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 …
Synthesis and folding of a mirror-image enzyme reveals ambidextrous chaperone activity
MT Weinstock, MT Jacobsen… - Proceedings of the …, 2014 - National Acad Sciences
Mirror-image proteins (composed of d-amino acids) are promising therapeutic agents and
drug discovery tools, but as synthesis of larger d-proteins becomes feasible, a major …
drug discovery tools, but as synthesis of larger d-proteins becomes feasible, a major …
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 …
The crystal structures of native and (S)-lysine-bound dihydrodipicolinate synthase from Escherichia coli with improved resolution show new features of biological …
Dihydrodipicolinate synthase (DHDPS) mediates the key first reaction common to the
biosynthesis of (S)-lysine and meso-diaminopimelate. The activity of DHDPS is allosterically …
biosynthesis of (S)-lysine and meso-diaminopimelate. The activity of DHDPS is allosterically …
Crystal structure and kinetic study of dihydrodipicolinate synthase from Mycobacterium tuberculosis
G Kefala, GL Evans, MDW Griffin… - Biochemical …, 2008 - portlandpress.com
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 …
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 …
Dihydrodipicolinate synthase: structure, dynamics, function, and evolution
Enzymes are usually comprised of multiple subunits and more often than not they are made
up of identical subunits. In this review we examine lysine biosynthesis and focus on the …
up of identical subunits. In this review we examine lysine biosynthesis and focus on the …
Dihydrodipicolinate synthase from Thermotoga maritima
FG Pearce, MA Perugini, HJ Mckerchar… - Biochemical …, 2006 - portlandpress.com
DHDPS (dihydrodipicolinate synthase) catalyses the branch point in lysine biosynthesis in
bacteria and plants and is feedback inhibited by lysine. DHDPS from the thermophilic …
bacteria and plants and is feedback inhibited by lysine. DHDPS from the thermophilic …
[HTML][HTML] Structural and functional characterization of Staphylococcus aureus dihydrodipicolinate synthase
Lysine biosynthesis is crucial for cell-wall formation in bacteria. Enzymes involved in lysine
biosynthesis are thus potential targets for anti-microbial therapeutics. Dihydrodipicolinate …
biosynthesis are thus potential targets for anti-microbial therapeutics. Dihydrodipicolinate …
Dihydrodipicolinate synthase (DHDPS) from Escherichia coli displays partial mixed inhibition with respect to its first substrate, pyruvate
Dihydrodipicolinate synthase (DHDPS, EC 4.2. 1.52) mediates the first unique reaction of (S)-
lysine biosynthesis in plants and microbes—the condensation of (S)-aspartate-β …
lysine biosynthesis in plants and microbes—the condensation of (S)-aspartate-β …