Sandbox Reserved 1506
From Proteopedia
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Serotonin N-acetyltransferase is also named aralkylamine-N-acetyltransferase (ANAAT). This enzyme catalyzes the acetylation of the amine group on serotonin, an intermediate in melatonin synthesis. It forms the penultimate enzyme in the melatonin pathway, as it is shown on fig1. | Serotonin N-acetyltransferase is also named aralkylamine-N-acetyltransferase (ANAAT). This enzyme catalyzes the acetylation of the amine group on serotonin, an intermediate in melatonin synthesis. It forms the penultimate enzyme in the melatonin pathway, as it is shown on fig1. | ||
| - | Circulating melatonin plays a role in the circadian rythm. Day/night differences in circulating melatonin levels provide a hormonal analog signal of environmental lighting, which is used in a variety of ways to optimize circadian and circannual rhythms in physiology[2]. The | ||
[[Image:melationin synthesis.jpg]] | [[Image:melationin synthesis.jpg]] | ||
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| + | == Relevance == | ||
| + | |||
| + | Circulating melatonin plays a role in the circadian rythm. Day/night differences in circulating melatonin levels provide a hormonal analog signal of environmental lighting, which is used in a variety of ways to optimize circadian and circannual rhythms in physiology[2]. Melatonin amount is around 10-fold | ||
| + | higher at night than during the day. | ||
| + | Its amount is correlated with ANAAT activity, which varies in parallel with melationin amount.[3] | ||
| + | |||
== Structure == | == Structure == | ||
| + | AANAT consists of an 8 stranded β sheet with five α helices, with a conserved motif in the center of the sheet forming a binding site for acetyl-CoA, the acetyl source. | ||
== Regulation == | == Regulation == | ||
| - | |||
| - | == Relevance == | ||
== Structural highlights == | == Structural highlights == | ||
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[2] Arendt, J. (1995) Melatonin and the Mammalian Pineal Gland (Chapman & Hall, London), pp. 201–285. | [2] Arendt, J. (1995) Melatonin and the Mammalian Pineal Gland (Chapman & Hall, London), pp. 201–285. | ||
| - | [3] Melatonin synthesis: 14-3-3-dependent activation and inhibition of arylalkylamine N -acetyltransferase mediated by phosphoserine-205 - Surajit Ganguly, Joan L. Weller, Anthony Ho, Philippe Chemineau, Benoit Malpaux, and David C. Klein - PNAS, January 25, 2005. | + | [3] Klein, D.C., and Weller, J.L. (1972). Rapid light induced decrease in pineal serotonin N-acetyltransferase activity. Science 177, 532–533. |
| + | |||
| + | [4]Gastel, J.A., Roseboom, P.H., Rinaldi, P.A., Weller, J.L., and Klein,D.C. (1998). Melatonin production: proteasomal proteolysis in serotonin N-acetyltransferase regulation. Science 279, 1358–1360. | ||
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| + | [5] Melatonin synthesis: 14-3-3-dependent activation and inhibition of arylalkylamine N -acetyltransferase mediated by phosphoserine-205 - Surajit Ganguly, Joan L. Weller, Anthony Ho, Philippe Chemineau, Benoit Malpaux, and David C. Klein - PNAS, January 25, 2005. | ||
| - | [ | + | [6] The Structural Basis of Ordered Substrate Binding by Serotonin N-Acetyltransferase: Enzyme Complex at 1.8 A ˚ Resolution with a Bisubstrate Analog - Alison Burgess Hickman,M. A. A. Namboodiri, David C. Klein, and Fred Dyda - Cell, Vol. 97, 361–369, April 30, 1999. |
Revision as of 12:54, 2 January 2019
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| This Sandbox is Reserved from 06/12/2018, through 30/06/2019 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1480 through Sandbox Reserved 1543. |
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Contents |
Function
Serotonin N-acetyltransferase is also named aralkylamine-N-acetyltransferase (ANAAT). This enzyme catalyzes the acetylation of the amine group on serotonin, an intermediate in melatonin synthesis. It forms the penultimate enzyme in the melatonin pathway, as it is shown on fig1.
Relevance
Circulating melatonin plays a role in the circadian rythm. Day/night differences in circulating melatonin levels provide a hormonal analog signal of environmental lighting, which is used in a variety of ways to optimize circadian and circannual rhythms in physiology[2]. Melatonin amount is around 10-fold higher at night than during the day. Its amount is correlated with ANAAT activity, which varies in parallel with melationin amount.[3]
Structure
AANAT consists of an 8 stranded β sheet with five α helices, with a conserved motif in the center of the sheet forming a binding site for acetyl-CoA, the acetyl source.
Regulation
Structural highlights
</StructureSection>
References
[1] Hickman, A. B; Klein, D. C; Dyda, F. Melatonin Biosynthesis: The Structure of Serotonin N-Acetyltransferase at 2.5A Resolution Suggests a Catalytic Mechanism. Mol. Cell. 1999, 3-1, 23-32.
[2] Arendt, J. (1995) Melatonin and the Mammalian Pineal Gland (Chapman & Hall, London), pp. 201–285.
[3] Klein, D.C., and Weller, J.L. (1972). Rapid light induced decrease in pineal serotonin N-acetyltransferase activity. Science 177, 532–533.
[4]Gastel, J.A., Roseboom, P.H., Rinaldi, P.A., Weller, J.L., and Klein,D.C. (1998). Melatonin production: proteasomal proteolysis in serotonin N-acetyltransferase regulation. Science 279, 1358–1360.
[5] Melatonin synthesis: 14-3-3-dependent activation and inhibition of arylalkylamine N -acetyltransferase mediated by phosphoserine-205 - Surajit Ganguly, Joan L. Weller, Anthony Ho, Philippe Chemineau, Benoit Malpaux, and David C. Klein - PNAS, January 25, 2005.
[6] The Structural Basis of Ordered Substrate Binding by Serotonin N-Acetyltransferase: Enzyme Complex at 1.8 A ˚ Resolution with a Bisubstrate Analog - Alison Burgess Hickman,M. A. A. Namboodiri, David C. Klein, and Fred Dyda - Cell, Vol. 97, 361–369, April 30, 1999.
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644

