Results 61 to 70 of about 23,761 (232)

Optimizing Group Transfer Catalysis by Copper Complex with Redox-Active Ligand in an Entatic State

open access: yesiScience, 2020
Summary: Metalloenzymes use earth-abundant non-noble metals to perform high-fidelity transformations in the biological world. To ensure chemical efficiency, metalloenzymes have acquired evolutionary reactivity-enhancing tools.
Yufeng Ren   +8 more
doaj   +1 more source

New isoxazolidinyl-based N-alkylethanolamines as new activators of human brain carbonic anhydrases

open access: yesJournal of Enzyme Inhibition and Medicinal Chemistry, 2023
Carbonic anhydrases (CAs) are widespread metalloenzymes which catalyse the reversible hydration of carbon dioxide (CO2) to bicarbonate (HCO3−) and a proton, relevant in many physiological processes. In the last few years, the involvement of CA activation
Doretta Cuffaro   +6 more
doaj   +1 more source

Iron conservation by reduction of metalloenzyme inventories in the marine diazotroph Crocosphaera watsonii [PDF]

open access: yes, 2010
The marine nitrogen fixing microorganisms (diazotrophs) are a major source of nitrogen to open ocean ecosystems and are predicted to be limited by iron in most marine environments.
Bertrand, Erin M.   +8 more
core   +2 more sources

Searching for novel carbonic anhydrase inhibitors: from virtual screening to the lab bench [PDF]

open access: yes, 2013
Carbonic Anhydrases (CAs) are zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide to bicarbonate both in prokaryotes and eukaryotes.
Cadoni, Roberta   +8 more
core  

Designed evolution of artificial metalloenzymes: protein catalysts made to order [PDF]

open access: yes, 2007
Artificial metalloenzymes based on biotin–streptavidin technology, a fusion of chemistry and biology, illustrate how asymmetric catalysts can be improved and evolved using chemogenetic ...
Creus, Marc, Ward, Thomas R.
core   +1 more source

Designing Hydrolytic Zinc Metalloenzymes

open access: yesBiochemistry, 2014
Zinc is an essential element required for the function of more than 300 enzymes spanning all classes. Despite years of dedicated study, questions regarding the connections between primary and secondary metal ligands and protein structure and function remain unanswered, despite numerous mechanistic, structural, biochemical, and synthetic model studies ...
Zastrow, Melissa L.   +1 more
openaire   +2 more sources

Biochemical, kinetic, and spectroscopic characterization of Ruegeria pomeroyi DddW - A mononuclear iron-dependent DMSP lyase [PDF]

open access: yes, 2015
The osmolyte dimethylsulfoniopropionate (DMSP) is a key nutrient in marine environments and its catabolism by bacteria through enzymes known as DMSP lyases generates dimethylsulfide (DMS), a gas of importance in climate regulation, the sulfur cycle, and ...
Brummett, Adam E   +4 more
core   +5 more sources

Amino Acids as Building Blocks for Carbonic Anhydrase Inhibitors

open access: yesMetabolites, 2018
Carbonic anhydrases (CAs) are a superfamily of metalloenzymes widespread in all life, classified into seven genetically different families (α–θ).
Niccolò Chiaramonte   +3 more
doaj   +1 more source

Novel 3-(6-methylpyridin-2-yl)coumarin-based chalcones as selective inhibitors of cancer-related carbonic anhydrases IX and XII endowed with anti-proliferative activity

open access: yesJournal of Enzyme Inhibition and Medicinal Chemistry, 2022
Carbonic anhydrases (CAs) are one of the promising targets for the development of anticancer agents. CA isoforms are implicated in various physiological processes and are expressed in both normal and cancerous cells.
Haytham O. Tawfik   +7 more
doaj   +1 more source

Artificial metalloenzymes : proteins as hosts for enantioselective catalysis [PDF]

open access: yes, 2005
Enantioselective catalysis is one of the most efficient ways to synthesize high-added-value enantiomerically pure organic compounds. As the subtle details which govern enantioselection cannot be reliably predicted or computed, catalysis relies more and ...
Thomas, Christophe M., Ward, Thomas R.
core   +1 more source

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