Formation of 4-ribitylamino-5-amino-2,6-dihydroxypyrimidine in an adenine-riboflavin doubleless mutant of Bacillus subtilis.

Mitsuda, Hisateru; Nakajima, Kenji; Yamada, Yukiko

doi:10.3177/jnsv.23.161

Cited by 7 publications

(3 citation statements)

References 10 publications

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“…In most cases the terminal catabolites in pteridine degradation are simple pteridines and lumazines (29)(30)(31). Though lumazines are usually formed by catabolic pathways, at least one, namely 6,7-dimethyl-8-ribityllumazine, is involved in anabolic metabolism, riboflavin biosynthesis, in the organisms Ashbya gossypii, Eremothecium ashbyii, mutants of Bacillus subtilis, and others (7,(32)(33)(34)(35).…”

Section: Resultsmentioning

confidence: 99%

Separation and structure of the prosthetic group of the blue fluorescence protein from the bioluminescent bacterium Photobacterium phosphoreum

Koka

Lee²

1979

Proc. Natl. Acad. Sci. U.S.A.

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ABSTRACr The highly fluorescent prosthetic group of the blue fluorescence protein purified from the bioluminescent bacterium Photobacterium phosphoreum has been dissociated and separated from its apoprotein by affinity chromatography on Cibacron Blue-Sepharose. It has been identified as 6,7-dimethyl-8(1'-D-ribityl)lumazine by several methods of characterization, all of which gave results identical to those for an authentic sample. In neutral solution, absorption maxima are at 407, 275 (shoulder), and 256 nm, with a single fluorescence maximum at 491 nm. The proton magnetic resonance spectrum exhibits a singlet at 2.66 ppm corresponding to the methyl substituted at the 6 position of lumazine and a multiplet centered at 3.85 ppm corresponding to the C-2'-5' protons of the ribityl group. A Raman spectrum was obtained by the technique of coherent anti-Stokes Raman scattering and the RF values by paper chromatography were determined in four solvent systems. The isolated compound was readily transformed into riboflavin by riboflavin synthetase. Fifty grams (dry weight) of P. phosphoreum contains at least 20 mg of this lumazine derivative, an amount comparable to that found in other microorganisms classified as riboflavin overproducers. The overproduction of this lumazine in this case apparently has to do with its function in the generation of bioluminescence.A blue fluorescence protein was isolated from extracts of the bioluminescent bacterium Photobacterium phosphoreum by Gast and Lee (1); the protein was shown to meet the requirements of the in vivo bioluminescence emitter by three significant observations: (i) its fluorescence emission is identical to the bioluminescence spectrum both in position of the maximum, 476 nm, and in spectral distribution; (ii) the in vitro bioluminescence reaction of reduced flavin mononucleotide, luciferase, oxygen, and long-chain aliphatic aldehyde is stimulated by the addition of this protein both in terms of the decay rate of light emission and the total light yield; and (iii) the in vitro bioluminescence spectrum is shifted to match that of the in vivo when this protein is included in the in vitro reaction (1). The blue fluorescence protein is associated with luciferase and has a molecular weight of 22,000 (1). The protein-bound prosthetic group is highly fluorescent, with a quantum yield of 0.45 (1). Alteration of solution conditions perturbs this fluorescence to match either the in vitro or the in vivo bioluminescence of P. phosphoreum (1).The blue fluorescence protein was further purified by affinity chromatography on a Cibacron Blue-Sepharose column, which removed all traces of flavin and other fluorescent impurities (2, 3). The purified protein showed absorption maxima at 412 and 274 nm with a single absorption band in the visible region (3).The finding of a blue fluorescence protein also in another species of bioluminescent bacterium, Photobacterium fischeri (4), suggests that the fluorophore functions in some way in the bioluminescence and therefore its chemical structure sho...

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Section: Resultsmentioning

confidence: 99%

Separation and structure of the prosthetic group of the blue fluorescence protein from the bioluminescent bacterium Photobacterium phosphoreum

Koka

Lee²

1979

Proc. Natl. Acad. Sci. U.S.A.

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“…91 We previously reported that guanosine triphosphate (1-3) is the most direct nucleotide precursor and is converted to riboflavin via 4-(1'-D-ribitylamino)-5 -amino-2, 6-dihydroxypyrimidine (4,5). In addition, we demonstrated the clear identity of structures (6) and functions (7) in differentiating between the pyrimidine intermediate and the byproduct formed in the riboflavin synthetase reaction.…”

Section: Discussionmentioning

confidence: 92%

Effects of various metabolites (sugars, carboxylic acids and alcohols) on riboflavin formation in non-growing cells of Ashbya gossypii.

Mitsuda

Nakajima

Ikeda

1978

Journal of Nutritional Science and Vitaminology, J Nutr Sci Vit

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“…The authors isolated a possible intermediate using glyoxal from a high flavinogenic mold, Eremothecium ashbyii (7) and an adenine-riboflavin doubleless mutant of Bacillus subtilis (8). The intermediate was proved to be 4-ribitylamino-5-amino-2, 6-di hydroxypyrimidine after crystallization through high purification by means of various column chromatographic analyses.…”

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confidence: 99%

Studies on the intermediates in the biosynthetic pathway of riboflavin. I. Identification of a green fluorescent compound, compound G1, accumulated in non-growing cells of Eremothecium ashbyii by the addition of dimeric diacetyl.

Mitsuda

Nakajima

Yamada

1977

Journal of Nutritional Science and Vitaminology, J Nutr Sci Vit

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Formation of 4-ribitylamino-5-amino-2,6-dihydroxypyrimidine in an adenine-riboflavin doubleless mutant of Bacillus subtilis.

Cited by 7 publications

References 10 publications

Separation and structure of the prosthetic group of the blue fluorescence protein from the bioluminescent bacterium Photobacterium phosphoreum

Separation and structure of the prosthetic group of the blue fluorescence protein from the bioluminescent bacterium Photobacterium phosphoreum

Effects of various metabolites (sugars, carboxylic acids and alcohols) on riboflavin formation in non-growing cells of Ashbya gossypii.

Studies on the intermediates in the biosynthetic pathway of riboflavin. I. Identification of a green fluorescent compound, compound G1, accumulated in non-growing cells of Eremothecium ashbyii by the addition of dimeric diacetyl.

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