Abstract
Histidase from Pseudomonas putida was inhibited by a variety of nucleotides and nucleosides. Guanine, xanthine and cytosine derivatives were the most potent inhibitors, with adenine, hypoxanthine and uracil derivatives considerably less inhibitory; the extent of phosphorylation was relatively unimportant. Kinetically, the actions of ATP, GTP and GMP were similar. Each exhibited an apparent non-competitive inhibition towards histidine with multiple binding sites. It was concluded that histidase activity could be controlled by variations in the total intracellular nucleotide concentration, thereby regulating C 1 unit production for purine biosynthesis.
Published Version
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