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Purification and characterization of aminopropionaldehyde dehydrogenase from Arthrobacter sp. TMP-1.

Aminopropionaldehyde dehydrogenase was purified to apparent homogeneity from 1,3-diaminopropane-grown cells of Arthrobacter sp. TMP-1. The native molecular mass and the subunit molecular mass of the enzyme were approximately 20,5000 and 52,000, respectively, suggesting that the enzyme is a tetramer of identical subunits. The apparent Michaelis constant (K(m)) for 1,3-diaminopropane was approximately 3 microM. The enzyme equally used both NAD(+) and NADP(+) as coenzymes. The apparent K(m) values for NAD(+) and NADP(+) were 255 microM and 108 microM, respectively. The maximum reaction rates (V(max)) for NAD(+) and NADP(+) were 102 and 83.3 micromol min(-1) mg(-1), respectively. Some tested aliphatic aldehydes and aromatic aldehydes were inert as substrates. The optimum pH was 8.0-8. 5. The enzyme was sensitive to sulfhydryl group-modifying reagents.[1]

References

  1. Purification and characterization of aminopropionaldehyde dehydrogenase from Arthrobacter sp. TMP-1. Tanaka, K., Matsuno, E., Shimizu, E., Shibai, H., Yorifuji, T. FEMS Microbiol. Lett. (2001) [Pubmed]
 
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