Isolation and properties of bacteriolytic enzyme-producing cocci from the human mouth. 1996

T Kanamoto, and H Eifuku-Koreeda, and M Inoue
Department of Preventive Dentistry, Kagoshima University Dental School, Japan.

One-hundred-and-one bacteriolytic enzyme producing organisms were isolated from various sites of the mouth. All were non-hemolytic, Gram-positive, and chain-forming cocci. Ninety-one strains, like the reference strains of Streptococcus defectivus and S. adjacens, were dependent on pyridoxal for growth and produced a chromophore. The Rapid ID32 STREP system speciated these isolates as S. defectivus, S. adjacens or Gemella morbillorum. The remaining 10 bacteriolytic isolates were pyridoxal-independent and 8 belonged to S. intermediate. Some pyridoxal-independent S. intermedius reference strains including ATCC27335T and all group D Enterococcus strains tested were also bacteriolytic. Thus, bacteriolytic enzyme production is common to nutritionally variant streptococci but not unique to S. defectives and S. adjacens. The nutritionally variant strains generally had arylamidases but not alkaline phosphatase. The S. defectivus strains produced alpha-and beta-galactosidases (biotype 1) whereas the S. adjacens strains generally produced N-acetyl-beta-glucosaminidase and some had beta-glucuronidase but others did not (biotypes 2 and 3). The C. morbillorum strains had no detectable activity of these glycosidases (biotype 4) but produced a chromophore and an arginine dihydrolase, exhibiting a physiological profile atypical of the Gemella species. This indicates the possible presence of an additional phenotypic group or a new species among the nutritionally variant streptococci.

UI MeSH Term Description Entries
D009055 Mouth The oval-shaped oral cavity located at the apex of the digestive tract and consisting of two parts: the vestibule and the oral cavity proper. Oral Cavity,Cavitas Oris,Cavitas oris propria,Mouth Cavity Proper,Oral Cavity Proper,Vestibule Oris,Vestibule of the Mouth,Cavity, Oral
D010860 Pigments, Biological Any normal or abnormal coloring matter in PLANTS; ANIMALS or micro-organisms. Biological Pigments
D011730 Pyridoxal The 4-carboxyaldehyde form of VITAMIN B 6 which is converted to PYRIDOXAL PHOSPHATE which is a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid.
D004798 Enzymes Biological molecules that possess catalytic activity. They may occur naturally or be synthetically created. Enzymes are usually proteins, however CATALYTIC RNA and CATALYTIC DNA molecules have also been identified. Biocatalyst,Enzyme,Biocatalysts
D005966 Glucuronidase Endo-beta-D-Glucuronidase,Endoglucuronidase,Exo-beta-D-Glucuronidase,beta-Glucuronidase,Endo beta D Glucuronidase,Exo beta D Glucuronidase,beta Glucuronidase
D006095 Gram-Positive Cocci Coccus-shaped bacteria that retain the crystal violet stain when treated by Gram's method. Gram Positive Cocci
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000118 Acetylglucosaminidase A beta-N-Acetylhexosaminidase that catalyzes the hydrolysis of terminal, non-reducing 2-acetamido-2-deoxy-beta-glucose residues in chitobiose and higher analogs as well as in glycoproteins. Has been used widely in structural studies on bacterial cell walls and in the study of diseases such as MUCOLIPIDOSIS and various inflammatory disorders of muscle and connective tissue. N-Acetyl-beta-D-glucosaminidase,Chitobiase,N,N-Diacetylchitobiase,N-Ac-beta-Glucosaminidase,NAGase,beta-D-Acetamido-2-Deoxyglucosidase,beta-D-N-acetylglucosaminidase,beta-N-Acetylglucosaminidase,N Ac beta Glucosaminidase,N Acetyl beta D glucosaminidase,N,N Diacetylchitobiase,beta D Acetamido 2 Deoxyglucosidase,beta D N acetylglucosaminidase,beta N Acetylglucosaminidase
D000469 Alkaline Phosphatase An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.1.
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

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