Purification and characterization of 3-dehydroquinase from Escherichia coli
Keyword(s):
A procedure has been developed for the purification of 3-dehydroquinase from Escherichia coli. Homogeneous enzyme with specific activity 163 units/mg of protein was obtained in 19% overall yield. The subunit Mr estimated from polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate was 29,000. The native Mr, estimated by gel permeation chromatography on Sephacryl S-200 (superfine) and on TSK G3000SW, was in the range 52,000-58,000, indicating that the enzyme is dimeric. The catalytic properties of the enzyme have been determined and shown to be very similar to those of the biosynthetic 3-dehydroquinase component of the arom multifunctional enzyme of Neurospora crassa.
1984 ◽
Vol 30
(9)
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pp. 1171-1178
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2001 ◽
Vol 67
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pp. 3746-3749
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1992 ◽
Vol 267
(8)
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pp. 5374-5379
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1984 ◽
Vol 120
(1)
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pp. 237-241
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1998 ◽
Vol 64
(2)
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pp. 789-792
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1983 ◽
Vol 29
(10)
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pp. 1361-1368
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