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Anandamide Amidohydrolase from Porcine Brain

1997
Ethanolamide of arachidonic acid was isolated from porcine brain as an endogenous ligand for cannabinoid receptors, and referred to as anandamide.1 In consideration of various biological activities of anandamide,2 it is very important to elucidate how the production and degradation of this new compound are regulated by enzymes within the cells.
Shozo Yamamoto   +3 more
openaire   +2 more sources

Distribution and characterization of anandamide amidohydrolase in mouse brain and liver

Life Sciences, 1998
Anandamide (N-Arachidonoylethanolamine) amidohydrolase catalyzing hydrolysis of anandamide was characterized in mice. The enzymatic activity was highest in the liver, followed by the brain and testis. Negligible activity was found in heart, lung and spleen. The activity in brain and liver was mainly localized in the microsomal fractions.
Ikuo Yamamoto   +6 more
openaire   +3 more sources

Partial purification and characterization of an amidohydrolase from soybean

Phytochemistry, 1969
Abstract A soluble enzyme with amidohydrolase activity was isolated from the roots of soybean seedlings and purified 45-fold by ammonium sulfate fractionation, gel filtration and cellulose ion-exchange chromatography. The enzyme hydrolyzed primarily N α -benzoyl- dl -arginine p -nitroanilide and to a slight extent the p -nitroanilides of glycine ...
G. Graf, Robert E. Hoagland
openaire   +2 more sources

Effects of Acidity and Alkalinity on the Stability of Amidohydrolases in Freshwater

Journal of Environmental Quality, 1983
AbstractThe influence of acidity and alkalinity on the enzymatic hydrolysis of amide‐N in the aquatic system was investigated by determining the stability of L‐asparaginase (EC [Enzyme Commission] 3.5.1.1). L‐glutaminase (EC 3.5.1.2), and amidase (EC 3.5.1.4), and urease (EC 3.5.1.5) with respect to pH in three freshwater lakes.
A. L. Page, W. T. Frankenberger
openaire   +2 more sources

Identification of Caerulomycin A Gene Cluster Implicates a Tailoring Amidohydrolase

Organic Letters, 2012
The biosynthetic gene cluster for caerulomycin A (1) was cloned and characterized from the marine actinomycete Actinoalloteichus cyanogriseus WH1-2216-6, which revealed an unusual hybrid polyketide synthase (PKS)/nonribosomal peptide synthetase (NRPS) system.
Weiming Zhu   +8 more
openaire   +3 more sources

Penicillin amidohydrolase productivity of locally isolated bacterial species

Folia Microbiologica, 1991
Penicillin amidohydrolase productivity of four locally isolated bacterial species is described. Organisms were identified as Escherichia coli, Pseudomonas aeruginosa, Sarcina lutea and Bacillus megaterium. Highest enzyme productivity of 3.2 U/mL with a corresponding dry cell mass of 4.5 g/L was recorded from S. lutea.
D. Shaikh, S M S Zoha, Z. A. Mahmood
openaire   +3 more sources

Stabilization of Penicillin Amidohydrolase Immobilized on Eupergit C

1982
Carrier bound enzymes are playing an increasing important role in industrial production, in part through development of carriers with good filtration properties and high loading capacity. Economically it is important how often one can reuse carrier bound enzymes. Therefore, we have looked at higher stability under repeated use. Since dithiols are known
K. Sauber, D. M. Kramer
openaire   +2 more sources

Penicillin acylases as amidohydrolases and acyl transfer catalysts

Biotechnology Letters, 1981
The hypothesis that an acyl-enzyme intermediate of the esterases from Xanthomonas citri and Acetobacter turbidans is reponsible for the acylation of 7-aminodeacetoxycephalosporanic acid and similar compounds by esters of amino acids, recently proposed by Kato, also accounts for the kinetics of hydrolysis of penicillin G by the amidohydrolase from E ...
openaire   +2 more sources

A fluorescence lifetime-based binding assay for acetylpolyamine amidohydrolases from Pseudomonas aeruginosa using a [1,3]dioxolo[4,5-f][1,3]benzodioxole (DBD) ligand probe

Analytical and Bioanalytical Chemistry, 2014
C. Meyners   +5 more
semanticscholar   +1 more source

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