Bisubstrate Inhibitors of the Enzyme Catechol  O ‐Methyltransferase (COMT): Efficient Inhibition Despite the Lack of a Nitro Group | Zendy

Paulini Ralph | Zendy; Lerner Christian | Zendy; JakobRoetne Roland | Zendy; Zürcher Gerhard | Zendy; Borroni Edilio | Zendy; Diederich François | Zendy

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Bisubstrate Inhibitors of the Enzyme Catechol O ‐Methyltransferase (COMT): Efficient Inhibition Despite the Lack of a Nitro Group

Author(s) -

Paulini Ralph,

Lerner Christian,

JakobRoetne Roland,

Zürcher Gerhard,

Borroni Edilio,

Diederich François

Publication year - 2004

Publication title -

chembiochem

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.05

H-Index - 126

eISSN - 1439-7633

pISSN - 1439-4227

DOI - 10.1002/cbic.200400084

Subject(s) - nitro , catechol o methyl transferase , chemistry , enzyme , methyltransferase , catechol , enzyme inhibition , stereochemistry , group (periodic table) , biochemistry , combinatorial chemistry , organic chemistry , methylation , allele , alkyl , gene

A new generation of bisubstrate inhibitors for the S ‐adenosylmethionine‐ and magnesium ion‐dependent enzyme catechol O ‐methyltransferase (COMT), feature binding affinities (IC 50 values) in the double‐digit nanomolar range despite the lack of a nitro group on the catechol moiety. Inhibitor potency does not directly correlate with the p K a value of the catechol HO groups and is strongly enhanced by hydrophobic aromatic substituents attached in a biaryl‐type fashion to position 5 of the catechol ring.

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