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Literature summary for 1.3.5.2 extracted from

  • Walse, B.; Dufe, V.; Svensson, B.; Fritzson, I.; Dahlberg, L.; Khairoullina, A.; Wellmar, U.; Al-Karadaghi, S.
    The structures of human dihydroorotate dehydrogenase with and without inhibitor reveal conformational flexibility in the inhibitor and substrate binding sites (2008), Biochemistry, 47, 8929-8936.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
-
 Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with inhibitors 6-chloro-2-(2'-fluorobiphenyl-4-yl)quinoline-4-carboxylic acid and and without any bound inhibitor, to 2.3 A, 2.1 A, and 3.0 A resolution, respectively. Inhibitor 5-methoxy-2-[(4-phenoxyphenyl)amino]benzoic acid 5-methoxy-2-[(4-phenoxyphenyl)amino]benzoic acid interacts with residue Y356. Loop region of residues L68-R72 may interfere with inhibitor/cofactor binding. Loop region N212-L224 may be important for the enzymatic reaction Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
5-methoxy-2-[(4-phenoxyphenyl)amino]benzoic acid
-
 Homo sapiens
6-chloro-2-(2'-fluorobiphenyl-4-yl)quinoline-4-carboxylic acid
-
 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q02127
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-dihydroorotate + 2,6-dichlorophenolindophenol
-
 Homo sapiens orotate + reduced 2,6-dichlorophenolindophenol
-
 ?

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.000015
-
 pH 8.0, 22°C Homo sapiens 6-chloro-2-(2'-fluorobiphenyl-4-yl)quinoline-4-carboxylic acid
0.000081
-
 pH 8.0, 22°C Homo sapiens 5-methoxy-2-[(4-phenoxyphenyl)amino]benzoic acid