Flavogenomics: a genomic and structural view of flavin-dependent proteins
Riboflavin (vitamin B2) serves as the precursor for FMN and FAD in almost all organisms that utilize the redox-active isoalloxazine ring system as a coenzyme in enzymatic reactions. The role of flavin, however, is not limited to redox processes, as ∼ 10% of flavin-dependent enzymes catalyze nonredox...
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| Hauptverfasser: | , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
2011
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| In: |
The FEBS journal
Year: 2011, Jahrgang: 278, Heft: 15, Pages: 2625-2634 |
| ISSN: | 1742-4658 |
| DOI: | 10.1111/j.1742-4658.2011.08202.x |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1111/j.1742-4658.2011.08202.x Verlag, lizenzpflichtig, Volltext: https://onlinelibrary.wiley.com/doi/abs/10.1111/j.1742-4658.2011.08202.x 
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| Verfasserangaben: | Peter Macheroux, Barbara Kappes and Steven E. Ealick |
MARC
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| 245 | 1 | 0 | |a Flavogenomics |b a genomic and structural view of flavin-dependent proteins |c Peter Macheroux, Barbara Kappes and Steven E. Ealick |
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| 520 | |a Riboflavin (vitamin B2) serves as the precursor for FMN and FAD in almost all organisms that utilize the redox-active isoalloxazine ring system as a coenzyme in enzymatic reactions. The role of flavin, however, is not limited to redox processes, as ∼ 10% of flavin-dependent enzymes catalyze nonredox reactions. Moreover, the flavin cofactor is also widely used as a signaling and sensing molecule in biological processes such as phototropism and nitrogen fixation. Here, we present a study of 374 flavin-dependent proteins analyzed with regard to their function, structure and distribution among 22 archaeal, eubacterial, protozoan and eukaryotic genomes. More than 90% of flavin-dependent enzymes are oxidoreductases, and the remaining enzymes are classified as transferases (4.3%), lyases (2.9%), isomerases (1.4%) and ligases (0.4%). The majority of enzymes utilize FAD (75%) rather than FMN (25%), and bind the cofactor noncovalently (90%). High-resolution structures are available for about half of the flavoproteins. FAD-containing proteins predominantly bind the cofactor in a Rossmann fold (∼ 50%), whereas FMN-containing proteins preferably adopt a (βα)8-(TIM)-barrel-like or flavodoxin-like fold. The number of genes encoding flavin-dependent proteins varies greatly in the genomes analyzed, and covers a range from ∼ 0.1% to 3.5% of the predicted genes. It appears that some species depend heavily on flavin-dependent oxidoreductases for degradation or biosynthesis, whereas others have minimized their flavoprotein arsenal. An understanding of ‘flavin-intensive’ lifestyles, such as in the human pathogen Mycobacterium tuberculosis, may result in valuable new intervention strategies that target either riboflavin biosynthesis or uptake. | ||
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| 650 | 4 | |a flavin adenine dinucleotide (FAD) | |
| 650 | 4 | |a flavin mononucleotide (FMN) | |
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| 700 | 1 | |a Ealick, Steven E. |e VerfasserIn |0 (DE-588)1273407431 |0 (DE-627)1823203442 |4 aut | |
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