Summary: Histidinol dehydrogenase has been purified from a derepressed mutant of B. A molecular weight of about 91000 was estimated by gel filtration. The native enzyme seems to be composed of two similar subunits which have a molecular weight of 52000 as determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The pI of the enzyme as determined by isoelectric focusing is 4.75. The enzyme is maximally active at pH 9.5. It is highly specific for NAD and histidinol, with a K (NAD) of 0.57 mM and a K (histidinol) of 14 μm. Mn is required for maximal activity. The enzyme is completely inactivated by 8 -urea but regains its activity very quickly upon removal of the urea. Mn and histidinol protect the enzyme from heat inactivation.


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