Literature summary for 3.4.14.5 extracted from

Engel, M.; Hoffmann, T.; Wagner, L.; Wermann, M.; Heiser, U.; Kiefersauer, R.; Huber, R.; Bode, W.; Demuth, H.U.; Brandstetter, H.
The crystal structure of dipeptidyl peptidase IV (CD26) reveals its functional regulation and enzymatic mechanism (2003), Proc. Natl. Acad. Sci. USA, 100, 5063-5068.

Application

Application	Comment	Organism
pharmacology	enzyme is a target for drug design	Sus scrofa

Cloned(Commentary)

Cloned (Comment)	Organism
DNA sequence determination and analysis	Sus scrofa

Crystallization (Commentary)

Crystallization (Comment)	Organism
20 mg/ml purified enzyme, sitting drop vapour diffusion method, room temperature, several days, from 20-22% PEG 2000, 0.1 ammonium sulfate, 0.1 M Tris-HCl, pH 8.0, covering of the drops with perfluoropolyether oil, humidity control during harvest of crystals, multiple wavelength anomalous dispersion using a mercury derivative and subsequent noncrystallographic symmetry averaging, structure determination and analysis, modeling	Sus scrofa

Crystallization (Comment)

Organism

20 mg/ml purified enzyme, sitting drop vapour diffusion method, room temperature, several days, from 20-22% PEG 2000, 0.1 ammonium sulfate, 0.1 M Tris-HCl, pH 8.0, covering of the drops with perfluoropolyether oil, humidity control during harvest of crystals, multiple wavelength anomalous dispersion using a mercury derivative and subsequent noncrystallographic symmetry averaging, structure determination and analysis, modeling

Sus scrofa

Inhibitors

Inhibitors	Comment	Organism	Structure
1-[2-amino-3-(4-iodophenyl)propanoyl]pyrrolidine--2-carbonitrile	-	Sus scrofa

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	-	Sus scrofa	16020	-

Organism

Organism	UniProt	Comment	Textmining
Sus scrofa	P22411	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	N-glycosylation at Asn279 is important for adenosine deaminase binding	Sus scrofa

Purification (Commentary)

Purification (Comment)	Organism
from kidney cortex, 280fold	Sus scrofa

Reaction

Reaction	Comment	Organism	Reaction ID
release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline	catalytic domain structure, active site and substrate recognition study	Sus scrofa	a

Source Tissue

Source Tissue	Comment	Organism	Textmining
kidney	cortex	Sus scrofa	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
42	-	above, purified enzyme	Sus scrofa

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	oligomerization state is important for interaction with other compounds, enzyme binds via Leu294 and Val341 to adenosine deaminase at T-cells, which is controlled by formation of a tetramer and glycosylation at Asn279	Sus scrofa	?	-	?

Subunits

Subunits	Comment	Organism
dimer	is likely to enhance the receptor-ligand affinity by bivalent interaction which may be critical for signal transduction into the cell	Sus scrofa
More	oligomerization study	Sus scrofa
tetramer	dimerization of dimers on the cell surface	Sus scrofa

Synonyms

Synonyms	Comment	Organism
dipeptidyl peptidase IV	-	Sus scrofa
DP IV	-	Sus scrofa

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.0000251	-	1-[2-amino-3-(4-iodophenyl)propanoyl]pyrrolidine--2-carbonitrile	-	Sus scrofa