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Molecular Recognition at the Active Site of Catechol-O-methyltransferase (COMT): Adenine Replacements in Bisubstrate Inhibitors

✍ Scribed by Dr. Manuel Ellermann; Dr. Ralph Paulini; Dr. Roland Jakob-Roetne; Dr. Christian Lerner; Dr. Edilio Borroni; Doris Roth; Dr. Andreas Ehler; Dr. W. Bernd Schweizer; Dr. Daniel Schlatter; Dr. Markus G. Rudolph; Prof. Dr. François Diederich


Book ID
102797617
Publisher
John Wiley and Sons
Year
2011
Tongue
English
Weight
838 KB
Volume
17
Category
Article
ISSN
0947-6539

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Molecular Recognition at the Active Site
✍ Manuel Ellermann; Roland Jakob-Roetne; Christian Lerner; Edilio Borroni; Daniel 📂 Article 📅 2009 🏛 John Wiley and Sons 🌐 English ⚖ 562 KB

Biologically active catechols, such as l-DOPA and the neurotransmitter dopamine, are inactivated by methylation. This reaction is catalyzed by the enzyme catechol-O-methyltransferase (COMT) in the presence of S-adenosylmethionine (SAM) and Mg 2+ ions. [1] Small nitrocatechol-based inhibitors of COMT