NDLI: NAD(P)+-independent aldehyde dehydrogenase from Pseudomonas testosteroni. A novel type of molybdenum-containing hydroxylase

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NAD(P)+-independent aldehyde dehydrogenase from Pseudomonas testosteroni. A novel type of molybdenum-containing hydroxylase

Content Provider	Scilit
Author	Poels, Paulus A. Groen, Barend W. Duine, Johannis A.
Copyright Year	1987
Description	Journal: Journal of Biological Inorganic Chemistry Aldehyde dehydrogenase from Pseudomonas testosteroni was purified to homogeneity. The enzyme has a pH optimum of 8.2, uses a wide range of aldehydes as substrates and cationic dyes (Wurster's blue, phenazine methosulphate and thionine), but not anionic dyes (ferricyanide and 2.6-dichloroindophenol), NAD(P)+ or O2, as electron acceptors. Haem c and pyrroloquinoline quinone appeared to be absent but the common cofactors of molybdenum hydroxylases were present. Xanthine was not a substrate and allopurinol was not an inhibitor. Alcohols were inhibitors only when turnover of the enzyme occurred in aldehyde conversion. The enzyme has a relative molecular mass of 186,000, consists of two subunits of equal size (Mr 92,000), and 1 enzyme molecule contains 1 FAD, 1 molybdopterin cofactor, 4 Fe and 4 S. It is a novel type of NAD(P)+-independent aldehyde dehydrogenase since its catalytic and physicochemical properties are quite different from those reported for already known aldehyde-converting enzymes like haemoprotein aldehyde dehydrogenase (EC 1.2.99.3), quino-protein alcohol dehydrogenases (EC 1.1.99.8) and molybdenum hydroxylases.
Related Links	http://onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1987.tb13552.x/pdf
Ending Page	579
Page Count	5
Starting Page	575
ISSN	09498257
e-ISSN	14321327
DOI	10.1111/j.1432-1033.1987.tb13552.x
Journal	Journal of Biological Inorganic Chemistry
Issue Number	3
Volume Number	166
Language	English
Publisher	Wiley-Blackwell
Publisher Date	1987-08-01
Access Restriction	Open
Subject Keyword	Journal: Journal of Biological Inorganic Chemistry Biotechnology and Microbiology Aldehyde Dehydrogenase
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

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