Cell‐free synthesis of 6‐hydroxy‐D‐nicotine oxidase containing covalently bound FAD

Hamm, Hans‐Heinrich; Decker, Karl

doi:10.1016/0014-5793(78)80571-7

FEBS Letters

1978

DOI: 10.1016/0014-5793(78)80571-7

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Cell‐free synthesis of 6‐hydroxy‐D‐nicotine oxidase containing covalently bound FAD

Hans‐Heinrich Hamm

Karl Decker

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1978

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Cited by 6 publications

References 8 publications

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Regulation of flavoprotein synthesis studied in vivo in a riboflavin-requiring mutant of Arthrobacter oxidans

Hamm

Decker

1978

Arch. Microbiol.

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The biosynthesis of two flavoproteins, 6-hydroxy-D-nicotine oxidase with covalently bound FAD and 6-hydroxy-L-nicotine oxidase containing non-covalently bound FAD, was studied in wild-type cells and in a riboflavin-requiring mutant of Arthrobacter oxidans. In the mutant cells, the rate of synthesis and the maximal activity level of both enzymes after induction by nicotine depended on the amount of added riboflavin. The low rate of synthesis in the presence of 2 micron riboflavin could be enhanced during the induction phase by further addition of riboflavin (33 micron). Inhibitors of translation (chloramphenicol or streptomycin) completely blocked the synthesis of both flavoproteins. Inhibitors of transcription (rifamycin S or actinomycin D) stopped the synthesis of both enantiozymes in wild-type cells and in the mutant grown in the presence of a saturating supply of riboflavin (15 micron). Under conditions of restricted flavoprotein synthesis (2 micron riboflavin in the medium), however, the mutant cells continued to synthesize the enzyme for 2--3 h after the addition of the transcription inhibitors. It appears, that in these cells a rather stable m-RNA accumulated during riboflavin-limited flavoprotein synthesis. The dependence of the effect of transcription inhibitors on the extracellular supply of riboflavin suggests that the regulation of the synthesis of both flavoproteins occurs not only by control of gene expression (induction by nicotine), but also at the level of translation through the availability of FAD.

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Regulation of flavoprotein synthesis studied in vivo in a riboflavin-requiring mutant of Arthrobacter oxidans

Hamm

Decker

1978

Arch. Microbiol.

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?-gulonolactone oxidase activity and vitamin C status in riboflavin-deficient rats

Kiuchi

Nishikimi²,

Yagi

1980

Biochimica et Biophysica Acta (BBA) - General Subjects

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Cell-free synthesis of the phenoxazinone synthetase subunit by polyribosomes from Streptomyces antibioticus.

Jones¹

1980

Journal of Biological Chemistry

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Cell‐free synthesis of 6‐hydroxy‐D‐nicotine oxidase containing covalently bound FAD

Cited by 6 publications

References 8 publications

Regulation of flavoprotein synthesis studied in vivo in a riboflavin-requiring mutant of Arthrobacter oxidans

Regulation of flavoprotein synthesis studied in vivo in a riboflavin-requiring mutant of Arthrobacter oxidans

?-gulonolactone oxidase activity and vitamin C status in riboflavin-deficient rats

Cell-free synthesis of the phenoxazinone synthetase subunit by polyribosomes from Streptomyces antibioticus.

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