Lactobacillus leichmannii

Deibel et al. produced filamentous Lactobacillus leichmannii in the absence of vitamin B]r Reversion to the normal cell form occurred on the addition of either vitamin B12 to a medium lacking the growth factor or of an excess of the desoxyriboside thymidine. 

In Russia, a popular milk drink traditionally made from unpasteurized mare s milk is known as kumiss. The fermentation is caused principally by L. bulgaricus, lactose-fermenting Torula yeasts, and Lactobacillus leichmannii. 

In certain health food literature, Spirulina, a blue-green algae, has been claimed to be a source of vitamin B12. It appears that this was based on the results obtained from the United States Pharmacopeia microbiological assay for vitamin B12. This assay uses Lactobacillus leichmannii as the test organism and it is known that this organism responds to some vitamin B12 analogs. Herbert and Drivas (H7) found that analogs of the vitamin accounted for more than 80% of what appeared to be vitamin B12. ... 

Incorporation of solvent hydrogen into the substrate does not rule out its transfer as hydride if the source of hydride is dithiol, as in the ribonucleotide reductases. In the most understood enzyme of this type, from Lactobacillus leichmannii, the function of the dithiol (45) is to reduce the cobamide coenzyme (46) and provide a source... 

Booker, S., and Stubbe, J., 1993, Cloning, sequencing, and expression of the adenosylcobal-amin-dependent ribonucleotide reductase from Lactobacillus leichmannii. Proc Natl. Acad. Set U.S.A. 90 8352n8356. 

Brown, M. L., and Li, J., 1998, Activation parameters for the carbon-cobalt bond homolysis of coenzyme B12 induced by the B[2-dependent ribonucleotide reductase from Lactobacillus leichmannii. J. Am. Chem. Soc. 120 9466n9474. 

Lin, A. N., Ashley, G. W., and Stubbe, J., 1987, Location of the redox-active thiols of ribonucleotide reductase sequence similarity between the Escherichia coli and Lactobacillus leichmannii enzymes. Biochemistry 26 6905n6909. 

Lactobacillus leichmannii. Curr. Opin. Chem. Biol. 1998 2 650-655. 

Ribonucleotide reductase has been studied extensively in two bacterial systems Escherichia coli (5) and Lactobacillus leichmannii (6). These two systems differ in their cofactor requirements and in the level of phosphorylation of the substrate. 

D(-)-Lactate Dehydrogenase Origin Lactobacillus leichmannii Roche Diagnostics D(-)-Lactate Dehydrogenase (D-LDH)... 

Unal, R., Kim, J.G., andYoucef, A.E. 2001. Inactivation of Escherichia coli 0151. Wl, Listeria monocytogenes, and Lactobacillus leichmannii by combinations of ozone and pulsed electric field. Journal of Food Processing 64 777-782. 

D-Lactic Acid, (R -2-Hydroxypropanoic acid d( —)-lactic acid levorOtatory lactic acid f-lactic acid D-Milchsiiure (German). C3HtO, mol wt 90,08. C 40,00%, H 6.71%, O 53,29%. Obtained by resolution of DL-lactic acid Purdie, Walker, J, Chem. Soc. 61, 754 (1892) Borsook et at. J. Biol. Chem. 102, 449 (1933). Convenient laboratory prepn from glucose using Lactobacillus leichmannii Brin,... 

Fortunately, a host of methods is available for achieving this goal. They include resolution of a D,L-mixture [238] inversion of L-lactic acid derivatives (see Sections 1.2.1.2 and 1.2.2.2) asymmetric reduction of pyruvates catalytically [239], enzymatically [240], or with chiral boranes [241] and diazotization of D-alanine derivatives, which proceeds with net retention of configuration [242,243]. In addition, D-lactic acid can be obtained by the fermentation of glucose with Lactobacillus leichmannii in the presence of calcium carbonate [244],... 

Radiometric microbiological assays (RMA) for measuring the levels of vitamin B12, folate, and niacin in biological fluids and food were developed using Lactobacillus leichmannii, casei, and plantarum, respectively- In the presence of the appropriate Cdabeled substrate, these organisms readily produce directly proportional to the amount of the... 

To search for the potential C-labeled substrate, several C compounds that were known to be metabolized by the microorganism were tested in the presence and absence of the essential nutrient in question. For the vitamin B12, we found that in the presence of guanido- C-arginine and cyanocobalamin (CN—Cbl) (27) Lactobacillus leichmannii produced the most significant amount of C02 within 16 h (Table II). Not every C-labeled compound tested was metabolized to 2 by L. leichmannii. On the other hand, U- C and 1- C glucose were metabolized even in the absence of CN—Cbl (Table II). 

During the process of purifying the two known nucleoside deoxyribosyl transferase activities from Lactobacillus leichmannii, a third isoenzyme was assayed, which... 

It is known that the microorganism Lactobacillus leichmannii has two nucleoside deoxyribosyl transferases, DRT I (which has no EC number yet) and DRT II (EC... 

If the microorganism Lactobacillus leichmannii is cultivated in the presence of 10 pM coenzyme B 12 and 125 pM adenosine, the enzyme V2 is in a conformation which results in a lag" in the progress curve v/t (the first feature of the practical recognition of hysteresis (see Figure 6). 

Within these groups there may be further substantial structure differences among individual enzymes. The long-held view that Lactobacillus leichmannii ribonucleotide reductase is typical of all B 12-dependent, and E. coli reductase of all other enzymes including the eukaryotic ones appears no longer warranted. 

The fermentative bacteria, Lactobacillus leichmannii probably possess the most simple of all ribonucleotide reductases, but the protein does require the most complex coenzyme known, 5 -deoxyadenosylcobalamin (Fig. 1). This corrinoid coenzyme catalyzes but few enzymatic reactions, usually involving an intramolecular 1,2-hydrogen shift as found in the common methylmalonylCoA succinylCoA isomerase reaction. Participation in deoxyribonucleotide formation, where hydrogen transfer occurs intermolecularly (Eq. I), was first implicated by the nutritional requirement of lactobacilli for vitamin B12 during DNA synthesis, and was verified in cell-free extracts by Blakley and H. A. Barker in 1964 The reaction has been studied in great detail in the laboratories of Beck Blakley and Hogenkamp ... 

Table 5. Kinetic data and effector specificity for reduction of natural and synthetic, or modified ribonucleotides catalyzed by the triphosphate reductase of Lactobacillus leichmannii and diphosphate reductase of E. coll, respectively. (Data from Ref. 135,136, 142)... 

Fig. 13. Dependence of the specific activities of Lactobacillus leichmannii (left) and Escherichia coli (right) ribonucleotide reductases upon coenzyme B12 and subunit B 2 concentration, respectively, in the absence and presence of allosteric effector nucleotides (dGTP for ATP reduction, dTTP for CDP reduction). Conditions as in Table 5...

C3HJO3, Mr 90.08. The racemate and the enantiomers occur in nature. (/f)-Form, mp. 53 °C, [0] -2.6° (HjO), pK 3.83. Prismatic platelets, soluble in water, ethanol, and ether, insoluble in chloroform. (/ )-(-)-L. is formed in the fermentation of glucose by Lactobacillus leichmannii and L. delbrueckii with 1 - and 2-valent metal ions it forms dextrorotatory salts and laevorotatory salts with 3-valent metal ions, e.g., zinc D-(+)-lactate 2H2O, [alo" -i-8.18° (HjO). (5)-form (sarcolactic acid, paralactic acid), mp. 53 °C, [ajp l 3.82° (H2O), pKg 3.79 (25 °C), is highly hygroscopic, occurs in blo, muscles serum, bile, kidneys, and other organs. The content of L. increases after strenuous muscle activity (lactate acidosis). The racemate, oil.mp. 17°C,bp. 122 °C(1.86 kPa), steam distillable, is widely distributed in nature, e. g., in sour milk products, in molasses as a result of partial fermentation of the sugars from apples and other fruits. For biochemistry and preparation, see Ut.. ... 

Reduction of ATP to the 2 -deoxy-compound has been carried out on a preparative scale using recombinant Lactobacillus leichmannii ribonucleotide triphosphate reductase. ... 

An efficient double oxidation of D-xylose to D-gf/ycero-aldopentos-2,3-diulose (2,3-diketo-D-xylose, 45) has been achieved (80% yield) using pyranose dehydrogenase from the mushroom Agaricus bisporus (Scheme 9). The gram scale 2 -deoxygenation of ATP has been achieved using a recombinant ribonucleoside triphosphate reductase from Lactobacillus leichmannii ... 

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