Literature summary for 3.4.14.4 extracted from

Agic, D.; Brkic, H.; Kazazic, S.; Tomic, A.; Abramic, M.
Aprotinin interacts with substrate-binding site of human dipeptidyl peptidase III (2018), J. Biomol. Struct. Dyn., 37, 3596-3606 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
molecular modeling of docking. Aprotinin interacts by its canonical binding epitope with the substrate binding cleft of DPP III. Thereby, free N-terminus of aprotinin is distant from the active-site zinc. The enzyme-inhibitor complex is stabilized by intermolecular hydrogen bonding network, electrostatic and hydrophobic interactions which mostly involve constituent amino acid residues of the DPP III substrate binding subsites S1, S1', S2, S2' and S3'	Homo sapiens

Crystallization (Comment)

Organism

molecular modeling of docking. Aprotinin interacts by its canonical binding epitope with the substrate binding cleft of DPP III. Thereby, free N-terminus of aprotinin is distant from the active-site zinc. The enzyme-inhibitor complex is stabilized by intermolecular hydrogen bonding network, electrostatic and hydrophobic interactions which mostly involve constituent amino acid residues of the DPP III substrate binding subsites S1, S1', S2, S2' and S3'

Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
Aprotinin	-	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9NY33	-	-

Synonyms

Synonyms	Comment	Organism
DPP3	-	Homo sapiens

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Release 2023.1 (January 2023)