Biochemical and genetic characterization of a novel enzyme of pentitol metabolism: D-arabitol-phosphate dehydrogenase.

@article{Povelainen2003BiochemicalAG,
  title={Biochemical and genetic characterization of a novel enzyme of pentitol metabolism: D-arabitol-phosphate dehydrogenase.},
  author={M. Povelainen and E. Eneyskaya and A. Kulminskaya and D. R. Ivanen and N. Kalkkinen and K. Neustroev and A. N. Miasnikov},
  journal={The Biochemical journal},
  year={2003},
  volume={371 Pt 1},
  pages={
          191-7
        }
}
An enzyme with a specificity that has not been described previously, D-arabitol-phosphate dehydrogenase (APDH), has been purified from cell lysate of Enterococcus avium. SDS/PAGE indicated that the enzyme had a molecular mass of 41+/-2 kDa, whereas a molecular mass of 160+/-5 kDa was observed under non-denaturing conditions, implying that the APDH may exist as a tetramer with identical subunits. Purified APDH was found to have a narrow substrate specificity, converting only D-arabitol 1… Expand
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