Abstract
AbstractCell‐free extracts from the phytopathogen Agrobacterium tumefaciens contained an enzyme(s) capable of cleaving nucleoside triphosphates, showing highest specific activity toward adenosine triphosphate. Differences are indicated between the adenosine triphosphate phospbohydrolase described hero and other microbial adenosine triphosphatases previously reported. The adenosine trit)hosphatasc activity was stimulated by Mg2+ and Mn2+ and inhibited by other divalent cations. Enzymatic activity was inhibited 100% by mercuric chloride, 38% by p‐chloromercuribenzoate, 22% by potassium fluoride, 12% by sodium azide, and 10% by iodoacetic acid, all at a final concentration of 10−2 M. The enzyme (s) had an optimal PH range of 7.8 to 8.0, and an optimal temperature for hydrolysis at 40deg;C.
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