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Literature summary for 4.3.3.7 extracted from

  • Burgess, B.R.; Dobson, R.C.; Dogovski, C.; Jameson, G.B.; Parker, M.W.; Perugini, M.A.
    Purification, crystallization and preliminary X-ray diffraction studies to near-atomic resolution of dihydrodipicolinate synthase from methicillin-resistant Staphylococcus aureus (2008), Acta Crystallogr. Sect. F, 64, 659-661.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.3.3.7

Application

Application Comment Organism
pharmacology structure of the enzyme guides the design of novel therapeutics against the methicillin-resistant pathogen Staphylococcus aureus

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 (DE3), pET11a expression vector Staphylococcus aureus

Crystallization (Commentary)

Crystallization (Comment) Organism
X-ray data-collection statistics, best crystal diffracting to beyond 1.45 A resolution Staphylococcus aureus

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus Q6GH13 methicillin-resistent MRSA252 strain
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Staphylococcus aureus MRSA252 Q6GH13 methicillin-resistent MRSA252 strain
-

Purification (Commentary)

Purification (Comment) Organism
gel filtration, SDS-PAGE Staphylococcus aureus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 archetypal subunit orientation in the crystal structure of other dihydrodipicolinate synthase enzymes not observed, structure refinement will provide information regarding the structural evolution of dihydrodipicolinate synthase and the design of antibiotics targeting lysine biosynthesis in Staphylococcus aureus Staphylococcus aureus

Synonyms

Synonyms Comment Organism
MRSA-DHDPS
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 Staphylococcus aureus