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We screened various thermophiles for  meso -diaminopimelate dehydrogenase ( meso -DAPDH, EC 1.4.1.16), which catalyzes the NAD(P)-dependent oxidative deamination of  meso -diaminopimelate, and found the enzyme in a thermophilic bacterium isolated from compost in Japan. The bacterium grew well aerobically at around 55°C and was identified as  Ureibacillus thermosphaericus  strain A1. We purified the enzyme about 47-fold to homogeneity from crude cell extract using five successive purification steps. The molecular mass of the purified protein was about 80 kDa, and the molecule consists of a homodimer with the subunit molecular mass of about 40 kDa. The optimum pH and temperature for the catalytic activity of the enzyme are about 10.5 and 65°C, respectively. The enzyme is highly selective for  meso -diaminopimelate as the electron donor, and NADP but not NAD can serve as the electron acceptor. The  K  m  values for  meso -diaminopimelate and NADP at 50°C and pH 10.5 are 1.6 mM and 0.13 mM, respectively. The nucleotide sequence of this  meso -DAPDH gene encodes a 326-amino acid peptide. When the gene was cloned and overexpressed in  Escherichia coli  Rosetta (DE3), the specific activity in the crude extract of the recombinant cells was about 18.0-fold higher than in the extract from  U. thermosphaericus  strain A1. This made more rapid and simpler purification of the enzyme possible.

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Highly stable meso-diaminopimelate dehydrogenase from an Ureibacillus thermosphaericus strain A1 isolated from a Japanese compost: purification, characterization and sequencing