| Online-Ressource |
Verfasst von: | Macheroux, Peter [VerfasserIn]  |
| Kappes, Barbara [VerfasserIn]  |
| Ealick, Steven E. [VerfasserIn]  |
Titel: | Flavogenomics |
Titelzusatz: | a genomic and structural view of flavin-dependent proteins |
Verf.angabe: | Peter Macheroux, Barbara Kappes and Steven E. Ealick |
Jahr: | 2011 |
Umfang: | 10 S. |
Fussnoten: | Gesehen am 22.11.2022 |
Titel Quelle: | Enthalten in: Vereinigung der Europäischen Biochemischen GesellschaftenThe FEBS journal |
Ort Quelle: | Oxford [u.a.] : Wiley-Blackwell, 2005 |
Jahr Quelle: | 2011 |
Band/Heft Quelle: | 278(2011), 15, Seite 2625-2634 |
ISSN Quelle: | 1742-4658 |
Abstract: | 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. |
DOI: | doi:10.1111/j.1742-4658.2011.08202.x |
URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext ; Verlag: https://doi.org/10.1111/j.1742-4658.2011.08202.x |
| Volltext: https://onlinelibrary.wiley.com/doi/abs/10.1111/j.1742-4658.2011.08202.x |
| DOI: https://doi.org/10.1111/j.1742-4658.2011.08202.x |
Datenträger: | Online-Ressource |
Sprache: | eng |
Sach-SW: | enzymes |
| flavin adenine dinucleotide (FAD) |
| flavin mononucleotide (FMN) |
| genomic distribution |
| oxidoreductases |
| redundancy |
| structures |
K10plus-PPN: | 1823203523 |
Verknüpfungen: | → Zeitschrift |