Results 1 to 10 of about 308,164 (234)
The CoFactor database: organic cofactors in enzyme catalysis [PDF]
Bioinformatics, 2010 Abstract Motivation: Organic enzyme cofactors are involved in many enzyme reactions. Therefore, the analysis of cofactors is crucial to gain a better understanding of enzyme catalysis. To aid this, we have created the CoFactor database. Results: CoFactor provides a web interface to access hand-curated data extracted from ...
Gemma L. Holliday +2 more
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Biosynthesis of Nitrogenase Cofactors [PDF]
Chemical Reviews, 2020 Nitrogenase harbors three distinct metal prosthetic groups that are required for its activity. The simplest one is a [4Fe-4S] cluster located at the Fe protein nitrogenase component. The MoFe protein component carries an [8Fe-7S] group called P-cluster and a [7Fe-9S-C-Mo-R-homocitrate] group called FeMo-co.
Stefan Burén +3 more
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Peroxisomal Cofactor Transport [PDF]
Biomolecules, 2020 Peroxisomes are eukaryotic organelles that are essential for growth and development. They are highly metabolically active and house many biochemical reactions, including lipid metabolism and synthesis of signaling molecules. Most of these metabolic pathways are shared with other compartments, such as Endoplasmic reticulum (ER), mitochondria, and ...
Anastasija Plett +2 more
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Identification of YdhV as the first molybdoenzyme binding a Bis-Mo-MPT cofactor in escherichia coli [PDF]
, 2019 The oxidoreductase YdhV in Escherichia coli has been predicted to belong to the family of molybdenum/tungsten cofactor (Moco/Wco)-containing enzymes. In this study, we characterized the YdhV protein in detail, which shares amino acid sequence homology ...
Dau, Holger +7 more
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Studies on the changes in protein fluorescence and enzymic activity of aspartate aminotransferase on binding of pyridoxal 5'-Phosphate [PDF]
, 1974 1. The a and ,B subforms of aspartate aminotransferase were purified from pig heart. 2. The a subform contained 2mol of pyridoxal 5'-phosphate. The apo-(a subform) could be fully reactived by combination with 2mol of cofactor. 3.
Evans, RW, Holbrook, J
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Journal of Biological Chemistry, 2013 The transition element molybdenum needs to be complexed by a special cofactor to gain catalytic activity. Molybdenum is bound to a unique pterin, thus forming the molybdenum cofactor (Moco), which, in different variants, is the active compound at the catalytic site of all molybdenum-containing enzymes in nature, except bacterial molybdenum nitrogenase.
openaire +3 more sources
Systems-Based Design of Bi-Ligand Inhibitors of Oxidoreductases: Filling the Chemical Proteomic Toolbox [PDF]
, 2004 Genomics-driven growth in the number of enzymes of unknown function has created a need for better strategies to characterize them. Since enzyme inhibitors have traditionally served this purpose, we present here an efficient systems-based inhibitor design
Baker, Brian +18 more
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The Geometry of the Catalytic Active Site in [FeFe]-hydrogenases is Determined by Hydrogen Bonding and Proton Transfer [PDF]
, 2019 [FeFe]-hydrogenases are efficient metalloenzymes that catalyze the oxidation and evolution of molecular hydrogen, H2. They serve as a blueprint for the design of synthetic H2-forming catalysts.
Apfel, Ulf-Peter +11 more
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Driven cofactor systems and Hamilton-Jacobi separability [PDF]
, 2011 This is a continuation of the work initiated in a previous paper on so-called driven cofactor systems, which are partially decoupling second-order differential equations of a special kind.
Benenti S +7 more
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Nutrient cross-feeding in the microbial world. [PDF]
, 2014 The stability and function of a microbial community depends on nutritional interactions among community members such as the cross-feeding of essential small molecules synthesized by a subset of the population.
Seth, Erica C, Taga, Michiko E
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