[Temperature dependence of membrane-bound aldehyde dehydrogenase from Acinetobacter: effect of solubilization and chain length of the substrates].
The NADP+-dependent aldehyde dehydrogenase of intracytoplasmic membranes of Acinetobacter calcoaceticus shows a characteristic behaviour of its reaction velocities in dependence on temperature. The calculated "real" activation energies depend on the increasing chain-length of the homologous aldehydes and grow appropriate to the membrane-bound and to the micellar form of the enzyme with 6.2 and 7.3 kJ/mole CH2-group, respectively. The values of the activation energy of the membrane-bound enzyme are - for each aldehyde of the homologous series - 12 kJ/mole larger than those of the solubilized enzyme (present as mixed micelles of enzyme, cholate and bacterial phospholipids).
Sorger
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Kretschmer
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Aurich
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D000150:Acinetobacter / Q000201:enzymology*; D000444:Aldehyde Dehydrogenase / Q000378:metabolism*; D007700:Kinetics; D009249:NADP / Q000378:metabolism*; D012995:Solubility; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D013696:Temperature
D009249:NADP; D000444:Aldehyde Dehydrogenase
Temperaturabhängigkeit der membrangebundenen Aldehyddehydrogenase aus Acinetobacter: Einfluss der Solubilisierung und der Kettenlänge der Substrate.