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- W1990381918 abstract "2-Hydroxy-6-oxo-7-methylocta-2,4-dienoate (6-isopropyl-HODA) hydrolase (CumD), an enzyme of the cumene biodegradation pathway encoded by the cumD gene of Pseudomonas fluorescens IP01, was purified to homogeneity from an overexpressing Escherichia coli strain. SDS-polyacrylamide gel electrophoresis and gel filtration demonstrated that it is a dimeric enzyme with a subunit molecular mass of 32 kDa. The pH optima for activity and stability were 8.0 and 7.0–9.0, respectively. The enzyme exhibited a biphasic Arrhenius plot of catalysis with two characteristic energies of activation with a break point at 20°C. The enzyme has a Km of 7.3 μM and a kcat of 21 s−1 for 6-isopropyl-HODA (150 mM phosphate, pH 7.5, 25°C), and its substrate specificity covers larger C6 substituents compared with another monoalkylbenzene hydrolase, TodR Unlike TodF, CumD could slightly hydrolyze 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate (6-phenyl-HODA). A mutant enzyme as to a putative active site residue, S103A, had 105-fold lower activity than that of the wild-type enzyme." @default.
- W1990381918 created "2016-06-24" @default.
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- W1990381918 date "2003-01-01" @default.
- W1990381918 modified "2023-10-18" @default.
- W1990381918 title "Improvement and applications of cell-free protein synthesis systems —Monograph—" @default.
- W1990381918 doi "https://doi.org/10.1016/s1389-1723(03)80136-6" @default.
- W1990381918 hasPublicationYear "2003" @default.
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