scholarly journals The Q rule in Bacteriodetes and the identification and characterization of Porphyromonas gingivalis Glutaminyl Cyclase.

2019 ◽  
Author(s):  
John Houston
Keyword(s):  
Porphyromonas Gingivalis ◽  
Glutaminyl Cyclase ◽  
Identification And Characterization

Structural and kinetic characterization of Porphyromonas gingivalis glutaminyl cyclase

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Sebastiaan Lamers ◽  
Qiaoli Feng ◽  
Yili Cheng ◽  
Sihong Yu ◽  
Bo Sun ◽  
...  
Keyword(s):  
Porphyromonas Gingivalis ◽  
Catalytic Mechanism ◽  
Biochemical Characterization ◽  
Bacterial Species ◽  
Benzimidazole Derivative ◽  
Amyloid Peptide ◽  
Glutaminyl Cyclase ◽  
Chemistry Development ◽  
Human Ortholog

Abstract Porphyromonas gingivalis is a bacterial species known to be involved in the pathogenesis of chronic periodontitis, that more recently has been as well associated with Alzheimer’s disease. P. gingivalis expresses a glutaminyl cyclase (PgQC) whose human ortholog is known to participate in the beta amyloid peptide metabolism. We have elucidated the crystal structure of PgQC at 1.95 Å resolution in unbound and in inhibitor-complexed forms. The structural characterization of PgQC confirmed that PgQC displays a mammalian fold rather than a bacterial fold. Our biochemical characterization indicates that PgQC uses a mammalian-like catalytic mechanism enabled by the residues Asp149, Glu182, Asp183, Asp218, Asp267 and His299. In addition, we could observe that a non-conserved Trp193 may drive differences in the binding affinity of ligands which might be useful for drug development. With a screening of a small molecule library, we have identified a benzimidazole derivative rendering PgQC inhibition in the low micromolar range that might be amenable for further medicinal chemistry development.

scholarly journals Identification and Characterization of Histatin 8 Receptors on Porphyromonas gingivalis Cell Surfaces.

1992 ◽  
Vol 42 (5) ◽  
pp. 689-695 ◽  
Author(s):  
Yukitaka MURAKAMI ◽  
Satoshi SHIZUKUISHI ◽  
Akira TSUNEMITSU ◽  
Kazuhisa NAKASHIMA ◽  
Yukio KATO ◽  
...  
Keyword(s):  
Porphyromonas Gingivalis ◽  
Cell Surfaces ◽  
Gingivalis Cell ◽  
Identification And Characterization ◽  
Histatin 8

scholarly journals 19. Identification and characterization of the Porphyromonas gingivalis hemK gene

2000 ◽  
Vol 54 (4) ◽  
pp. 373
Author(s):  
Akito Kusaba ◽  
Sumio Akifusa ◽  
Toshihiro Ansai ◽  
Tadamichi Takehara
Keyword(s):  
Porphyromonas Gingivalis ◽  
Identification And Characterization

scholarly journals Lysine-specific gingipain K and heme/hemoglobin receptor HmuR are involved in heme utilization in Porphyromonas gingivalis.

2004 ◽  
Vol 51 (1) ◽  
pp. 253-262 ◽  
Author(s):  
Waltena Simpson ◽  
Teresa Olczak ◽  
Caroline A Genco
Keyword(s):  
Porphyromonas Gingivalis ◽  
Type Strain ◽  
Double Mutant ◽  
Wild Type Strain ◽  
Wild Type ◽  
Outer Membrane Receptor ◽  
Iron Source ◽  
Identification And Characterization

We have previously reported on the identification and characterization of the Porphyromonas gingivalis A7436 strain outer membrane receptor HmuR, which is involved in the acquisition of hemin and hemoglobin. We demonstrated that HmuR interacts with the lysine- (Kgp) and arginine- (HRgpA) specific proteases (gingipains) and that Kgp and HRgpA can bind and degrade hemoglobin. Here, we report on the physiological significance of the HmuR-Kgp complex in heme utilization in P. gingivalis through the construction and characterization of a defined kgp mutant and a hmuR kgp double mutant in P. gingivalis A7436. The P. gingivalis kgp mutant exhibited a decreased ability to bind both hemin and hemoglobin. Growth of this strain with hemoglobin was delayed and its ability to utilize hemin as a sole iron source was diminished as compared to the wild type strain. Inactivation of both the hmuR and kgp genes resulted in further decreased ability of P. gingivalis to bind hemoglobin and hemin, as well as diminished ability to utilize either hemin or hemoglobin as a sole iron source. Collectively, these in vivo results further confirmed that both HmuR and Kgp are involved in the utilization of hemin and hemoglobin in P. gingivalis A7436.

Identification and characterization of a UbK family kinase in Porphyromonas gingivalis which phosphorylates the RprY response regulator

2021 ◽  
Author(s):  
John D. Perpich ◽  
Lan Yakoumatos ◽  
Parker Johns ◽  
Kendall S. Stocke ◽  
Zackary R. Fitzsimonds ◽  
...  
Keyword(s):  
Porphyromonas Gingivalis ◽  
Response Regulator ◽  
Identification And Characterization
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