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Succinic semialdehyde reductase Gox1801 from Gluconobacter oxydans in comparison to other succinic semialdehyde-reducing enzymes.
Appl Microbiol Biotechnol. 2015 May; 99(9):3929-39.AM

Abstract

Gluconobacter oxydans is an industrially important bacterium that possesses many uncharacterized oxidoreductases, which might be exploited for novel biotechnological applications. In this study, gene gox1801 was homologously overexpressed in G. oxydans and it was found that the relative expression of gox1801 was 13-fold higher than that in the control strain. Gox1801 was predicted to belong to the 3-hydroxyisobutyrate dehydrogenase-type proteins. The purified enzyme had a native molecular mass of 134 kDa and forms a homotetramer. Analysis of the enzymatic activity revealed that Gox1801 is a succinic semialdehyde reductase that used NADH and NADPH as electron donors. Lower activities were observed with glyoxal, methylglyoxal, and phenylglyoxal. The enzyme was compared to the succinic semialdehyde reductase GsSSAR from Geobacter sulfurreducens and the γ-hydroxybutyrate dehydrogenase YihU from Escherichia coli K-12. The comparison revealed that Gox1801 is the first enzyme from an aerobic bacterium reducing succinic semialdehyde with high catalytic efficiency. As a novel succinic semialdehyde reductase, Gox1801 has the potential to be used in the biotechnological production of γ-hydroxybutyrate.

Authors+Show Affiliations

Institute of Microbiology and Biotechnology, Meckenheimer Allee 168, 53115, Bonn, Germany.No affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

25425279

Citation

Meyer, Maria, et al. "Succinic Semialdehyde Reductase Gox1801 From Gluconobacter Oxydans in Comparison to Other Succinic Semialdehyde-reducing Enzymes." Applied Microbiology and Biotechnology, vol. 99, no. 9, 2015, pp. 3929-39.
Meyer M, Schweiger P, Deppenmeier U. Succinic semialdehyde reductase Gox1801 from Gluconobacter oxydans in comparison to other succinic semialdehyde-reducing enzymes. Appl Microbiol Biotechnol. 2015;99(9):3929-39.
Meyer, M., Schweiger, P., & Deppenmeier, U. (2015). Succinic semialdehyde reductase Gox1801 from Gluconobacter oxydans in comparison to other succinic semialdehyde-reducing enzymes. Applied Microbiology and Biotechnology, 99(9), 3929-39. https://doi.org/10.1007/s00253-014-6191-8
Meyer M, Schweiger P, Deppenmeier U. Succinic Semialdehyde Reductase Gox1801 From Gluconobacter Oxydans in Comparison to Other Succinic Semialdehyde-reducing Enzymes. Appl Microbiol Biotechnol. 2015;99(9):3929-39. PubMed PMID: 25425279.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Succinic semialdehyde reductase Gox1801 from Gluconobacter oxydans in comparison to other succinic semialdehyde-reducing enzymes. AU - Meyer,Maria, AU - Schweiger,Paul, AU - Deppenmeier,Uwe, Y1 - 2014/11/26/ PY - 2014/08/26/received PY - 2014/10/25/accepted PY - 2014/10/23/revised PY - 2014/11/27/entrez PY - 2014/11/27/pubmed PY - 2015/12/29/medline SP - 3929 EP - 39 JF - Applied microbiology and biotechnology JO - Appl. Microbiol. Biotechnol. VL - 99 IS - 9 N2 - Gluconobacter oxydans is an industrially important bacterium that possesses many uncharacterized oxidoreductases, which might be exploited for novel biotechnological applications. In this study, gene gox1801 was homologously overexpressed in G. oxydans and it was found that the relative expression of gox1801 was 13-fold higher than that in the control strain. Gox1801 was predicted to belong to the 3-hydroxyisobutyrate dehydrogenase-type proteins. The purified enzyme had a native molecular mass of 134 kDa and forms a homotetramer. Analysis of the enzymatic activity revealed that Gox1801 is a succinic semialdehyde reductase that used NADH and NADPH as electron donors. Lower activities were observed with glyoxal, methylglyoxal, and phenylglyoxal. The enzyme was compared to the succinic semialdehyde reductase GsSSAR from Geobacter sulfurreducens and the γ-hydroxybutyrate dehydrogenase YihU from Escherichia coli K-12. The comparison revealed that Gox1801 is the first enzyme from an aerobic bacterium reducing succinic semialdehyde with high catalytic efficiency. As a novel succinic semialdehyde reductase, Gox1801 has the potential to be used in the biotechnological production of γ-hydroxybutyrate. SN - 1432-0614 UR - https://www.unboundmedicine.com/medline/citation/25425279/Succinic_semialdehyde_reductase_Gox1801_from_Gluconobacter_oxydans_in_comparison_to_other_succinic_semialdehyde_reducing_enzymes_ L2 - https://dx.doi.org/10.1007/s00253-014-6191-8 DB - PRIME DP - Unbound Medicine ER -