Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.1.8 (cholinesterase)
 12,691 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Plasma pseudocholinesterase and porcine liver esterase were used to catalyse the incorporation of the stable isotope oxygen-18 into the carboxyl moiety of lipoxygenase metabolites of arachidonic acid. This simple method produces eicosanoid products containing two oxygen-18 atoms; but the enzymes studied were found to display large substrate specificity in the efficiencies at which oxygen-18 could be incorporated into the lipoxygenase metabolites. Furthermore, [18O2]LTB4 was found not to back exchange during in vitro incubation with human neutrophils. The methods involved for stable isotope incorporation are simple, efficient and produce highly enriched species in a short time. By varying the type of esterase, the amount of esterase or the length of incubation highly enriched species of all eicosanoids tested could be prepared.
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PMID:Preparation of oxygen-18-labeled lipoxygenase metabolites of arachidonic acid. 300 15

Two new lignans trivially named negundins A (1) and B (2), were isolated along with (+)-diasyringaresinol (3), (+)-lyoniresinol (4), vitrofolal E (5) and vitrofolal F (6), reported for the first time from this species. The structures of the new compounds were established through spectral studies. Compound 2 showed potent inhibitory activity against lipoxygenase enzyme, while 5 showed moderate activity against butyryl-cholinesterase.
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PMID:Enzyme inhibiting lignans from Vitex negundo. 1552 May 11

A series of variably substituted chalcones were synthesized by condensation of substituted acetophenones with mono-, di- or trisubstituded benzaldehydes. It was observed that some of these compounds have the potential to inhibit acetylcholinesterase, whereas others show activity against butyrylcholinesterase, depending on the substitution pattern at the two aromatic rings of these chalcones. Similarly, lipoxygenase was inhibited by two of these compounds. It has been observed that inhibition of the three enzymes was concentration dependent with the IC50 values ranging from 28.2-134.5 microM against acetylcholinesterase, 16.0-23.1 microM against butyrylcholinesterase and 57.6-71.7 microM against lipoxygenase, respectively.
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PMID:Synthesis and inhibitory potential towards acetylcholinesterase, butyrylcholinesterase and lipoxygenase of some variably substituted chalcones. 1589 83

Twenty two crude ethanolic extracts from 14 indigenous medicinal plants were subjected to enzyme inhibition screening against acetylcholinesterase (AChE), butyrylcholinesterase (BChE) and lipoxygenase enzymes (LO). Three extracts showed activity against AChE, nine extracts were found to be active against BChE and four extracts inhibited the enzyme LO. The most significant inhibition activities (> or =50%) were found in extracts derived from Aloe vera (leaves), Alpinia galanga (rhizome), Curcuma longa (rhizome), Cymbopogon citratus (leaves), Ocimum americanum (leaves), Ocimum americanum (stem) and Withania somnifera (roots).
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PMID:In vitro enzyme inhibition activities of crude ethanolic extracts derived from medicinal plants of Pakistan. 1601 Aug 21

In vitro enzymes inhibition activities of the crude methanolic extract and various fractions of Colchicum luteum Baker (Liliaceae) including chloroform, ethyl acetate, n-butanol and aqueous were carried out against actylcholinesterase, butyrylcholinesterase, lipoxygenase and urease enzymes. A significant enzyme inhibition activity (89%) is shown by the crude methanolic extract and its fractions against lipoxygenase, while low to significant activity (32-75%) was evident against butyrylcholinesterase. The crude methanolic extract and its various fractions demonstrated low activity (29-61%) against acetylcholinesterase and no activity against urease.
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PMID:Inhibition activities of Colchicum luteum baker on lipoxygenase and other enzymes. 1705 79

Four new pterocarpans, atricarpan A (=(-)-1,2-dihydroxy-4-(hydroxymethyl)-3,9-dimethoxypterocarpan; 1), atricarpan B (=(-)-2,3-ethylenedioxy)-1,4-dihydroxy-9-methoxypterocarpan; 2), atricarpan C (=(-)-1,9-dimethoxypterocarpan-3-carboxylic acid; 3), and atricarpan D (=(-)-2,9-dimethoxy-4-(5-oxohexyl)pterocarpan; 4) were isolated from the BuOH extract of the whole plant of Zygophyllum eurypterum. The structure elucidations of those compounds were based primarily on 1D- and 2D-NMR analysis, including COSY, HMBC, and HMQC correlations. Compounds 1-4 also inhibited butyrylcholinesterase (BChE; EC 3.1.1.8) enzyme in a concentration-dependent manner with IC(50) values between 12.5-65.0 microM. Similarly, compounds 1 and 4 inhibited lipoxygenase (LOX; EC 1.13.11.12) and acetylcholinesterase (AChE; EC 3.1.1.7) enzymes with IC50 values of 13.5 and 20.5 muM, respectively.
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PMID:Isolation of four new pterocarpans from Zygophyllum eurypterum (Syn. Z. atriplicoides) with enzyme-inhibition properties. 1719 32

Bractin A (=(2S,3S,4R,5E)-2-{[(2R)-2-hydroxydodecanoyl]amino}triacont-5-ene-1,3,4-triol; 1) and bractin B (=(2S,3S,4R,5E,8E)-2-{[(2R)-2-hydroxyhexacosanoyl]amino}pentadeca-5,8-diene-3,4,15-triol 1-O-beta-D-glucopyranoside; 2), new sphingolipids, and bractic acid (=(5Z,10Z,15Z)-2-decyl-4,7,8,12,13,17,18-heptahydroxy-20,23-dioxopentacosa-5,10,15-trienoic acid; 3), a long-chain polyhydroxy acid, were isolated from the whole plant Ajuga bracteosa along with four known diterpenoids 4-7. Their structures were deduced by spectral studies including 1D- and 2D-NMR spectroscopy. Compounds 1-3 displayed inhibitory potential against enzyme lipoxygenase, while compounds 4-7 inhibited cholinesterase enzymes in a concentration-dependent manner with IC(50) values in the range 10.0-33.0, 14.0-35.2, and 10.0-19.0 microM for lipoxygenase, acetylcholinesterase, and butyrylcholinesterase, respectively. Lineweaver-Burk, and Dixon plots, and their secondary replots indicated that all compounds exhibit non-competitive type of inhibition with K(i) values in the range of 9.5-35.2, 15.2-36.0, and 11.6-20.5 microM, for lipoxygenase, acetylcholinesterase, and butyrylcholinesterase, respectively.
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PMID:Isolation and enzyme-inhibition studies of the chemical constituents from Ajuga bracteosa. 1725 36

The crude methanolic extract and various fractions of Andrachne cardifolia Muell, including chloroform, ethyl acetate and n-butanol fractions were subjected to in vitro enzyme inhibition activity against acetylcholinesterase, butyrylcholinesterase, lipoxygenase and urease enzymes. A significant enzyme inhibition activity (40-89%) was shown by the crude methanolic extract and its fractions against lipoxygenase, while low to significant activity (40-71%) against butyrylcholinesterase. The crude methanolic extract and its various fractions demonstrated poor to significant activity (25-73%) against acetylcholinesterase and no activity against urease.
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PMID:Enzyme inhibition activities of Andrachne cardifolia Muell. 1751 51

An alcoholic extract obtained from the rhizomes of Gloriosa superba Linn (Colchicaceae) was screened for enzyme inhibition activities. The crude extract and its subsequent fractions including chloroform, ethyl acetate, n-butanol and aqueous were screened against lipoxygenase, actylcholinesterase, butyrylcholinesterase and urease. An outstanding inhibition on lipoxygenase was observed. The highest enzyme inhibition potency was expressed by the chloroform fraction (90%) among the tested fractions on lipoxygenase. Overall 67-90% inhibition was found for lipoxygenase, 46-69% for acetylcholinesterase and 10-33% for butyrylcholinesterase, while urease was not inhibited.
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PMID:Enzyme inhibition activities of the extracts from rhizomes of Gloriosa superba Linn (Colchicaceae). 1823 25

The crude methanolic extract and chloroform, ethyl acetate and n-butanol fractions of Teucrium royleanum were examined as inhibitors of actylcholinesterase, butyrylcholinesterase, lipoxygenase and urease. A significant enzyme inhibition activity (52-83%) was shown by the crude methanolic extract and its fractions against acetylcholinesterase, while low to outstanding enzyme inhibitory activity was shown (19-93%) against butyrylcholinesterase. The crude methanolic extract and its various fractions demonstrated low activity against lipoxygenase and inactive against urease.
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PMID:Enzyme inhibition activities of Teucrium royleanum. 1823 27


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