NAD(P)-dependent aldehyde dehydrogenases induced during growth of Ralstonia eutropha strain Bo on tetrahydrofurfuryl alcohol.
Different aldehyde dehydrogenases (AlDHs) were formed during growth of Ralstonia eutropha Bo on tetrahydrofurfuryl alcohol (THFA). One of these enzymes, AlDH 4, was purified and characterized as a homodimer containing no prosthetic groups, showing a strong substrate inhibition, and having an N-terminal sequence similar to those of various NAD(P)-dependent AlDHs. The conversion rate of THFA by the quinohemoprotein THFA dehydrogenase was increased by AlDH 4.
Schräder
T
T
Institut für Mikrobiologie, Martin-Luther-Universität Halle-Wittenberg, Halle, Germany.
Zarnt
G
G
Andreesen
J R
JR
D000429:Alcohol Oxidoreductases / Q000378:metabolism; D000444:Aldehyde Dehydrogenase / Q000096:biosynthesis*; D000445:Aldehyde Oxidoreductases / Q000096:biosynthesis*; D001426:Bacterial Proteins; D001673:Biodegradation, Environmental; D020118:Cupriavidus necator / Q000201:enzymology*; D004790:Enzyme Induction; D005663:Furans / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial; D009243:NAD; D009249:NADP; D015262:Xenobiotics / Q000378:metabolism*
D001426:Bacterial Proteins; D005663:Furans; D015262:Xenobiotics; D009243:NAD; D009249:NADP; D000429:Alcohol Oxidoreductases; C442136:tetrahydrofurfuryl alcohol dehydrogenase; D000445:Aldehyde Oxidoreductases; D000444:Aldehyde Dehydrogenase; C018699:aldehyde dehydrogenase (NAD(P)+); C018675:tetrahydrofurfuryl alcohol