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. 1972 Oct;112(1):439–444. doi: 10.1128/jb.112.1.439-444.1972

Adenine Phosphoribosyltransferase in Mycoplasma mycoides and Escherichia coli

Iris L Sin 1, L R Finch 1
PMCID: PMC251430  PMID: 4562405

Abstract

Some kinetic properties of the adenine phosphoribosyltransferases from Escherichia coli and Mycoplasma mycoides have been studied. For the E. coli enzyme, Michaelis constants for adenine and 5-phosphoribosyl-1-pyrophosphate (PRPP) are 1.3 and 10 μm, respectively. Adenosine monophosphate, the most effective nucleotide inhibitor, inhibits competitively with respect to PRPP, the inhibition constant being 26 μm. The M. mycoides enzyme has more complex kinetics. The response to increasing PRPP concentration is sigmoidal, the degree of sigmoidality depending on both the concentration of adenine and the pH. At low PRPP levels, high concentrations of adenine are inhibitory. Guanosine monophosphate is the most effective inhibitor, being inhibitory at all pH values, but other nucleotides have been found to activate at pH 7 and inhibit at pH 8. The elution profile of the M. mycoides enzyme from Sephadex suggests an association of enzyme subunits in the presence of PRPP. This is consistent with the observed kinetics if the associated form has increased stability and activity.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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