publication . Article . 2016

Reconstruction of diaminopimelic acid biosynthesis allows characterisation of Mycobacterium tuberculosis N-succinyl-L,L-diaminopimelic acid desuccinylase.

Christopher Dowson;
Open Access
  • Published: 15 Mar 2016 Journal: Scientific Reports, volume 6 (eissn: 2045-2322, Copyright policy)
  • Publisher: Springer Science and Business Media LLC
  • Country: United Kingdom
Abstract
With the increased incidence of tuberculosis (TB) caused by Mycobacterium tuberculosis there is an urgent need for new and better anti-tubercular drugs. N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE) is a key enzyme in the succinylase pathway for the biosynthesis of meso-diaminopimelic acid (meso-DAP) and L-lysine. DapE is a zinc containing metallohydrolase which hydrolyses N-succinyl L,L diaminopimelic acid (L,L-NSDAP) to L,L-diaminopimelic acid (L,L-DAP) and succinate. M. tuberculosis DapE (MtDapE) was cloned, over-expressed and purified as an N-terminal hexahistidine ((His)6) tagged fusion containing one zinc ion per DapE monomer. We redesigned the D...
Subjects
free text keywords: Multidisciplinary, Histidine, Biology, Biosynthesis, chemistry.chemical_compound, chemistry, Enzyme, chemistry.chemical_classification, Mycobacterium tuberculosis, biology.organism_classification, Zinc, chemistry.chemical_element, Diaminopimelic acid, Oligopeptide, Binding site, Microbiology, Biochemistry, QR, RA, RC, RM, Article
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publication . Article . 2016

Reconstruction of diaminopimelic acid biosynthesis allows characterisation of Mycobacterium tuberculosis N-succinyl-L,L-diaminopimelic acid desuccinylase.

Christopher Dowson;