Literature summary for 3.4.14.5 extracted from

Lee, H.K.; Kim, M.K.; Kim, H.D.; Kim, H.J.; Kim, J.W.; Lee, J.O.; Kim, C.W.; Kim, E.E.
Unique binding mode of evogliptin with human dipeptidyl peptidase IV (2017), Biochem. Biophys. Res. Commun., 494, 452-459 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with inhibitor (3R)-4-[(3R)-3-amino-4-(2,4,5-trifluorophenyl)butanoyl]-3-[(2-methylpropan-2-yl)oxymethyl]piperazin-2-one. The binding of the trifluorophenyl moiety in the S1 pocket and the piperazine-2-one moiety have hydrophobic interactions with Phe357 in the S2 extensive subsite, and the multiple hydrogen bonds made by the (R)-beta-amine group in the S2 pocket and the contacts made by the (R)-tert-butyl group with Arg125 contribute to the high potency of the inhibitor	Homo sapiens

Crystallization (Comment)

Organism

in complex with inhibitor (3R)-4-[(3R)-3-amino-4-(2,4,5-trifluorophenyl)butanoyl]-3-[(2-methylpropan-2-yl)oxymethyl]piperazin-2-one. The binding of the trifluorophenyl moiety in the S1 pocket and the piperazine-2-one moiety have hydrophobic interactions with Phe357 in the S2 extensive subsite, and the multiple hydrogen bonds made by the (R)-beta-amine group in the S2 pocket and the contacts made by the (R)-tert-butyl group with Arg125 contribute to the high potency of the inhibitor

Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
(3R)-4-[(3R)-3-amino-4-(2,4,5-trifluorophenyl)butanoyl]-3-[(2-methylpropan-2-yl)oxymethyl]piperazin-2-one	i.e. evogliptin	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P27487	-	-

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Release 2023.1 (January 2023)