THE PURIFICATION AND PROPERTIES OF D-ALLOSE-6-KINASE FROM AEROBACTER AEROGENES

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Abstract
The inducible enzyme, D-alIose-6-kinase, has been purified 25-fold from cell-free extracts of Aerobacler aerogenes. The enzyme, which was free of D-phosphoall-ose isomerase activity, had an optimum pH at 6.5, and, at 0 °C, was most stable between 6.5 and 7.5. A requirement for Mg++was demonstrated, Ca++ions being only 37% as effective as Mg++at a concentration of 0.005 M. The activation by 0.005 M MgCl2was reduced 50% by 0.01 M Versene. Of 23 sugars and related compounds tested, the kinase phosphorylated D-allose (100), D-glucose (20), D-ribose (6.3), D-galactose (3.5), and allitol (2.8). The Kmfor D-allose as substrate was 0.98X10"3M. CTP is about 50% and UTP about 43% as effective as ATP as phosphate donors. The enzyme is sensitive to Hg++ions and sulp-hydryl reagents.The product of the reaction of the enzyme with D-allose and ATP was identified as D-allose-6-phosphate by determination of acid-labile phosphate, by periodate oxidation studies, and by chromatography of the dephosphorylated sugar moiety.

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