Biological activities of racemomycin-B, .BETA.-lysine rich streptothricin antibiotic, the main component of Streptomyces lavendulae OP-2.

Inamori, Yoshihiko; Amino, Hisako; Tsuboi, Mariko; Yamaguchi, Satomi; Tsujibo, Hiroshi

doi:10.1248/cpb.38.2296

Cited by 6 publications

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“…Clostridia use LAM in the metabolism of ( S )-α-lysine as a source of carbon and nitrogen and so require a high activity. In other organisms, β-lysine is used in cellular defense mechanisms, such as the production of antibiotics ( − ). In E. coli and Bacillus sp., high activity may not be beneficial in the production of the few molecules of β-lysine required to produce a specialized molecule.…”

Section: Discussionmentioning

confidence: 99%

“…Lysine 2,3-aminomutase (LAM) from Clostridium subterminale SB4 is encoded by the gene kamA and catalyzes the interconversion of ( S )-α-lysine and ( S )-β-lysine ( − ). This enzyme plays a role in lysine metabolism in species such as C. subterminale and Porphyromonas gingivalis , whereas in species such as Streptomyces sp., β-lysine produced by LAM is a constituent of a family of structurally diverse antibiotics ( − ). The action of LAM requires SAM, a [4Fe-4S] cluster, and PLP to catalyze the isomerization of ( S )-α-lysine ( − ).…”

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confidence: 99%

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Enantiomeric Free Radicals and Enzymatic Control of Stereochemistry in a Radical Mechanism: The Case of Lysine 2,3-Aminomutases

Behshad

et al. 2006

Biochemistry

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The product of yjeK in Escherichia coli is a homologue of lysine 2,3-aminomutase (LAM) from Clostridium subterminale SB4, and both enzymes catalyze the isomerization of (S)- but not (R)-alpha-lysine by radical mechanisms. The turnover number for LAM from E. coli is 5.0 min(-1), 0.1% of the value for clostridial LAM. The reaction of E. coli LAM with (S)-alpha-[3,3,4,4,5,5,6,6-(2)H8]lysine proceeds with a kinetic isotope effect (kH/kD) of 1.4, suggesting that hydrogen transfer is not rate-limiting. The product of the E. coli enzyme is (R)-beta-lysine, the enantiomer of the clostridial product. Beta-lysine-related radicals are observed in the reactions of both enzymes by electron paramagnetic resonance (EPR). The radical in the reaction of clostridial LAM has the (S)-configuration, whereas that in the reaction of E. coli LAM has the (R)-configuration. Moreover, the conformations of the beta-lysine-related radicals at the active sites of E. coli and clostridial LAM are different. The nuclear hyperfine splitting between the C3 hydrogen and the unpaired electron at C2 shows the dihedral angle to be 6 degrees, unlike the value of 77 degrees reported for the analogous radical bound to the clostridial enzyme. Reaction of (S)-4-thialysine produces a substrate-related radical in the steady state of E. coli LAM, as in the action of the clostridial enzyme. While (S)-beta-lysine is not a substrate for E. coli LAM, it undergoes hydrogen abstraction to form an (S)-beta-lysine-related radical with the same stereochemistry of hydrogen transfer from C2 of (S)-beta-lysine to the 5'-deoxyadenosyl radical as in the action of the clostridial enzyme. The resulting beta-lysyl radical has a conformation different from that at the active site of clostridial LAM. All evidence indicates that the opposite stereochemistry displayed by E. coli LAM is determined by the conformation of the lysine side chain in the active site. Stereochemical models for the actions of LAM from C. subterminale and E. coli are presented.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Enantiomeric Free Radicals and Enzymatic Control of Stereochemistry in a Radical Mechanism: The Case of Lysine 2,3-Aminomutases

Behshad

et al. 2006

Biochemistry

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“…Once they were introduced into the cell by electroporation, all three peptides were able to inhibit cell growth at concentrations of 10 times lower than their MICs (Liang and Kim, 1999). The antimicrobial activity of racemomycin compounds tended to be stronger with increase in the number of beta-lysine moieties in the molecule (Inamori et al, 1990).…”

Section: Antimicrobial Peptidesmentioning

confidence: 98%

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2001

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Lysine, an essential cationic amino acid, has a positively charged R group. The structure of lysine is given as (H(3)N(+)-)CH(-COO(-))-CH(2)-CH(2)-CH(2)-CH(2)-N(+)H(3).While the anabolic role(s) of the molecule has been in focus for quite a few decades now, its biological properties, e.g. role in cellular proliferation in vitro (both anchorage dependent and anchorage independent) and in vivo, its ability to induce strong inflammatory and immune responses - both humoral and cell mediated, its role in augmented healing of all types of wounds in animal models as well as in human subjects (both acute and chronic), as well as its role in inducing extensive angiogenic responses, have never received reasonable attention so far. In the current brief and indicative review (rather than exhaustive reviews of each area), we intend to bring these biological properties of the molecule to focus while discussing a few other interesting aspects - lysine as a food preservative as well as its possible role(s) in immune therapy. While the areas look extremely divergent, we propose a common denominator in the form of a possible molecular mechanism of action of the molecule in all these diverse situations.

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“…strain fd2-tb, which can produce streptothricins (STs), was isolated from a soil sample collected in Shanghai, China. STs can inhibit protein synthesis in prokaryotic cells and show antibacterial, antifungal and antiviral bioactivities ( 1 , 2 ). STs are used to treat bacterial and fungal diseases in agriculture ( 3 ).…”

Section: Genome Announcementmentioning

confidence: 99%

Draft Genome Sequence of the Streptothricin-Producing Strain Streptomyces sp. fd2-tb

Tang

Cen

et al. 2015

Genome Announc

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Biological activities of racemomycin-B, .BETA.-lysine rich streptothricin antibiotic, the main component of Streptomyces lavendulae OP-2.

Cited by 6 publications

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Enantiomeric Free Radicals and Enzymatic Control of Stereochemistry in a Radical Mechanism: The Case of Lysine 2,3-Aminomutases

Enantiomeric Free Radicals and Enzymatic Control of Stereochemistry in a Radical Mechanism: The Case of Lysine 2,3-Aminomutases

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Draft Genome Sequence of the Streptothricin-Producing Strain Streptomyces sp. fd2-tb

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