Flavogenomics

• Verfasst von: Macheroux, Peter [VerfasserIn]
• Verfasst von: Kappes, Barbara [VerfasserIn]
• Verfasst von: 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
• DOI: doi:10.1111/j.1742-4658.2011.08202.x
• Datenträger: Online-Ressource
• Sprache: eng
• Sach-SW: enzymes
• Sach-SW: flavin adenine dinucleotide (FAD)
• Sach-SW: flavin mononucleotide (FMN)
• Sach-SW: genomic distribution
• Sach-SW: oxidoreductases
• Sach-SW: redundancy
• Sach-SW: structures
• K10plus-PPN: 1823203523

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.