Identification and characterization of a mycobacterial NAD+-dependent alcohol dehydrogenase with superior reduction of diacetyl to (S)-acetoin. Issue 11 (2nd November 2014)

• Record Type: Journal Article
• Authors: Takeda, Minoru; Anamizu, Shiori; Motomatsu, Shigekazu; Chen, Xue; Thapa Chhetri, Rajan
• Is Part Of: Bioscience, biotechnology, and biochemistry. Volume 78:Issue 11(2014)
• Page Start: 1879
• Page End: 1886
• Publication Date: 2014-11-02
• Subjects: Mycobacterium -- diacetyl -- (S)-acetoin -- reductase -- NADH recycle; Biotechnology -- Periodicals; Biochemistry -- Periodicals; 660.6
• DOI: 10.1080/09168451.2014.943649
• Languages: English
• ISSNs: 0916-8451

Abstract

Abstract: An enzyme capable of reducing acetoin in the presence of NADH was purified from Mycobacterium sp. B-009, a non-clinical bacterial strain of soil origin. The enzyme is a homotetramer and can be classified as a medium-chain alcohol dehydrogenase/reductase based on the molecular weight of the monomer. Identification of the structural gene revealed a limited distribution of homologous genes only among actinomycetes. In addition to its activity as a reductase specific for ( S )-acetoin (EC 1.1.1.76), the enzyme showed both diacetyl reductase (EC 1.1.1.304) and NAD + -dependent alcohol dehydrogenase (EC 1.1.1.1) activities. ( S )-Acetoin and diacetyl reductases belong to a group of short-chain alcohol dehydrogenase/reductases but do not have superior abilities to dehydrogenate monoalcohols. Thus, the purified enzyme can be readily distinguished from other enzymes. We used the dual functionality of the enzyme to effectively reduce diacetyl to ( S )-acetoin, coupled with the oxidation of 1-butanol. Graphical abstract: : Enantioselective conversion of diacetyl to ( S )-acetoin coupled with oxidation of 1-butanol to butyl aldehyde using a newly found Mycobacterial alcohol dehydrogenase.