The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana. (September 2021)
- Record Type:
- Journal Article
- Title:
- The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana. (September 2021)
- Main Title:
- The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
- Authors:
- Eggers, Reinmar
Jammer, Alexandra
Jha, Shalinee
Kerschbaumer, Bianca
Lahham, Majd
Strandback, Emilia
Toplak, Marina
Wallner, Silvia
Winkler, Andreas
Macheroux, Peter - Abstract:
- Abstract: Flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) are utilized as coenzymes in many biochemical reduction-oxidation reactions owing to the ability of the tricyclic isoalloxazine ring system to employ the oxidized, radical and reduced state. We have analyzed the genome of Arabidopsis thaliana to establish an inventory of genes encoding flavin-dependent enzymes (flavoenzymes) as a basis to explore the range of flavin-dependent biochemical reactions that occur in this model plant. Expectedly, flavoenzymes catalyze many pivotal reactions in primary catabolism, which are connected to the degradation of basic metabolites, such as fatty and amino acids as well as carbohydrates and purines. On the other hand, flavoenzymes play diverse roles in anabolic reactions most notably the biosynthesis of amino acids as well as the biosynthesis of pyrimidines and sterols. Importantly, the role of flavoenzymes goes much beyond these basic reactions and extends into pathways that are equally crucial for plant life, for example the production of natural products. In this context, we outline the participation of flavoenzymes in the biosynthesis and maintenance of cofactors, coenzymes and accessory plant pigments ( e. g. carotenoids) as well as phytohormones. Moreover, several multigene families have emerged as important components of plant immunity, for example the family of berberine bridge enzyme-like enzymes, flavin-dependent monooxygenases and NADPH oxidases.Abstract: Flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) are utilized as coenzymes in many biochemical reduction-oxidation reactions owing to the ability of the tricyclic isoalloxazine ring system to employ the oxidized, radical and reduced state. We have analyzed the genome of Arabidopsis thaliana to establish an inventory of genes encoding flavin-dependent enzymes (flavoenzymes) as a basis to explore the range of flavin-dependent biochemical reactions that occur in this model plant. Expectedly, flavoenzymes catalyze many pivotal reactions in primary catabolism, which are connected to the degradation of basic metabolites, such as fatty and amino acids as well as carbohydrates and purines. On the other hand, flavoenzymes play diverse roles in anabolic reactions most notably the biosynthesis of amino acids as well as the biosynthesis of pyrimidines and sterols. Importantly, the role of flavoenzymes goes much beyond these basic reactions and extends into pathways that are equally crucial for plant life, for example the production of natural products. In this context, we outline the participation of flavoenzymes in the biosynthesis and maintenance of cofactors, coenzymes and accessory plant pigments ( e. g. carotenoids) as well as phytohormones. Moreover, several multigene families have emerged as important components of plant immunity, for example the family of berberine bridge enzyme-like enzymes, flavin-dependent monooxygenases and NADPH oxidases. Furthermore, the versatility of flavoenzymes is highlighted by their role in reactions leading to tRNA-modifications, chromatin regulation and cellular redox homeostasis. The favorable photochemical properties of the flavin chromophore are exploited by photoreceptors to govern crucial processes of plant adaptation and development. Finally, a sequence- and structure-based approach was undertaken to gain insight into the catalytic role of uncharacterized flavoenzymes indicating their involvement in unknown biochemical reactions and pathways in A. thaliana . Graphical abstract: Image 1 Highlights: 262 genes encode flavoproteins accounting for 0.93% of the protein coding regions. The genome harbors a remarkable number of multigene families of flavoenzymes. Flavoenzymes are crucial for plant-specific reactions in secondary metabolism. Flavoproteins play central roles in processes regulated by blue light. As many as 37 putative flavoenzymes are involved in unknown reactions. … (more)
- Is Part Of:
- Phytochemistry. Volume 189(2021)
- Journal:
- Phytochemistry
- Issue:
- Volume 189(2021)
- Issue Display:
- Volume 189, Issue 2021 (2021)
- Year:
- 2021
- Volume:
- 189
- Issue:
- 2021
- Issue Sort Value:
- 2021-0189-2021-0000
- Page Start:
- Page End:
- Publication Date:
- 2021-09
- Subjects:
- Anabolism -- Catabolism -- Cofactors -- Defense -- Detoxification -- Photoreceptor -- Phytohormones -- Reactive oxygen species -- Redox homeostasis
2-PG 2-phosphoglycolate -- 4-OH-ICN 4-hydroxyindole-3-carbonyl nitrile -- AAO abscisic aldehyde oxidase -- ABA abscisic acid -- ACAD acyl-CoA dehydrogenase -- ACX acyl-CoA oxidase -- AHAS acetohydroxy acid synthase -- AIR12 AUXIN INDUCED IN ROOT CULTURE 12 -- AOX alternative oxidase -- A. thaliana Arabidopsis thaliana -- ATR NADPH-dependent cytochrome reductase -- BBE berberine bridge enzyme -- B. cinerea Botrytis cinerea -- CCE/CCT C-terminal extension/cryptochrome C-terminus -- CD cellodextrin -- CELLOX cellodextrin oxidase -- CKX cytokinin dehydrogenase -- CoQ ubiquinone -- COQ6 hydroxylase in ubiquinone biosynthesis -- CPD cyclobutene pyrimidine dimer -- CPR NADPH-cytochrome P450 reductase -- CREG cellular repressor of E1A stimulated genes -- CRTISO carotene cis-trans isomerase -- cry cryptochrome -- CS chorismate synthase -- DAAO D-amino acid oxidase -- DAMP damage-associated molecular patterns -- DASH Drosophila-Arabidopsis-Synechocystis-Human -- DHBPS 3, 4-dihydroxy-2-butanone-4-phosphate synthase -- D2HGDH D-2-hydroxyglutarate dehydrogenase -- DHODH dihydroorotate dehydrogenase -- DHPDH dihydropyrimidine dehydrogenase -- DLDH D-lactate dehydrogenase -- DUS tRNA-dihydrouridine synthase -- DWF1 Dwarf1 -- EPSP 5-enolpyruvylshikimate 3-phosphate synthase -- ERO endoplasmic reticulum oxidoreductin -- Erv essential for respiration and viability -- E. coli Escherichia coli -- mETC electron transport chain -- ETF electron transferring flavoprotein -- ETF-QO ETF-quinone oxidoreductase -- ETFDH ETF dehydrogenase -- FAD flavin adenine dinucleotide -- FADS FAD-synthetase -- FCLY farnesylcysteine lyase -- Fd ferredoxin -- FKF kelch repeat F-box -- FLC flowering locus C -- FMN flavin mononucleotide -- FMO flavin-containing monooxygenase -- FNR ferredoxin-dependent reductase -- FPMO flavoprotein monooxygenass -- FQR1 flavodoxin-like quinone reductase -- FRO metallo reductase -- GidA glucose inhibited division family A (protein)/MnmG -- tRNA uridine modifying enzyme -- GSH/GSSG reduced/oxidized glutathione -- GALDH L-galactono-1, 4-lactone dehydrogenase -- GltS NADH-dependent glutamate synthase -- GLU ferredoxin-dependent glutamate synthase -- GMC oxidoreductase glucose-methanol-choline oxidoreductase -- GOOX glucooligosaccharide oxidase -- GOX glycolate oxidase -- GPDH glycerol-3-phosphate dehydrogenase -- GR glutathione reductase -- GTP guanine triphosphate -- GULO L-gulono-1, 4-lactone dehydrogenase (homolog) -- h human -- HAOX 2-hydroxy acid oxidase -- HCAR 7-hydroxymethyl chlorophyll a reductase -- HNL hydroxynitrile lyase -- HTH hothead -- IAA indole-3-acetic acid -- IBA indole butyric acid -- IBR IBA-response -- IDI isopentenyl diphosphate isomerase -- IPA indole pyruvic acid -- IVD isovaleryl-CoA dehydrogenase -- JA jasmonic acid -- LASPO L-aspartate oxidase -- L2HGDH L-2-hydroxyglutarate dehydrogenase -- LKP LOV kelch protein -- LOV light-oxygen-voltage domain -- LipPD lipoamide dehydrogenase -- LSD lysine-specific histone demethylase -- MAMP microbe-associated molecular pattern -- Moco molybdopterin cofactor -- MDHA(R) monodehydroascorbate (reductase) -- MnmE GTP- and folate binding subunit of the tRNA-uridine modifying enzyme complex -- MORF multiple organellar RNA editing factor -- MTHF 5, 10-methylentetrahydrofolate -- MTHFR methylenetetrahydrofolate reductase -- NDA1, NDA2, NDB1, NDB3 and NDB4 NAD(P)H dehydrogenases of the alternative pathway -- NDC1 demethylphylloquinone reductase -- NHP N-hydroxypipecolic acid -- NO nitric oxide -- NOX NADPH oxidase -- NQO1 NAD(P)H:quinone oxidoreductase 1 -- NQR NAD(P)H:quinone oxidoreductase -- NR nitrate reductase -- OG oligogalacturonides -- OGOX oligogalacturonide oxidase -- OPDA 12-oxophytodienoic acid -- OPR 12-oxophytodienoic acid reductase -- OYE old yellow enzyme -- PAO polyamine oxidase -- P5C pyrroline-5-carboxylate -- P6C Δ1-piperideine-6-carboxylate -- PDI protein disulfide isomerase -- PDS phytoene dehydrogenase -- PHOT phototropin -- PHR photolyase homology region -- Pip pipecolic acid -- ProDH proline dehydrogenase -- PLP PAS-LOV protein -- PNPO pyridoxamine/pyridoxine 5′-phosphate oxidase -- P5P pyridoxal 5′-phosphate -- PPCDC 4′-phosphopantothenoylcysteine decarboxylase -- PPO protoporphyrinogen IX oxidase -- PYD1 pyrimidine dehydrogenase -- QSOX quiescin sulfhydryl oxidase -- RBOH respiratory burst oxidase homolog -- RFK riboflavin kinase -- ROS reactive oxygen species -- Ru5P ribulose 5-phosphate -- SA salicylic acid -- SAH S-adenosylhomocysteine -- SAM S-adenosylmethionine -- SAR systemic acquired resistance -- S. cerevisiae Saccharomyces cerevisiae -- SDH succinate dehydrogenase -- SOX sarcosine oxidase -- SQLE squalene monooxygenase (epoxidase) -- SWIRM domain was found in the proteins SWI3, Rsc8 and Moira -- TPP thiamine pyrophosphate -- TrmE A. thaliana homolog of bacterial MnmE -- Trx thioredoxin -- TrxR thioredoxin reductase -- UDP uridine diphosphate -- VAO vanillyl alcohol oxidase -- WrbA tryptophan (W) repressor-binding protein -- XDH xanthine dehydrogenase -- YUCCA flavin-dependent monooxygenase involved in auxin biosynthesis -- ZEP zeaxanthine epoxidase -- ZTL ZEITLUPE
Botanical chemistry -- Periodicals
Biochemistry -- Periodicals
Botany -- Periodicals
Chimie végétale -- Périodiques
572.2 - Journal URLs:
- http://www.sciencedirect.com/science/journal/00319422 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.phytochem.2021.112822 ↗
- Languages:
- English
- ISSNs:
- 0031-9422
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6489.800000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 17535.xml