Results 31 to 40 of about 6,120 (217)
Inhibitors of bacterial and plants urease [PDF]
, 2013 Urease is an important virulence factor for Helicobacter pylori and Proteus mirabilis as well as in environmental transformations of certain nitrogenous compounds.
Macegoniuk, Katarzyna
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Frontiers in Microbiology, 2016 Nicotinamidases catalyze the hydrolysis of the amide bond in nicotinamide to produce ammonia and nicotinic acid. These enzymes are an essential component of the NAD+ salvage pathway and are implicated in the viability of several pathogenic organisms. Its
Rubén Zapata-Pérez +4 more
doaj +1 more source
Systematic site-directed mutagenesis to characterize subunit interactions in E. coli asparaginase II, an enzyme [PDF]
, 2005 L-asparaginases (EC 3.5.1.1) catalyze the hydrolysis of L-asparagine to aspartic acid and ammonia. Asparaginases of bacterial origin have been used for over 40 years in the treatment of acute lymphatic leukemia (ALL).
Röhm, Klaus-Heinrich (Prof.) +1 more
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Ureide Catabolism in Soybeans [PDF]
Plant Physiology, 1988 We demonstrate that allantoate is catabolized in soybean seedcoat extracts by an enzyme complex that has allantoate amidohydrolase and ureidoglycolate amidohydrolase activities. Soybean seedcoat extracts released (14)CO(2) from [ureido-(14)C]ureidoglycolate under conditions in which urease is not detectable.
Rodney G. Winkler +2 more
openaire +3 more sources
Structure-guided engineering of molinate hydrolase for the degradation of thiocarbamate pesticides.
PLoS ONE, 2015 Molinate is a recalcitrant thiocarbamate used to control grass weeds in rice fields. The recently described molinate hydrolase, from Gulosibacter molinativorax ON4T, plays a key role in the only known molinate degradation pathway ending in the formation ...
José P Leite +6 more
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Tackling Critical Catalytic Residues in Helicobacter pylori L-Asparaginase
Biomolecules, 2015 Bacterial asparaginases (amidohydrolases, EC 3.5.1.1) are important enzymes in cancer therapy, especially for Acute Lymphoblastic Leukemia. They are tetrameric enzymes able to catalyze the deamination of L-ASN and, to a variable extent, of L-GLN, on ...
Maristella Maggi +3 more
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Current Advances in Ochratoxin A-Degrading Enzymes [PDF]
Shipin KexueOchratoxin A (OTA) poses a serious threat to human and animal health as well as the ecological environment due to its high toxicity, stable physicochemical properties, and widespread occurrence in food and feed.
NIU Zehui, LIANG Zhihong
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Journal of Lipid Research, 2015 Ceramidases catalyze the cleavage of ceramides into sphingosine and fatty acids. Previously, we reported on the use of the RBM14 fluorogenic ceramide analogs to determine acidic ceramidase activity.
Mireia Casasampere +12 more
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Evolutionary expansion of the amidohydrolase superfamily in bacteria in response to the synthetic compounds molinate and diuron [PDF]
, 2015 The amidohydrolase superfamily has remarkable functional diversity, with considerable structural and functional annotation of known sequences. In microbes, the recent evolution of several members of this family to catalyze the breakdown of environmental ...
Carr, Paul D. +8 more
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Effects of pH on the inhibition of fatty acid amidohydrolase by ibuprofen [PDF]
British Journal of Pharmacology, 2001 The pharmacological properties of fatty acid amidohydrolase (FAAH) at different assay pH values were investigated using [3H]‐anandamide ([3H]‐AEA) as substrate in rat brain homogenates and in COS‐7 cells transfected with wild type and mutant FAAH. Rat brain hydrolysis of [3H]‐AEA showed pH dependency with an optimum around pH 8‐9.
Christopher J. Fowler +4 more
openaire +4 more sources