A novel NADP⁺-dependent l-1-amino-2-propanol dehydrogenase from Rhodococcus erythropolis MAK154: a promising enzyme for the production of double chiral aminoalcohols

Abstract

Aim: A novel NADP+‐dependent l‐1‐amino‐2‐propanol dehydrogenase was isolated from Rhodococcus erythropolis MAK154, and characterized. Methods and Results: The enzyme was inducibly produced on cultivation with aminoalcohols such as 1‐amino‐2‐propanol, 1‐amino‐2‐butanol and 2‐aminocyclohexanol. The enzyme catalyses the NADP+‐dependent oxidation of several aminoalcohols, and also the NADPH‐dependent asymmetric reduction of an aminoketone compound to a double chiral aminoalcohol, d‐pseudoephedrine. Amino acid sequence analysis showed that the enzyme might belong to the short‐chain dehydrogenase/reductase family. Conclusions: NADP+‐dependent l‐1‐amino‐2‐propanol dehydrogenase isolated from R. erythropolis MAK154 reversibly catalysed dehydrogenation of aminoalcohols, and exhibited a unique sterospecifity for the reduction reaction. Significance and Impact of the Study: The enzyme is a promising catalyst for the production of double chiral compound, d‐pseudoephedrine, from prochiral substrate.

Purification and characterization of a novel glutamate dehydrogenase from Geotrichum candidum with higher alcohol and amino acid activity

“…The native-PAGE and HPLC analyses indicated that the enzyme was composed of 4 monomeric subunits. This is different from all currently reported higher alcohol-reducing enzymes that typically have subunits that have dimolecular weights of 26–80 kDa (Kataoka et al 2006; Kulig et al 2013; Yamada-Onodera et al 2007). By examination of the phylogenetic tree of the NAD(P)-dependent ADH family of proteins and related amino acid sequences in the existing protein database (NCBI) (Jeon et al 2008), the G. candidum S12 GDH obtained in this study may exhibit alcohol dehydrogenase and GDH (EC1.4.1.3) activity for activity towards glutamate and higher alcohols, respectively.…”

Expressed sequence tag analysis of khat (Catha edulis) provides a putative molecular biochemical basis for the biosynthesis of phenylpropylamino alkaloids

“…In each case, reduction to a specific stereoisomer occurs via an enzyme belonging to the short chain dehydrogenase/reductase (SDR) protein family. Interestingly, a bacterial SDR protein was found to reduce N -methylated ( S )-cathinone to (1 S ,2 S )-pseudoephedrine, but not to (1 R ,2 S )-ephedrine (Kataoka et al , 2006, 2008), which supports the hypothesis that two distinct SDR enzymes are involved in the formation of (1 S ,2 S )-cathine and (1 R ,2 S )-norephedrine, respectively (Krizevski et al , 2010). …”

Bacterial microcompartments

“…microcompartment) has been linked to aminoalcohol or aminoketone metabolism 91 . However, only one of the putatively encapsulated enzymes of RMM has been characterized, the L-1-amino-2-propanol dehydrogenase 92 . Very few representative loci are available for these relatively rare BMC types, making it difficult to predict which genes are conserved near those encoding shell proteins, and therefore likely to functionally associated with the organelle These questions will likely be addressed owing to the increasing number of available sequenced bacterial genomes 93 .…”