• Proceedings of the Korean Biophysical Society Conference
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• 1996.07a
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• pp.45-45
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• 1996

Flavin-peptides were purified from pyranose oxidase (EC 1.1.3.10) after tryptic- chymotryptic and tryptic digestion. The spectral and chromatographic properties of these flavin peptides showed that the FAD of pyranose oxidase appears to be bound, by way of the 8${\alpha}$-methylene group, to the N-l position of the imidazole ring of the histidine. Automated sequence analysis showed that the amino acid sequence of the tryptic-chymotryptic flavin-peptide from pyranose oxidase is Ser-Thr-X-Trp and that of the tryptic flavin-peptide is Met-Ser-Thr-X-Trp. (omitted)

• The Korean Journal of Zoology
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• v.38 no.4
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• pp.498-504
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• 1995

The effeds of riboflavin defidency on the biosynthesis of flavin pepddes and levels of flavoenzymes and catecholamines have been investigated. The percentage of 14C. riboflavin radioactivity formed in mitochondria appeared to increase up to 2 weeks but started to decline at 3 weeks. A significant increase of radioactivity incorporation into mitochondria and into trypsin-digestable plus trypsin-non-digestibie flavin peptides was detected in riboflavin-deficient animals. More than 35% of incorporation was observed at the end of the first week and 160% higher incorporation was observed in fiavin peptide after the second week. Activities of MAO and succinate dehydrogenase were affected markedly by riboflavin status whereas those of acetyichoilnesterase were not affected. Riboflavin defidency also brought about marked reductions in levels of epineplrrine and norepinephrine. it is concluded that the levels of flavin peptides, MAO and succinate dehydrogenase, and catecholamines were affected significanily by the availability of riboflavin and in particular the duration of its depiction.

• Journal of Microbiology and Biotechnology
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• v.26 no.9
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• pp.1636-1642
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• 2016

Phenalamide is a bioactive secondary metabolite produced by Myxococcus stipitatus. We identified a 56 kb phenalamide biosynthetic gene cluster from M. stipitatus DSM 14675 by genomic sequence analysis and mutational analysis. The cluster is comprised of 12 genes (MYSTI_04318- MYSTI_04329) encoding three pyruvate dehydrogenase subunits, eight polyketide synthase modules, a non-ribosomal peptide synthase module, a hypothetical protein, and a putative flavin adenine dinucleotide-binding protein. Disruption of the MYSTI_04324 or MYSTI_04325 genes by plasmid insertion resulted in a defect in phenalamide production. The organization of the phenalamide biosynthetic modules encoded by the fifth to tenth genes (MYSTI_04320-MYSTI_04325) was very similar to that of the myxalamid biosynthetic gene cluster from Stigmatella aurantiaca Sg a15, as expected from similar backbone structures of the two substances. However, the loading module and the first extension module of the phenalamide synthase encoded by the first to fourth genes (MYSTI_04326-MYSTI_04329) were found only in the phenalamide biosynthetic gene cluster from M. stipitatus DSM 14675.