Literature summary 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
EC Number |
Application |
Comment |
Organism |
---|
3.4.14.5 |
pharmacology |
enzyme is a target for drug design |
Sus scrofa |
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
3.4.14.5 |
DNA sequence determination and analysis |
Sus scrofa |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
3.4.14.5 |
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
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
3.4.14.5 |
1-[2-amino-3-(4-iodophenyl)propanoyl]pyrrolidine--2-carbonitrile |
- |
Sus scrofa |
|
Localization
EC Number |
Localization |
Comment |
Organism |
GeneOntology No. |
Textmining |
---|
3.4.14.5 |
membrane |
- |
Sus scrofa |
16020 |
- |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.4.14.5 |
Sus scrofa |
P22411 |
- |
- |
Posttranslational Modification
EC Number |
Posttranslational Modification |
Comment |
Organism |
---|
3.4.14.5 |
glycoprotein |
N-glycosylation at Asn279 is important for adenosine deaminase binding |
Sus scrofa |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
3.4.14.5 |
from kidney cortex, 280fold |
Sus scrofa |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
3.4.14.5 |
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 |
|
Source Tissue
EC Number |
Source Tissue |
Comment |
Organism |
Textmining |
---|
3.4.14.5 |
kidney |
cortex |
Sus scrofa |
- |
Specific Activity [micromol/min/mg]
EC Number |
Specific Activity Minimum [µmol/min/mg] |
Specific Activity Maximum [µmol/min/mg] |
Comment |
Organism |
---|
3.4.14.5 |
42 |
- |
above, purified enzyme |
Sus scrofa |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
3.4.14.5 |
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
EC Number |
Subunits |
Comment |
Organism |
---|
3.4.14.5 |
dimer |
is likely to enhance the receptor-ligand affinity by bivalent interaction which may be critical for signal transduction into the cell |
Sus scrofa |
3.4.14.5 |
More |
oligomerization study |
Sus scrofa |
3.4.14.5 |
tetramer |
dimerization of dimers on the cell surface |
Sus scrofa |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
3.4.14.5 |
dipeptidyl peptidase IV |
- |
Sus scrofa |
3.4.14.5 |
DP IV |
- |
Sus scrofa |
Ki Value [mM]
EC Number |
Ki Value [mM] |
Ki Value maximum [mM] |
Inhibitor |
Comment |
Organism |
Structure |
---|
3.4.14.5 |
0.0000251 |
- |
1-[2-amino-3-(4-iodophenyl)propanoyl]pyrrolidine--2-carbonitrile |
- |
Sus scrofa |
|