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Article

An intramolecular disulfide bridge as a catalytic switch for serotonin N-acetyltransferase.

The Journal of biological chemistry - 15 Nov 2002

Tsuboi Seiji, Kotani Yoshifumi, Ogawa Ken'ichi, Hatanaka Tadashi, Yatsushiro Shouki, Otsuka Masato, Moriyama Yoshinori

Abstract excerpt

Serotonin N-acetyltransferase (EC. 2.3.1.87) (AA-NAT) is a melatonin rhythm-generating enzyme in pineal glands. To establish a melatonin rhythm, AA-NAT activity is precisely regulated through several signaling pathways. Here we show novel regulation of AA-NAT activity, in which an intramolecular disulfide bond may function as a switch for the catalysis. Recombinant AA-NAT activity was irreversibly inhibited by...

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PMID: 12215431
DOI: 10.1074/jbc.M203305200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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