Results 71 to 80 of about 180,264 (297)

MacroD1 Is a Promiscuous ADP-Ribosyl Hydrolase Localized to Mitochondria

open access: yesFrontiers in Microbiology, 2018
MacroD1 is a macrodomain containing protein that has mono-ADP-ribose hydrolase enzymatic activity toward several ADP-ribose adducts. Dysregulation of MacroD1 expression has been shown to be associated with the pathogenesis of several forms of cancer.
Thomas Agnew   +5 more
doaj   +1 more source

Purification, Characterization, and Structural Studies of a Sulfatase from Pedobacter yulinensis

open access: yesMolecules, 2021
Sulfatases are ubiquitous enzymes that hydrolyze sulfate from sulfated organic substrates such as carbohydrates, steroids, and flavones. These enzymes can be exploited in the field of biotechnology to analyze sulfated metabolites in humans, such as ...
Caleb R. Schlachter   +5 more
doaj   +1 more source

Xenobiotic-hydrolysing esterases from crops and Arabidopses: characterisation of a S-formylglutathione hydrolase [PDF]

open access: yes, 2003
Esterases represent an ancient family of enzymes, found across all kingdoms, which have diverged and occupied a wide range of functional niches. Because of their biochemical diversity and electrophoretic variability, esterases are widely used as genetic ...
Kordić, Sandra
core  

Discovery and rational engineering of PET hydrolase with both mesophilic and thermophilic PET hydrolase properties: Supplementary information

open access: yes, 2023
Supporting data for "  Discovery and rational engineering of PET hydrolase with both mesophilic and thermophilic PET hydrolase properties". The dataset serves as the supporting information and provides the raw data for the thesis "   Discovery and ...
Jaewon Jang (16468438)   +5 more
core   +1 more source

p190A/ARHGAP35 and p190B/ARHGAP5 proteins in endometrial cancer: a novel cancer‐relevant paralog interplay

open access: yesMolecular Oncology, EarlyView.
This study identifies ARHGAP5, in addition to the frequently mutated ARHGAP35, as significantly mutated in endometrial cancer. Mutations in both genes co‐occur and are associated with their correlated downregulation. Functional CRISPR studies show that both paralogs regulate similar pathways, including actin cytoskeleton organization.
Mathilde Pinault   +12 more
wiley   +1 more source

Identification, Characterization, and Immobilization of an Organic Solvent-Stable Alkaline Hydrolase (PA27) from Pseudomonas aeruginosa MH38

open access: yesMolecules, 2014
An organic solvent-stable alkaline hydrolase (PA27) from Pseudomonas aeruginosa MH38 was expressed, characterized, and immobilized for biotechnological applications.
Eunjin Jang   +2 more
doaj   +1 more source

The crystal structure of the Borrelia burgdorferi nicotinamidase BBE22 resolves a long‐standing annotation error

open access: yesFEBS Open Bio, EarlyView.
The crystal structure of Borrelia burgdorferi nicotinamidase (PncA/BBE22) reveals the correct full‐length protein initiated from a non‐canonical AUU start codon. The structure validates previous biochemical findings and resolves a long‐standing annotation error, demonstrating that the truncated database sequence is structurally incompatible with the ...
Kalvis Brangulis
wiley   +1 more source

Cloning and characterization of the first member of the Nudix family from Arabidopsis thaliana. [PDF]

open access: yes, 2002
The sequence motif commonly called a Nudix box, represented by (GX(5)EX(7)REVXEEXGU) is the marker of a widely distributed family of enzymes that catalyze the hydrolysis of a variety of nucleoside diphosphate derivatives. Here we describe the cloning and
Dobrzanska, Marta   +3 more
core   +1 more source

Identifying and characterising a plant GH1 β‐glucosidase that exhibits hydrolytic activity on N‐linked glucopyranoside

open access: yesFEBS Open Bio, EarlyView.
We report the first β‐glucosidase with demonstrated hydrolytic activity on an N‐linked glycopyranoside. The enzyme, native to maize, was biochemically characterised for this novel reaction, and structural modelling of the enzyme–substrate complex revealed several clues to the underlying reduced catalytic rate relative to its native O‐glycopyranoside ...
Hani Gharabli   +3 more
wiley   +1 more source

Les lipases sont des hydrolases atypiques : principales caractéristiques et applications [PDF]

open access: yesBiotechnologie, Agronomie, Société et Environnement, 2008
ipases are atypical hydrolases: principal characteristics and applications. Due to their kinetic and substrate specificities, triacylglycerol acyl-hydrolases or lipases are atypical enzymes.
Fickers P., Thonart P., Destain J.
doaj  

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