An enantioselective NADP(+)-dependent alcohol dehydrogenase responsible for cooxidative production of (3S)-5-hydroxy-3-methyl-pentanoic acid

作者：Takeda Minoru^*; Matsumura Aline Tiemi; Kurosaki Kaishi; Chhetri Rajan Thapa; Motomatsu Shigekazu; Suzuki Ichiro; Sahabi Danladi Mahuta

来源：Bioscience Biotechnology and Biochemistry, 2016, 80(6): 1155-1163.

DOI：10.1080/09168451.2016.1148578

• 3-Metyl-1,5-pentandiol
• Cooxidation
• (3S)-5-Hydroxy-3-methyl-pentanoic acid
• Alcohol dehydrogenase
• Mycobacterium

A soil bacterium, Mycobacterium sp. B-009, is able to grow on racemic 1,2-propanediol (PD). The strain was revealed to oxidize 3-methyl-1,5-pentanediol (MPD) to 5-hydroxy-3-methyl-pentanoic acid (HMPA) during growth on PD. MPD was converted into an almost equimolar amount of the S-form of HMPA (S-HMPA) at 72%ee, suggesting the presence of an enantioselective MPD dehydrogenase (MPD-DH). As expected, an NADP(+)-dependent alcohol dehydrogenase, which catalyzes the initial step of MPD oxidation, was detected and purified from the cell-free extract. This enzyme was suggested to be a homodimeric medium-chain alcohol dehydrogenase/reductase (MDR). The catalytic and kinetic parameters indicated that MPD is the most suitable substrate for the enzyme. The enzyme was encoded by a 1047-bp gene (mpd1) and several mycobacterial strains were found to have putative MDR genes similar to mpd1. In a phylogenetic tree, MPD-DH formed an independent clade together with the putative MDR of Mycobacterium neoaurum, which produces opportunistic infections.

• 出版日期2016