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. 1974 Oct;143(1):63–66. doi: 10.1042/bj1430063

Activation of carbamoyl phosphate synthase by N-acetyl-l-aspartate

Henry Jay Forman *, Ronald Waddell *, Paul B Hamilton †, Santiago Grisolia *,‡
PMCID: PMC1168352  PMID: 4377221

Abstract

Carbamoyl phosphate synthase from liver of both rat and frog, normally dependent on N-acetyl-l-glutamate (on the basis of Km and physiological concentrations) as an activator, was shown to be activated by high concentrations of N-acetyl-l-aspartate. However, the high concentrations of N-acetyl-l-aspartate required for activation produce non-competitive inhibition. Similarly, high concentrations of N-acetyl-l-glutamate, in very large excess of the amount required to activate the enzyme, inhibit. The limit for N-acetyl-l-glutamate as an impurity in N-acetyl-l-aspartate was found to be less than 1 in 5000 parts, far below the 1 in 250 parts needed to produce the activation observed with N-acetyl-l-aspartate.

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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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