The universally conserved enzyme CTP synthase (CTPS) forms filaments in bacteria and eukaryotes. In bacteria, polymerization inhibits CTPS activity and is required for nucleotide homeostasis. Here we ...

This work presents a physical model that explains the effects of electric fields on high-valent Fe–oxo heme protein reactivity, attributing these effects to shifts in the energy levels of reactant ...

Once taken out of the active sites, the same functional groups used by enzymes for catalysis tend to lose their "magical" catalytic power in small-molecule enzyme models. We report a small-molecule ...

Enzymes belonging to acyl:CoA synthetase (ACS) superfamily activate wide variety of substrates and play major role in increasing the structural and functional diversity of various secondary ...

Proceedings of the National Academy of Sciences of the United States of America, Vol. 82, No. 8 (Apr. 15, 1985), pp. 2272-2276 (5 pages) We have replaced the glutamic acid-165 at the active site of ...

The goal of rational computer-aided enzyme design is hampered by the lack of knowledge of the maximum possible rate enhancement. We address this problem by considering the enzyme DhlA, which is ...

A research team believes it has solved a long-standing controversy in the field of bioinorganic chemistry about the identity and location of metal atoms in a key methane-oxidizing metalloenzyme ...

Natural enzymes have an exquisite ability to selectively and efficiently catalyze biochemical processes. Scientists have a great interest in harnessing that ability and putting these protein catalysts ...

Different enzymes contain up to 20 different amino acids linked together to form a chain which then folds into the globular enzyme shape. Enzymes have active sites which only match specific substrates ...

Creative Commons (CC): This is a Creative Commons license. Attribution (BY): Credit must be given to the creator. Despite the demonstrable dependence of enzyme functionality on solvation, the notion ...

Protein misfolding is recognized as an important pathophysiological cause of protein deficiency in many genetic disorders. Inherited mutations can disrupt native protein folding, thereby producing ...