Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.5.1.4 (deaminase)
 5,113 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Proteolytic enzymes from the organism Porphyromonas gingivalis are believed to be involved in the development of periodontitis. Studies on both crude extracts and purified trypsinlike enzymes from this organism indicate that substantial stimulation of both amidase and proteinase activities can be obtained during incubation with glycine-containing compounds. We postulate that P. gingivalis may have developed this unusual property to take advantage of the glycine-rich environment which occurs during the periodontitis-associated degradation of gingival collagen. The finding of such a stimulation in crevicular fluids from discrete periodontal sites has been correlated with the presence of P. gingivalis and could be utilized for the early detection of infection by this organism during the onset of periodontitis.
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PMID:Stimulation of proteinase and amidase activities in Porphyromonas (Bacteroides) gingivalis by amino acids and dipeptides. 185 99

We isolated an enzyme from a major periodontal pathogen, Porphyromonas gingivalis (also called Bacteroides gingivalis), that is capable of initially increasing the coagulant activity of high molecular weight kininogen (HK), releasing bradykinin from HK and low molecular weight kininogen (LK), and destroying the light chain (coagulant portion) of HK. This enzyme, a membrane-bound thiol proteinase that preferentially cleaves the P1-Lys position of tripeptide substrates, is also able to rapidly render fibrinogen nonclottable. We will refer to this enzyme as lys-gingivain because of its origin from P. gingivalis, its classification as a thiol proteinase, and its action as a lysyl-amidase. The activity of lys-gingivain is enhanced by beta-mercaptoethanol, and the enzyme has a molecular mass of 68-70 kDa, a pH optimum of 7.4, and is not inactivated by plasma protease inhibitors. The second-order rate constant for the destruction of the coagulant activity of the HK light chain (surface-binding domain) at 23 degrees C is 2.3 x 10(7) M-1 s-1, and, for cleavages that render fibrinogen unclottable, is 2.05 x 10(6) M-1 s-1. These data suggest that lys-gingivain is a very potent proteinase that would be fully functional in anaerobic periodontal crevices and might participate in the pathogenesis of periodontitis. Lys-gingivain appears to be the most potent kininogenase and fibrase to be described to date.
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PMID:Purification and characterization of a potent 70-kDa thiol lysyl-proteinase (Lys-gingivain) from Porphyromonas gingivalis that cleaves kininogens and fibrinogen. 838 28

Carcinoma of exocrine pancreas is the fourth leading cause of cancer deaths, worldwide. The prevalence of this disease is very high in patients with chronic pancreatitis. Orodigestive cancers are frequently seen in patients with periodontitis. These findings suggest that this type of cancer may have some bacterial origins. This study hypothesizes that the peptidyl arginine deaminase (PAD) enzymes found in oral bacteria may be responsible for the p53 point mutations that occur in patients with pancreatic cancer. Porphyromonas gingivalis, Prevotella intermedia, Tannerella forsythia, and Treponema denticola possess the PAD enzyme, and p53 arginine mutations have been detected in patients with pancreatic cancer. Moreover, the Pro allele p53Arg72-Pro is a risk factor for the development of this cancer. Anti-P. gingivalis antibody titers have been found to be higher in patients with pancreatic cancer as compared to healthy controls. The hypothesis in question can be tested if the DNA of P. gingivalis or the antibodies against P. gingivalis can be detected in patients with the p53 arginine mutation.If this hypothesis is true, it could reveal the real cause of pancreatic cancer, which is a fatal disease. Further studies are necessary in order to confirm this hypothesis.
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PMID:Oral bacteria in pancreatic cancer: mutagenesis of the p53 tumour suppressor gene. 2661 37