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A new NAD(H)-dependent meso-2,3-butanediol dehydrogenase from an industrially potential strain Serratia marcescens H30.
Appl Microbiol Biotechnol. 2014 Feb; 98(3):1175-84.AM

Abstract

The budC gene coding for a new meso-2,3-butanediol dehydrogenase (BDH) from Serratia marcescens H30 was cloned and expressed in Escherichia coli BL21(DE3), purified, and characterized for its properties. The recombinant BDH with a molecular weight of 27.4 kDa exhibited a reversible transformation between acetoin and 2,3-butanediol. In the presence of NADH, BDH could catalyze the reduction of diacetyl and (3R)-acetoin to (3S)-acetoin and meso-2,3-butanediol, respectively, while (3S)-acetoin as a substrate could be further transformed into (2S, 3S)-2,3-butanediol at pH 9.0. For diol oxidation reactions, (3R)-acetoin and (3S)-acetoin were obtained when meso-2,3-butanediol and (2S,3S)-2,3-butanediol were used as the substrates with BDH and NAD(+). (2R,3R)-2,3-butanediol was not a substrate for the BDH at all. The low K m value (4.1 mM) in meso-2,3-butanediol oxidation reaction and no activity for diacetyl, acetoin, and 2,3-butanediol as the substrates with NADP(+)/NADPH suggested that the budC gene product belongs to a NAD(H)-dependent meso-2,3-BDH. Maximum activities for diacetyl and (3S/3R)-acetoin reduction were observed at pH 8.0 and pH 5.0 while for meso-2,3-butanediol oxidation it was pH 8.0. However, the optimum temperature for oxidation and reduction reactions was about 40 °C. In addition, the BDH activity for meso-2,3-butanediol oxidation was enhanced in the presence of Fe(2+) and for diacetyl and (3S/3R)-acetoin reduction in the presence of Mg(2+) and Mn(2+), while several metal ions inhibited its activity, particularly Fe(3+) for reduction of diacetyl and acetoin. Sequence analysis showed that the BDH from S. marcescens H30 possessed two conserved sequences including the coenzyme binding motif (GxxxGxG) and the active-site motif (YxxxK), which are present in the short-chain dehydrogenase/reductase superfamily.

Authors+Show Affiliations

Key Laboratory of Biopesticide and Chemical Biology, Ministry of Education, College of Life Science, Fujian Agriculture and Forestry University, Fuzhou, Fujian Province, 350002, People's Republic of China.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

23666479

Citation

Zhang, Liaoyuan, et al. "A New NAD(H)-dependent Meso-2,3-butanediol Dehydrogenase From an Industrially Potential Strain Serratia Marcescens H30." Applied Microbiology and Biotechnology, vol. 98, no. 3, 2014, pp. 1175-84.
Zhang L, Xu Q, Zhan S, et al. A new NAD(H)-dependent meso-2,3-butanediol dehydrogenase from an industrially potential strain Serratia marcescens H30. Appl Microbiol Biotechnol. 2014;98(3):1175-84.
Zhang, L., Xu, Q., Zhan, S., Li, Y., Lin, H., Sun, S., Sha, L., Hu, K., Guan, X., & Shen, Y. (2014). A new NAD(H)-dependent meso-2,3-butanediol dehydrogenase from an industrially potential strain Serratia marcescens H30. Applied Microbiology and Biotechnology, 98(3), 1175-84. https://doi.org/10.1007/s00253-013-4959-x
Zhang L, et al. A New NAD(H)-dependent Meso-2,3-butanediol Dehydrogenase From an Industrially Potential Strain Serratia Marcescens H30. Appl Microbiol Biotechnol. 2014;98(3):1175-84. PubMed PMID: 23666479.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A new NAD(H)-dependent meso-2,3-butanediol dehydrogenase from an industrially potential strain Serratia marcescens H30. AU - Zhang,Liaoyuan, AU - Xu,Quanming, AU - Zhan,Senran, AU - Li,Yongyu, AU - Lin,Hui, AU - Sun,Shujing, AU - Sha,Li, AU - Hu,Kaihui, AU - Guan,Xiong, AU - Shen,Yaling, Y1 - 2013/05/12/ PY - 2013/02/18/received PY - 2013/04/27/accepted PY - 2013/04/26/revised PY - 2013/5/14/entrez PY - 2013/5/15/pubmed PY - 2014/12/15/medline SP - 1175 EP - 84 JF - Applied microbiology and biotechnology JO - Appl. Microbiol. Biotechnol. VL - 98 IS - 3 N2 - The budC gene coding for a new meso-2,3-butanediol dehydrogenase (BDH) from Serratia marcescens H30 was cloned and expressed in Escherichia coli BL21(DE3), purified, and characterized for its properties. The recombinant BDH with a molecular weight of 27.4 kDa exhibited a reversible transformation between acetoin and 2,3-butanediol. In the presence of NADH, BDH could catalyze the reduction of diacetyl and (3R)-acetoin to (3S)-acetoin and meso-2,3-butanediol, respectively, while (3S)-acetoin as a substrate could be further transformed into (2S, 3S)-2,3-butanediol at pH 9.0. For diol oxidation reactions, (3R)-acetoin and (3S)-acetoin were obtained when meso-2,3-butanediol and (2S,3S)-2,3-butanediol were used as the substrates with BDH and NAD(+). (2R,3R)-2,3-butanediol was not a substrate for the BDH at all. The low K m value (4.1 mM) in meso-2,3-butanediol oxidation reaction and no activity for diacetyl, acetoin, and 2,3-butanediol as the substrates with NADP(+)/NADPH suggested that the budC gene product belongs to a NAD(H)-dependent meso-2,3-BDH. Maximum activities for diacetyl and (3S/3R)-acetoin reduction were observed at pH 8.0 and pH 5.0 while for meso-2,3-butanediol oxidation it was pH 8.0. However, the optimum temperature for oxidation and reduction reactions was about 40 °C. In addition, the BDH activity for meso-2,3-butanediol oxidation was enhanced in the presence of Fe(2+) and for diacetyl and (3S/3R)-acetoin reduction in the presence of Mg(2+) and Mn(2+), while several metal ions inhibited its activity, particularly Fe(3+) for reduction of diacetyl and acetoin. Sequence analysis showed that the BDH from S. marcescens H30 possessed two conserved sequences including the coenzyme binding motif (GxxxGxG) and the active-site motif (YxxxK), which are present in the short-chain dehydrogenase/reductase superfamily. SN - 1432-0614 UR - https://www.unboundmedicine.com/medline/citation/23666479/A_new_NAD_H__dependent_meso_23_butanediol_dehydrogenase_from_an_industrially_potential_strain_Serratia_marcescens_H30_ L2 - https://dx.doi.org/10.1007/s00253-013-4959-x DB - PRIME DP - Unbound Medicine ER -