Cereus licheniformis

Amino acids E. cloacae-214 (Ref. 46) E. coli B. cereus B. licheniformis S. aureus ... 

Although much of the early work on the j3-lactamases was carried out with Gram-positive bacteria such as B. cereus [171], B. licheniformis [172] and Staphylococcus aureus [173], recent studies have shown the enzymes to play an important role in resistance of the enterobacteraceae and Ps. aeruginosa to the /3-lactam antibiotics [141]. 

Over 80 different (3-lactamases are now known. One classification is a system that divides the enzymes into three classes A, B, and C. Classes A and C are active-site serine enzymes. The serine residue in class A enzymes is at position 70. This class contains four major (3-lactamases 749/C (from B. licheniformis), PCI (from S. aureus), 569/H P-lactamase I (from B. cereus), and PBR322 and RTEM (from E. coli). As with other serine-type hydrolytic enzymes (acetylcholinesterase, trypsin), the mechanism of action requires initial formation of an acylated enzyme, in this case acylation of ser-70 followed by hydrolysis of the derivative to regenerate the enzyme ... 

It should be appreciated, however, that the enzymes of a functionally similar type may not infrequently be cell-bound in one species of bacterium and in another they may be extracellular—e.g.9 penicillinase and alkaline phosphatase of E. coli are cell-bound, whereas those of Bacillus cereus are extracellular (6). Even in the same strain of bacterium, an enzyme may be partly cell-bound and partially extracellular penicillinase of Bacillus licheniformis is an example (60). Consequently, the above classification is not so distinctive and may change, depending on the circumstances of cells or by their mutation. 

Taylor, J.M. et al. (2005) Fleat-stable toxin production by strains of Bacillus cereus. Bacillus firmus. Bacillus mega-terium. Bacillus simplex and Bacillus licheniformis. FEMS Microbiol. Lett., 242 (2), 313-317. 

B. cereus, B. globigii spores, B. subtilis, MS-2 aldolase, E. coli, Secale cerate, coliphage, fog oil, diesel and wood smoke, pollen, type X, dry yeast B. cereus, B. licheniformis, B. subtilis, E. coli, S. aureus... 

B. cereus, B. licheniformis, B. subtilis, B. thuringiensis, E. coli, S. aureus... 

Microbiota predominating the kinema fermentation were studied. The functional microorganisms are Bacillus species, B. subtilis, Bacillus licheniformis. Bacillus cereus. Bacillus circulans, Bacillus thuringiensis and Bacillus sphaericus (Sarkar, Hasenack, Nout, 2002). In addition, some bacteria are found frequently that have their origin in post-contamination after cooking. These include Enterococcus faecium and yeasts such as Candida parapsilosis and Geotrichum candidum (Sarkar et al., 1994). 

The inducible formation of penicillinase in B. cereus, S. aureus, and B. licheniformis shares common features— particularly the apparent action of the inducer at the cell surface, and (relatively) slow response. 

Davies [84] reported irreversible binding of penicillin to B. licheniformis 749 of 5000 molecules per cell (at 0°C), several-fold the level of binding to B. cereus and S. aureus. Though penicillinase synthesis decreased about 2 hours after induction, no release of the bound penicillin was detected. 

Davies (unpublished observations, 1970) has noted that the binding of penicillin to B. licheniformis 749 doubled when the experiment is carried out at 37°C instead of 0°C however, cells loaded with penicillin at 0°C induce poorly or not at all on regrowth at 37°C. This is in direct contrast to the behavior of B. cereus 569 (see Section III, A, 1). 

The three penicillinase regulation systems in B. cereus, B. licheni-formis, and S. aureus show similarities in properties, though the comparisons can be taken only to a certain point. To compound the evidence from these three systems into a single model may be incorrect, but it is defensible on the basis of Occam s razor, and from the observation that the penicillinase systems of B. licheniformis and S. aureus show at least a similar degree of genetic complexity, coupled with the fact that the penicillinases from these two organisms have been shown to share about 40 % identity of amino-acid sequence [Ambler and Meadway, 91]. 

Obt. from polysaccharides of Chromobacterium violaceum. Bacillus licheniformis, Bacillus subtilis. Bacillus cereus and Staphylococcus aureus. Also in swine erysipelas bacteria Erysipelothix insidiosa). 

Femandez-No IC, Bohme K, Diaz-Bao M, Cepeda A, Barros-Velazquez J, Calo-Mata P. Char-aeterisation and profiling of Bacillus subtilis. Bacillus cereus and Bacillus licheniformis by MALDI-TOF mass fingerprinting. Food Microbiol. 2013 33(2) 235 2. 

Bacillus licheniformis Bacillus circulans Bacillus amyloliquefaciens Bacillus cereus Bacillus megaterium Aspergillus niger... 

In general, biosensing of IMP is performed by sequential applications of 5 -nucleotidase (or alkaline phosphatase), nucleoside phosphorylase, and xanthine oxidase, and the oxygen consumption or UA production by the final enzymatic reaction (xanthine oxidase) is monitored. The series of enzymatic reactions, however, is complicated, and the optimal conditions for each of these three enzymes are different. Matsumoto et al. [7] reported a simpler enzymatic system that used IMP dehydrogenase (IMPDH) from Bacillus cereus and NADH oxidase (NOD) from Bacillus licheniformis. 

Glu-166 This residue is a strong candidate for a general base catalyst of /3-lactamase. Substitution of Glu-166, which is conserved in class A )8-lactamases, by Gin in the /3-lactamase I of B. cereus 569/H (53) or the jS-lactamase of B. licheniformis 749C (39) results in a nearly complete loss of catalytic activity. 

---