ArticleExtremophiles : life under extreme conditions2008
Characterization of a thermostable dihydrodipicolinate synthase from Thermoanaerobacter tengcongensis.
Article in Extremophiles : life under extreme conditions, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 21 citations in OpenAlex.
- ColorimetricHeliyon · 2023Article
- Molecular evolution of an oligomeric biocatalyst functioning in lysine biosynthesis.Biophysical reviews · 2018Review
- DHAP-dependent aldolases from (hyper)thermophiles: biochemistry and applications.Extremophiles : life under extreme conditions · 2014Review
- Medicago truncatula dihydrodipicolinate synthase (DHDPS) enzymes display novel regulatory properties.Plant molecular biology · 2013Article
- Substrate-mediated stabilization of a tetrameric drug target reveals Achilles heel in anthrax.The Journal of biological chemistry · 2010Article
- Crystallization and preliminary X-ray analysis of dihydrodipicolinate synthase from Clostridium botulinum in the presence of its substrate pyruvate.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
- Expression, purification, crystallization and preliminary X-ray diffraction analysis of dihydrodipicolinate synthase from Bacillus anthracis in the presence of pyruvate.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
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5 authors at 1 institution in 1 country.
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Abstract
Dihydrodipicolinate synthase (DHDPS) catalyses the first reaction of the (S)-lysine biosynthesis pathway in bacteria and plants. The hypothetical gene for dihydrodipicolinate synthase (dapA) of Thermoanaerobacter tengcongensis was found in a cluster containing several genes of the diaminopimelate lysine-synthesis pathway. The dapA gene was cloned in Escherichia coli, DHDPS was subsequently produced and purified to homogeneity. The T. tengcongensis DHDPS was found to be thermostable (T0.5=3 h at 90 degrees C). The specific condensation of pyruvate and (S)-aspartate-beta -semialdehyde was catalyzed optimally at 80 degrees C at pH 8.0. Enzyme kinetics were determined at 60 degrees C, as close as possible to in vivo conditions. The established kinetic parameters were in the same range as for example E. coli dihydrodipicolinate synthase. The specific activity of the T. tengcongensis DHDPS was relatively high even at 30 degrees C. Like most dihydrodipicolinate synthases known at present, the DHDPS of T. tengcongensis seems to be a tetramer. A structural model reveals that the active site is well conserved. The binding site of the allosteric inhibitor lysine appears not to be conserved, which agrees with the fact that the DHDPS of T. tengcongensis is not inhibited by lysine under physiological conditions.
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