caa a22 4500 605499896 CHVBK 20210128100553.0 cr unu---uuuuu 210128e20150501xx s 000 0 eng 10.1007/s00253-014-6191-8 doi (NATIONALLICENCE)springer-10.1007/s00253-014-6191-8 Succinic semialdehyde reductase Gox1801 from Gluconobacter oxydans in comparison to other succinic semialdehyde - reducing enzymes [Elektronische Daten] [Maria Meyer, Paul Schweiger, Uwe Deppenmeier] 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 134kDa 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. Springer-Verlag Berlin Heidelberg, 2014 Acetic acid bacteria nationallicence Incomplete oxidation nationallicence Oxidoreductase nationallicence Biotransformation nationallicence Aldehyde reduction nationallicence γ-Hydroxybutyrate nationallicence Meyer Maria Institute of Microbiology and Biotechnology, Meckenheimer Allee 168, 53115, Bonn, Germany aut Schweiger Paul Biology Department, Missouri State University, 901 S. National Ave, 65897, Springfield, MO, USA aut Deppenmeier Uwe Institute of Microbiology and Biotechnology, Meckenheimer Allee 168, 53115, Bonn, Germany aut Applied Microbiology and Biotechnology Springer Berlin Heidelberg 99/9(2015-05-01), 3929-3939 0175-7598 99:9<3929 2015 99 253 https://doi.org/10.1007/s00253-014-6191-8 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00253-014-6191-8 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Meyer Maria Institute of Microbiology and Biotechnology, Meckenheimer Allee 168, 53115, Bonn, Germany aut NATIONALLICENCE 700 1- Schweiger Paul Biology Department, Missouri State University, 901 S. National Ave, 65897, Springfield, MO, USA aut NATIONALLICENCE 700 1- Deppenmeier Uwe Institute of Microbiology and Biotechnology, Meckenheimer Allee 168, 53115, Bonn, Germany aut NATIONALLICENCE 773 0- Applied Microbiology and Biotechnology Springer Berlin Heidelberg 99/9(2015-05-01), 3929-3939 0175-7598 99:9<3929 2015 99 253