs have been observed in the serine proteases, thermolysin, and phospholipase A2, and the His-Asp pair may play a similar functional role in all of these enzymes. Histidine 8-11 phospholipase A2 group IB Homo sapiens 83-99 6848515-8 1983 Similar His-Asp pairs have been observed in the serine proteases, thermolysin, and phospholipase A2, and the His-Asp pair may play a similar functional role in all of these enzymes. Histidine 109-112 phospholipase A2 group IB Homo sapiens 83-99 1091-6 1975 The most striking differences were the loss of one histidine and one methionine in the isoenzyme, corresponding to residues 24 and 27, respectively, in alpha-phospholipase A2. Histidine 51-60 phospholipase A2 group IB Homo sapiens 158-174 19461-0 1977 Spectral perturbations of the histidine and tryptophan in cobra venom phospholipase A2 upon metal ion and mixed micelle binding. Histidine 30-39 phospholipase A2 group IB Homo sapiens 70-86 32340168-2 2020 However, it has recently been documented that a radical intermediate formed during carbon monoxide release from ruthenium (Ru)-based CORM (CORM-2) interacts with histidine and can inactivate bee phospholipase A2 activity. Histidine 162-171 phospholipase A2 group IB Homo sapiens 195-211 4856505-0 1974 Histidine at the active site of phospholipase A2. Histidine 0-9 phospholipase A2 group IB Homo sapiens 32-48 25230085-1 2014 Within the phospholipase A2 (PLA2) superfamily, secreted PLA2 (sPLA2) enzymes comprise the largest family that contains 11 to 12 mammalian isoforms with a conserved His-Asp catalytic dyad. Histidine 165-168 phospholipase A2 group IB Homo sapiens 11-27 31679116-9 2020 Exposure of PLA2 to a Ru-based CORM in the presence of histidine-rich human albumin resulted in loss of inhibition of PLA2. Histidine 55-64 phospholipase A2 group IB Homo sapiens 12-16 31679116-9 2020 Exposure of PLA2 to a Ru-based CORM in the presence of histidine-rich human albumin resulted in loss of inhibition of PLA2. Histidine 55-64 phospholipase A2 group IB Homo sapiens 118-122 31679116-10 2020 Ru-based CORM likely inhibit bee venom PLA2 anticoagulant activity via formation of reactive Ru species that bind to histidine residues of the enzyme. Histidine 117-126 phospholipase A2 group IB Homo sapiens 39-43 25230085-1 2014 Within the phospholipase A2 (PLA2) superfamily, secreted PLA2 (sPLA2) enzymes comprise the largest family that contains 11 to 12 mammalian isoforms with a conserved His-Asp catalytic dyad. Histidine 165-168 phospholipase A2 group IB Homo sapiens 29-33 25230085-1 2014 Within the phospholipase A2 (PLA2) superfamily, secreted PLA2 (sPLA2) enzymes comprise the largest family that contains 11 to 12 mammalian isoforms with a conserved His-Asp catalytic dyad. Histidine 165-168 phospholipase A2 group IB Homo sapiens 57-61 18989812-6 2008 Our central idea was to inhibit the PLA(2) and Mel activities through histidine alkylation and or tryptophan oxidation (with pbb, para-bromo-phenacyl bromide, and/or NBS- N-bromosuccinimide, respectively) to make their encapsulations possible within stabilized liposomes. Histidine 70-79 phospholipase A2 group IB Homo sapiens 36-42 23022039-2 2013 More than one third of the mammalian PLA(2) enzymes belong to the secreted PLA(2) (sPLA(2)) family, which consists of low molecular mass, Ca(2+)-requiring enzymes with a His-Asp catalytic dyad. Histidine 170-173 phospholipase A2 group IB Homo sapiens 37-43 23022039-2 2013 More than one third of the mammalian PLA(2) enzymes belong to the secreted PLA(2) (sPLA(2)) family, which consists of low molecular mass, Ca(2+)-requiring enzymes with a His-Asp catalytic dyad. Histidine 170-173 phospholipase A2 group IB Homo sapiens 75-81 19118607-2 2009 Modification of His-48 (according to the sequence alignment with porcine pancreatic PLA(2)) with p-bromophenacyl bromide (BPB) caused over 99.9% drop in enzymatic activity Naja naja atra PLA(2). Histidine 16-19 phospholipase A2 group IB Homo sapiens 84-90 19118607-2 2009 Modification of His-48 (according to the sequence alignment with porcine pancreatic PLA(2)) with p-bromophenacyl bromide (BPB) caused over 99.9% drop in enzymatic activity Naja naja atra PLA(2). Histidine 16-19 phospholipase A2 group IB Homo sapiens 187-193