Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

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.
    View publication on PubMedView publication on EuropePMC

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