[HTML][HTML] The structural basis of allosteric regulation in proteins
Allosteric regulation of protein function occurs when the regulatory trigger, such as the
binding of a small-molecule effector or inhibitor, takes place some distance from the …
binding of a small-molecule effector or inhibitor, takes place some distance from the …
Inhibition of lysine biosynthesis: an evolving antibiotic strategy
Bacterial biosynthesis of lysine has come under increased scrutiny as a target for novel
antibacterial agents as it provides lysine for protein synthesis and both lysine and meso …
antibacterial agents as it provides lysine for protein synthesis and both lysine and meso …
[HTML][HTML] GroEL/ES chaperonin modulates the mechanism and accelerates the rate of TIM-barrel domain folding
The GroEL/ES chaperonin system functions as a protein folding cage. Many obligate
substrates of GroEL share the (βα) 8 TIM-barrel fold, but how the chaperonin promotes …
substrates of GroEL share the (βα) 8 TIM-barrel fold, but how the chaperonin promotes …
The coordinated action of the enzymes in the L-lysine biosynthetic pathway and how to inhibit it for antibiotic targets
Background Antimicrobial resistance is a global health issue that requires immediate
attention in terms of new antibiotics and new antibiotic targets. The l-lysine biosynthesis …
attention in terms of new antibiotics and new antibiotic targets. The l-lysine biosynthesis …
Structure and evolution of a novel dimeric enzyme from a clinically important bacterial pathogen
BR Burgess, RCJ Dobson, MF Bailey… - Journal of Biological …, 2008 - ASBMB
Dihydrodipicolinate synthase (DHDPS) catalyzes the first committed step of the lysine
biosynthetic pathway. The tetrameric structure of DHDPS is thought to be essential for …
biosynthetic pathway. The tetrameric structure of DHDPS is thought to be essential for …
Evolution of quaternary structure in a homotetrameric enzyme
Dihydrodipicolinate synthase (DHDPS) is an essential enzyme in (S)-lysine biosynthesis
and an important antibiotic target. All X-ray crystal structures solved to date reveal a …
and an important antibiotic target. All X-ray crystal structures solved to date reveal a …
Structural determinants defining the allosteric inhibition of an essential antibiotic target
Dihydrodipicolinate synthase (DHDPS) catalyzes the first committed step in the lysine
biosynthesis pathway of bacteria. The pathway can be regulated by feedback inhibition of …
biosynthesis pathway of bacteria. The pathway can be regulated by feedback inhibition of …
Crystal structure and kinetic study of dihydrodipicolinate synthase from Mycobacterium tuberculosis
The three-dimensional structure of the enzyme dihydrodipicolinate synthase (KEGG entry
Rv2753c, EC 4.2. 1.52) from Mycobacterium tuberculosis (Mtb-DHDPS) was determined and …
Rv2753c, EC 4.2. 1.52) from Mycobacterium tuberculosis (Mtb-DHDPS) was determined and …
Exploring the allosteric mechanism of dihydrodipicolinate synthase by reverse engineering of the allosteric inhibitor binding sites and its application for lysine …
Abstract Dihydrodipicolinate synthase (DHDPS, EC 4.2. 1.52) catalyzes the first committed
reaction of l-lysine biosynthesis in bacteria and plants and is allosterically regulated by l …
reaction of l-lysine biosynthesis in bacteria and plants and is allosterically regulated by l …
Characterisation of the First Enzymes Committed to Lysine Biosynthesis in Arabidopsis thaliana
In plants, the lysine biosynthetic pathway is an attractive target for both the development of
herbicides and increasing the nutritional value of crops given that lysine is a limiting amino …
herbicides and increasing the nutritional value of crops given that lysine is a limiting amino …