Results 111 to 120 of about 3,170 (164)
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Glucono-δ-lactonase from Escherichia coli
Biochimica et Biophysica Acta (BBA) - Enzymology, 1972Escherichia coli K12 has been shown to contain a glucono-δ-lactonase (d-glucono-δ-lactone hydrolase, EC 3.1.1.17). A convenient assay has been developed which is based on the spectral change of a pH indicator during the hydrolysis of the lactone. The enzyme has been purified about 105-fold. Its substrate specificity has been investigated. The enzyme is
F, Hucho, K, Wallenfels
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PON1 lactonase activity and its association with cardiovascular disease
Clinica Chimica Acta, 2020Paraoxonase 1 (PON1) is important in the development of atherosclerosis, and it has become the subject of intensive research. Our aim was to evaluate the association of serum PON1 activity and polymorphisms with cardiovascular disease (CVD) using four different substrates.Activity of PON1-related to arylesterase (AREase and 4-CMPAse), paraoxonase ...
Mike Mackness, A E Rojas-Garcia
exaly +3 more sources
Structural Basis for Natural Lactonase and Promiscuous Phosphotriesterase Activities
Journal of Molecular Biology, 2008Organophosphates are the largest class of known insecticides, several of which are potent nerve agents. Consequently, organophosphate-degrading enzymes are of great scientific interest as bioscavengers and biodecontaminants. Recently, a hyperthermophilic phosphotriesterase (known as SsoPox), from the Archaeon Sulfolobus solfataricus, has been isolated ...
Giuseppe Manco +2 more
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Studies on the enantioselectivity of bacterial lactonases
2022Owing to their biological significance, increased efforts are being directed towards the production of lactones in optically pure form. One method of synthesis is via a microbial equivalent of the Baeyer-Villiger reaction. This reaction is common in microorganisms possessing a monooxygenase enzyme which is induced as part of the catabolic machinery ...
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Hyperthermophilic phosphotriesterases/lactonases for the environment and human health
Environmental Technology, 2010In the last decades the idea to use enzymes for environmental bioremediation has been more and more proposed and, in the light of this, new solutions have been suggested and detailed studies on some classes of enzymes have been performed. In particular, our attention in the last few years has been focused on the enzymes belonging to the amidohydrolase ...
Mandrich L, Merone L, Manco G
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The degradation of mefrusid the participation of a “lactonase” in drug metabolism
Biochimica et Biophysica Acta (BBA) - General Subjects, 1972Abstract The metabolite of the diuretic Mefrusid, the lactone II, is an a reversible equilibrium with the corresponding open acid form III. The equilibrium is pH dependent and at pH 7.3 the acid form is strongly favoured (90%). However, between pH 7 and 8 at room or body temperature in the absence of enzymes the equilibrium is formed only very slowly.
J, Pütter, K, Schlossmann
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Induction of glucose oxidase, catalase, and lactonase in Aspergillus niger
Current Genetics, 1993The induction of glucose oxidase, catalase, and lactonase activities was studied both in wild-type and in glucose oxidase regulatory and structural mutants of Aspergillus niger. The structural gene for glucose oxidase was isolated and used for Northern analysis and in transformation experiments using various gox mutations.
Witteveen, C.F.B. +7 more
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1975
Publisher Summary This chapter discusses the assay and purification procedure of actinomycin lactonase. The enzyme catalyzes the conversion of a neutral molecule to an acidic compound. The assay is based upon the use of radioactive actinomycin. Both product and substrate are extracted from the reaction mixture with an organic solvent at an acid pH ...
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Publisher Summary This chapter discusses the assay and purification procedure of actinomycin lactonase. The enzyme catalyzes the conversion of a neutral molecule to an acidic compound. The assay is based upon the use of radioactive actinomycin. Both product and substrate are extracted from the reaction mixture with an organic solvent at an acid pH ...
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Studies on the glucono-δ-lactonase of Psudomonas fluorescens
Biochimica et Biophysica Acta, 1960Abstract The first stage of the oxidative metabolism of d -glucose by Pseudomonas fluorescens is the conversion of d -glucopyranose into d -glucono-δ-lactone. This lactone is hydrolysed to gluconic acid by an enzyme found in the soluble fraction of cell-free extracts of the bacterium. the lactonase has been purified a hundredfold and some of its
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Lactonases with oragnophosphatase activity: Structural and evolutionary perspectives
Chemico-Biological Interactions, 2010Serum paraoxonase (PON1) is well recognized for its ability to hydrolyze arylesters, toxic oxon metabolites of organophosphate insecticides and nerve agents. PON1 is a member of gene family including also PON2 and PON3; however, the later two enzymes have very limited arylesterase and practically no organophosphatase activity.
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