Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.21 (beta-glucosidase)
 3,280 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Fifty-six strains of lactobacilli were examined for the production of glycosidases and proteases (arylamidases) that could be associated with the ability to grow in vivo and/or be a factor in the pathogenesis of endocarditis. The strains were from seven species, with an emphasis on Lactobacillus rhamnosus and Lact. paracasei subsp. paracasei, both of which have been associated with endocarditis and provided 12 of the 13 strains isolated from cases of the disease. Other species were Lact. acidophilus, Lact. plantarum, Lact. salivarius, Lact. fermentum and Lact. oris. Commonly expressed glycosidase activities were alpha-D-galactosidase and beta-N-acetyl-D-glucosaminidase followed by beta-D-glucosidase and alpha-L-fucosidase. The combined production of beta-N-acetyl-D-glucosaminidase and alpha-D-galactosidase was a feature of the endocarditis isolates. In contrast, beta-D-galactosidase was produced by very few of the strains within species implicated in endocarditis but most of the strains of Lact. salivarius, Lact. fermentum and Lact. oris. The most commonly produced arylamidases active against substrates employed for testing human blood clotting cascade were activated protein C(Ca)-like, activated factor X(Xa)-like and Hageman factor-like followed by kallikrein-like and chymotrypsin-like enzymes.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Enzyme production by lactobacilli and the potential link with infective endocarditis. 769 50

The effects of growth conditions on the properties of the endocarditis-producing oral bacterium Streptococcus sanguis FSS2 were studied. This strain produces a variety of proteases and glycosidases, including a thrombin-like activity that is a potential virulence factor for endocarditis. Cultures were grown with limiting glucose or galactose in chemostats over a range of dilution rates and pH levels, and the following activities were measured at pH 7.5: thrombin-like, Hageman factor-like, N-acetyl-beta-D-galactosaminidase, beta-D-glucosidase, and beta-D-galactosidase. At growth pH 6.5, specific activities generally decreased as the dilution rate increased from 0.05 to 0.40 h(-1). At a dilution rate of 0.1 h(-1), specific activities generally were highest at growth pH 6.5 and lower and approximately equal at growth pH 5.5 and 7.5. The major exception was the thrombin-like activity, for which the specific activity at growth pH 7.5 was approximately 5-fold higher than at growth pH 5.5. Hageman factor-like activity was apparently glucose catabolite repressible, as its activity was 3-fold higher in galactose cultures. The measured activities changed as functions of growth conditions and thus were modulated by environment. Environmental regulation of thrombin-like activity by pH is consistent with an activity that is less important on tooth surfaces than in tissues.
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PMID:Modulation of glycosidase and protease activities by chemostat growth conditions in an endocarditis strain of Streptococcus sanguis. 860 41