Gingipain aminopeptidase activities in Porphyromonas gingivalis. 2012

Florian Veillard, and Barbara Potempa, and Marcin Poreba, and Marcin Drag, and Jan Potempa
Oral Health and Systemic Diseases Research Group, University of Louisville School of Dentistry, Louisville, KY, USA. ftveil01@louisville.edu

Bestatin, a specific inhibitor of metalloaminopeptidases,inhibits the growth of Porphyromonas gingivalis. To identify its target enzyme, a library of fluorescent substrates was used but no metalloaminopeptidase activity was found. The aminopeptidase activity of P. gingivalis was bestatin-insensitive and directed exclusively toward N-terminal arginine and lysine substrates. Class-specific inhibitors and gingipain-null mutants showed that gingipains were the only enzymes responsible for this activity.The kinetic constants obtained for Rgps were comparable to those of human aminopeptidases but Kgp aminopeptidase activity was weaker. This finding reveals a new role for gingipains as aminopeptidases in the degradation of proteins and peptides in P. gingivalis.

UI MeSH Term Description Entries
D007930 Leucine An essential branched-chain amino acid important for hemoglobin formation. L-Leucine,Leucine, L-Isomer,L-Isomer Leucine,Leucine, L Isomer
D003546 Cysteine Endopeptidases ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000080867 Gingipain Cysteine Endopeptidases Cysteine endoproteinases, from periodontal pathogen PORPHYROMONAS GINGIVALIS, acting as virulence factors associated with PERIODONTITIS. They are produced as pre-proproteins which mature into ARGININE and LYSINE specific endopeptidases. Arg-Gingipain,Arginine Gingipain,Gingipain,Gingipain K,Gingipain Proteases,KGP Protease,Lys-Gingipain,Lysine Gingipain,RGP-2 Gingipain,RGPB Protein,Argingipain,Gingipain R,Gingipain R1,Gingipain R2,Gingipains,Arg Gingipain,Cysteine Endopeptidases, Gingipain,Gingipain, Arginine,Gingipain, Lysine,Gingipain, RGP-2,Lys Gingipain,RGP 2 Gingipain
D000626 Aminopeptidases A subclass of EXOPEPTIDASES that act on the free N terminus end of a polypeptide liberating a single amino acid residue. EC 3.4.11. Aminopeptidase
D013379 Substrate Specificity A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts. Specificities, Substrate,Specificity, Substrate,Substrate Specificities
D016866 Bacteroidaceae Infections Infections with bacteria of the family BACTEROIDACEAE. Infections, Bacteroidaceae,Bacteroidaceae Infection,Infection, Bacteroidaceae
D016966 Porphyromonas gingivalis A species of gram-negative, anaerobic, rod-shaped bacteria originally classified within the BACTEROIDES genus. This bacterium produces a cell-bound, oxygen-sensitive collagenase and is isolated from the human mouth. Bacteroides gingivalis
D017353 Gene Deletion A genetic rearrangement through loss of segments of DNA or RNA, bringing sequences which are normally separated into close proximity. This deletion may be detected using cytogenetic techniques and can also be inferred from the phenotype, indicating a deletion at one specific locus. Deletion, Gene,Deletions, Gene,Gene Deletions
D018829 Adhesins, Bacterial Cell-surface components or appendages of bacteria that facilitate adhesion (BACTERIAL ADHESION) to other cells or to inanimate surfaces. Most fimbriae (FIMBRIAE, BACTERIAL) of gram-negative bacteria function as adhesins, but in many cases it is a minor subunit protein at the tip of the fimbriae that is the actual adhesin. In gram-positive bacteria, a protein or polysaccharide surface layer serves as the specific adhesin. What is sometimes called polymeric adhesin (BIOFILMS) is distinct from protein adhesin. Adhesins, Fimbrial,Bacterial Adhesins,Fimbrial Adhesins,Adhesin, Bacterial,Bacterial Adhesin

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