Expression, purification and preliminary crystallographic analysis of dipeptidyl peptidase IV fromPorphyromonas gingivalis

Expression, purification and preliminary crystallographic analysis of dipeptidyl peptidase IV from Porphyromonas gingivalis.

The asaccharolytic periodontopathogen Porphyromonas gingivalis produces membrane-anchored proteases such as dipeptidyl peptidase IV that are involved in the destruction of host periodontal tissue. The extracellular domain of this enzyme was overexpressed in Escherichia coli as an N-terminal His-tag fusion protein, purified using standard metal-affinity chromatography and crystallized using the ...

Dipeptidyl peptidase IV of Streptococcus anginosus: purification and characterization.

We found that N-unblocked nine p-nitroanilde derivatives of amino acids or peptides were hydrolyzed by the crude cell extracts of Streptococcus anginosus NCTC 10713. Then dipeptidyl peptidase IV was purified 323-fold by the procedures including ammonium sulfate concentration, anion exchange chromatography (twice), gel filtration (twice), hydrophobic interaction chromatography, and isoelectric f...

Emerging family of proline-specific peptidases of Porphyromonas gingivalis: purification and characterization of serine dipeptidyl peptidase, a structural and functional homologue of mammalian prolyl dipeptidyl peptidase IV.

Porphyromonas gingivalis is an asaccharolytic and anaerobic bacterium that possesses a complex proteolytic system which is essential for its growth and evasion of host defense mechanisms. In this report, we show the purification and characterization of prolyl dipeptidyl peptidase IV (DPPIV) produced by this organism. The enzyme was purified to homogeneity, and its enzymatic activity and biochem...

Targeting Dipeptidyl Peptidase IV (CD26)

Crystallization and preliminary crystallographic analysis of porcine acylaminoacyl peptidase.

Acylaminoacyl peptidase (also known as acylamino-acid-releasing enzyme or acylpeptide hydrolase; EC 3.4.19.1) is an unusual member of the prolyl oligopeptidase family catalysing the hydrolysis of an N-acylated peptide to an acylamino acid and a peptide with a free N-terminus. Acylaminoacyl peptidase purified from porcine liver has been crystallized in mother liquor containing 0.1 M Tris-HCl pH ...