An enantioselective NADP+-dependent alcohol dehydrogenase responsible for cooxidative production of (3S)-5-hydroxy-3-methyl-pentanoic acid. Issue 6 (2nd June 2016)

• Record Type: Journal Article
• Authors: Takeda, Minoru; Matsumura, Aline Tiemi; Kurosaki, Kaishi; Chhetri, Rajan Thapa; Motomatsu, Shigekazu; Suzuki, Ichiro; Sahabi, Danladi Mahuta
• Is Part Of: Bioscience, biotechnology, and biochemistry. Volume 80:Issue 6(2016)
• Page Start: 1155
• Page End: 1163
• Publication Date: 2016-06-02
• Subjects: 3-Metyl-1, 5-pentandiol -- Cooxidation -- (3S)-5-Hydroxy-3-methyl-pentanoic acid -- Alcohol dehydrogenase -- Mycobacterium; Biotechnology -- Periodicals; Biochemistry -- Periodicals; 660.6
• DOI: 10.1080/09168451.2016.1148578
• Languages: English
• ISSNs: 0916-8451

Abstract

Abstract: 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. Graphical abstract: : Cooxidation of 3-metyl-1, 5-pentanediol to (3 S )-5-hydroxy-3-methyl-pentanoic acid by strain B-009.