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Science 31 July 1981:
Vol. 213. no. 4507, pp. 571 - 573
DOI: 10.1126/science.7017937

Articles

Science, Vol 213, Issue 4507, 571-573
Copyright © 1981 by American Association for the Advancement of Science


articles

Pineal N-acetyltransferase is inactivated by disulfide-containing peptides: insulin is the most potent

MA Namboodiri, JT Favilla, and DC Klein

Pineal N-acetyltransferase can be inactivated in broken cell preparations by cystamine through a mechanism of thiol-disulfide exchange. Some, but not all, disulfide-containing peptides can inactivate this enzyme; the most potent inactivator is insulin. These findings suggest that a disulfide-containing peptide with high reactivity toward N-acetyltransferase may participate in the intracellular regulation of this enzyme.


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An Intramolecular Disulfide Bridge as a Catalytic Switch for Serotonin N-Acetyltransferase.
S. Tsuboi, Y. Kotani, K.'i. Ogawa, T. Hatanaka, S. Yatsushiro, M. Otsuka, and Y. Moriyama (2002)
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Pineal Serotonin N-Acetyltransferase: Expression Cloning and Molecular Analysis.
S. L. Coon, P. H. Roseboom, R. Baler, J. L. Weller, M. A. A. Namboodiri, E. V. Koonin, and D. C. Klein (1995)
Science 270, 1681-1683
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cAMP Regulation of Arylalkylamine N-Acetyltransferase (AANAT, EC 2.3.1.87). A NEW CELL LINE (1E7) PROVIDES EVIDENCE OF INTRACELLULAR AANAT ACTIVATION.
S. L. Coon, J. L. Weller, H.-W. Korf, M. A. A. Namboodiri, M. Rollag, and D. C. Klein (2001)
J. Biol. Chem. 276, 24097-24107
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