• Microbiology and Biotechnology Letters
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• v.19 no.6
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• pp.588-591
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• 1991

S-adenosyl-L-methionine (SAM) is essential substrate for biological methylation reactions. The present work describes a reoptimized procedure of SAM preparation in laboratory scale by the method of yeast fermentation. The fermentation medium enriched with methionine and the culture conditions were reoptimized. The isolation steps consisted of 5 steps including extractions, precipitations, and chromatography. This improved procedure over original method provides relatively high yield of biologically active product within a 4 day-period.

• Journal of Applied Biological Chemistry
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• v.50 no.4
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• pp.288-292
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• 2007

• Journal of Microbiology and Biotechnology
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• v.16 no.5
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• pp.799-803
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• 2006

It was reported that an accumulation of Sadenosyl-L-methionine increases production of actinorhodin in Streptomyces lividans and induces antibiotic biosynthetic genes. We also obtained the same result in Streptomyces coelicolor A3(2). Therefore, in order to identify proteins changed by the addition of S-adenosyl-L-methionine in S. coelicolor A3(2), LC/MS/MS analyses were carried out. Thirteen proteins that were not observed in the control were found.

• Proceedings of the Botanical Society of Korea Conference
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• 1999.04a
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• pp.14-14
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• 1999

• Archives of Pharmacal Research
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• v.22 no.3
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• pp.237-242
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• 1999

A proteinacious inhibitor with a molecular weight of 1,600 Da which inhibits S-adenosyl-L-methionine-dependent transmethylation reactions was purified from porcine liver to homogeneity by procedures including boiling, Sephadex G-25 column chromatography and repeated HPLC. Employing both Nuclear Magnetic Resonance (NMR) and Fast Atom Bombardment-Mass (FAB-Mass) spectroscopy, S-adenosylhomocysteine was conclusively identified as an integral part of the inhibitor. The purified S-adenosylhomocysteine was competitive with S-adenosyl-L-methionine with Ki value of $6.3{\times}10^{-6}$ M towards protein methylase II.

• YAKHAK HOEJI
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• v.38 no.4
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• pp.430-439
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• 1994

S-Adenosyl-L-methionine synthetase (ATP: methionine S-Adenosyltransferase, EC 2.5.1.6; AdoMet synthetase) catalyzes the biosynthesis of S-Adenosyl-L-methionine(AdoMet) from methionine in the presence of ATP. To elucidate the role of transmethylation reaction in the pancreatic tissues, we examined AdoMet synthetase and isozyme activities, and AdoMet contents in the various tissues. The activities of AdoMet synthetase marked the highest in the kidney, and the lowest in the testis among the various tissues of rat. Considerable amounts of AdoMet synthetase activities were detected in the pancreatic tissues of various animals except for those of frog. The level of ${\alpha}$ and ${\gamma}$ isozyme activities were present in the pancreatic tissues of various animals, while ${\beta}$ isozyme activities were detected as trace. AdoMet synthetase activities of rat brain, liver, testis were decreased with growth. In the rat pancreatic tissues, AdoMet synthetase activities were increased during 16 days after birth and then decreased between 16 and 47 days of age. Levels of AdoMet contents of rat brain and testis were decreased with growth. However, AdoMet contents of rat pancreas were decreased until 26 days of age, and then increased thereafter. AdoMet synthetase isozyme patterns did not vary with growth in the pancreas and testis. But, in the liver, ${\beta}$ form is strikingly increased with growth.

• Food Science and Biotechnology
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• v.17 no.1
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• pp.184-187
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• 2008

S-Adenosyl-L-methionine (SAM) is an important metabolic intermediate in living organisms and participates in many reactions as a methyl group donor. SAM has been used as a dietary supplement and is proposed to have beneficial effects on the liver and brain. The aim of this study was to find lactic acid bacteria with high SAM-producing ability to be used as SAM enhancing probiotics. We used high performance liquid chromatography (HPLC) to quantify the amount of SAM produced, and found that Bifidobacterium bifidum BGN4 produced a significantly higher amount of SAM than other Bifidobacterium or Lactobacillus strains. The effect of various carbon and nitrogen sources on SAM production was examined. This study confirmed that Bifidobacterium may be utilized as a source of SAM in the functional food industry.

• YAKHAK HOEJI
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• v.31 no.5
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• pp.266-272
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• 1987

It is reasonably well known that there is a relationship between myelin formation and methylation of myelin basic protein in nerve cells. One of the suggestions is that arginine methylation of myelin basic protein could be of aid in the conjugation of myelin protein with the nonpolar lipid to form myelin. Abnormality in methylation of myclin basic protein might induce the neurological diseases in experimental animals as well as in human being. In the biological system, the methylation reaction is catalyzed by protein methaylse I using S-adenosyl-L-methionine as methyl donor. In this study, we examined the changes of S-adenosyl-L-methionine concentration and protein methylase I activity in developing rat brain tissues. The results are sumraerized as followings: (1) In brain tissues of fetus rat, the concentration of S-adenosyl-L-methionine was gradually decreased until to birth. However, the concentration in brain tissues of infant rat was suddenly increased at 7th day(just before myelination occur) birth. (2) Protein methylase I activity was decreased until to birth in brain of fetus rat and increased temporally just after birth, However, the enzyme activity showed no changes around 7th day after birth.

• Journal of Microbiology and Biotechnology
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• v.16 no.7
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• pp.1154-1157
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• 2006

It is known that overexpression of S-adenosyl-L-methionine (SAM) synthetase or exogenous addition of SAM enhances the production of actinorhodin, one of pigmented antibiotics found from Streptomyces coelicolor. In order to discover a novel compound as a signal molecule to produce actinorhodin instead of SAM, several compounds were synthesized based on the relationships between structures of the SAM analogues and their actinorhodin productivities. Of these, a few compounds showed better productivities of actinorhodin than SAM.

• Food Science and Biotechnology
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• v.17 no.4
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• pp.857-860
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• 2008

S-Adenosyl-L-methionine (SAM) is a bioactive material used in the treatment of depression, osteoarthritis, and liver disease. To obtain lactic acid bacteria (LAB) producing high concentrations of SAM, LAB were isolated from commercial kimchi and from prepared kimchi products that contained shrimp jeotgal (fermented salty seafood) or sand lance jeotgal or that were fermented at 5 or $10^{\circ}C$, respectively, when pH was 4.2 to 4.8 and titratable acidity 0.6 to 0.9. Among the 179 LAB strains isolated from the fermented kimchi products, the genus Leuconostoc produced the highest intracellular level of SAM (1.58 mM) and Lactobacillus produced the second highest level (up to 1.47 mM) in the strain culture. This is the first study to quantify SAM in LAB isolated from fermented kimchi prepared by a general kimchi recipe. Ultimately, the selected strains (Leuconostoc mesentroides subsp. mesenteroides/dextranicum KSK417, L. mesentroides subsp. mesenteroides/dextranicum KJM401, and Lactobacillus bifermentans QMW327) could be useful as starters to manufacture fermented foods containing high levels of SAM.