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

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...

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Autori principali: Akita, Hironaga, Fujino, Yasuhiro, Doi, Katsumi, Ohshima, Toshihisa
Natura: Artigo
Lingua:Inglês
Pubblicazione: Springer 2011
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Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC3293039/
https://ncbi.nlm.nih.gov/pubmed/22117688
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1186/2191-0855-1-43
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