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. 1976 Jan;57(1):23–28. doi: 10.1104/pp.57.1.23

Some Regulatory Properties of Pea Leaf Carbamoyl Phosphate Synthetase 1

Thomas Denny O'Neal a,2, Aubrey W Naylor a
PMCID: PMC541956  PMID: 16659418

Abstract

Carbamoyl phosphate synthetase of pea shoots (Pisum sativum L.) was purified 101-fold. Its stability was greatly increased by the addition of substrates and activators. The enzyme was strongly inhibited by micromolar amounts of UMP (Ki less than 2 μm). UDP, UTP, TMP, and ADP were also inhibitory. AMP caused either slight activation (under certain conditions) or was inhibitory. Uridine nucleotides were competitive inhibitors, as was AMP, while ADP was a noncompetitive inhibitor. Enzyme activity was increased manyfold by the activator ornithine. Ornithine acted by increasing the affinity for Mg·ATP by a factor of 8 or more. Other activators were IMP, GMP, ITP, and GTP, IMP, like ornithine, increased the Michaelis constant for Mg·ATP. The activators ornithine, GMP, and IMP (but not GTP and ITP) completely reversed inhibition caused by pyrimidine nucleotides while increasing the inhibition caused by ADP and AMP.

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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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