Results 31 to 40 of about 5,211 (236)

Diagnosis of dihydropyrimidinase deficiency in a Chinese boy with dihydropyrimidinuria [PDF]

open access: yes, 2013
published_or_final_versio
Lam, CW   +5 more
core   +1 more source

Omics-driven identification and elimination of valerolactam catabolism in Pseudomonas putida KT2440 for increased product titer. [PDF]

open access: yes, 2019
Pseudomonas putida is a promising bacterial chassis for metabolic engineering given its ability to metabolize a wide array of carbon sources, especially aromatic compounds derived from lignin.
Baidoo, Edward EK   +13 more
core   +4 more sources

Structure-guided engineering of molinate hydrolase for the degradation of thiocarbamate pesticides.

open access: yesPLoS 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
doaj   +1 more source

Combined whole-cell high-throughput functional screening for identification of new nicotinamidases/pyrazinamidases in metagenomic/polygenomic libraries

open access: yesFrontiers 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]

open access: yes, 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
core   +1 more source

Tackling Critical Catalytic Residues in Helicobacter pylori L-Asparaginase

open access: yesBiomolecules, 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
doaj   +1 more source

Stereochemical aspects of the nucleophilic attack in different classes of l-asparaginases

open access: yesIUCrJ
L-Asparaginases hydrolyze L-asparagine to L-aspartate with the release of ammonia. Currently, three completely unrelated structural classes of L-asparaginases are known, further subdivided into five types.
Miroslaw Gilski   +2 more
doaj   +1 more source

Current Advances in Ochratoxin A-Degrading Enzymes [PDF]

open access: yesShipin Kexue
Ochratoxin 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
doaj   +1 more source

Dali server update [PDF]

open access: yes, 2016
The Dali server (http://ekhidna2.biocenter.helsinki.fi/dali) is a network service for comparing protein structures in 3D. In favourable cases, comparing 3D structures may reveal biologically interesting similarities that are not detectable by comparing ...
Holm, Liisa, Laakso, Laura M.
core   +2 more sources

Activity of neutral and alkaline ceramidases on fluorogenic N-acylated coumarin-containing aminodiols

open access: yesJournal 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
doaj   +1 more source

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