The growing VAO flavoprotein family

Leferink, Nicole G. H.; Heuts, Dominic P. H. M.; Fraaije, Marco W.; Berkel, Willem J.H. van

doi:10.1016/j.abb.2008.01.027

Cited by 114 publications

(98 citation statements)

References 74 publications

(61 reference statements)

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“…AAO activity in B. adusta (Romero et al 2010), whose sequence corresponds to BJEAD_171002 from the JGI genome, has been characterized largely showing higher activity on p-hydroxy and chlorinated benzyl alcohols than Pleurotus AAO (Romero et al 2009). p-Hydroxybenzyl alcohols are the typical substrates of vanillyl alcohol oxidase, a flavoenzyme from a different superfamily (Leferink et al 2008), but they are not efficiently oxidized by Pleurotus AAO, whose best substrates are p-methoxylated benzyl alcohols (Guillén et al 1992, Ferreira et al 2005. Therefore the best characterized Polyporales AAO shows catalytic properties intermediate between Agaricales AAO and vanillylalcohol oxidase.…”

Section: Discussionmentioning

confidence: 99%

A survey of genes encoding H2O2-producing GMC oxidoreductases in 10 Polyporales genomes

Ferreira¹,

Carro²,

Serrano³

et al. 2015

Mycologia

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The genomes of three representative Polyporales (Bjerkandera adusta, Phlebia brevispora and a member of the Ganoderma lucidum complex) recently were sequenced to expand our knowledge on the diversity and distribution of genes involved in degradation of plant polymers in this Basidiomycota order, which includes most wood-rotting fungi. Oxidases, including members of the glucose-methanol-choline (GMC) oxidoreductase superfamily, play a central role in the above degradative process because they generate extracellular H 2 O 2 acting as the ultimate oxidizer in both white-rot and brown-rot decay. The survey was completed by analyzing the GMC genes in the available genomes of seven more species to cover the four Polyporales clades. First, an in silico search for sequences encoding members of the aryl-alcohol oxidase, glucose oxidase, methanol oxidase, pyranose oxidase, cellobiose dehydrogenase and pyranose dehydrogenase families was performed. The curated sequences were subjected to an analysis of their evolutionary relationships, followed by estimation of gene duplication/ reduction history during fungal evolution. Second, the molecular structures of the near one hundred GMC oxidoreductases identified were modeled to gain insight into their structural variation and expected catalytic properties. In contrast to ligninolytic peroxidases, whose genes are present in all white-rot Polyporales genomes and absent from those of brown-rot species, the H 2 O 2 -generating oxidases are widely distributed in both fungal types. This indicates that the GMC oxidases provide H 2 O 2 for both ligninolytic peroxidase activity (in white-rot decay) and Fenton attack on cellulose (in brown-rot decay), after the transition between both decay patterns in Polyporales occurred.

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Section: Discussionmentioning

confidence: 99%

A survey of genes encoding H2O2-producing GMC oxidoreductases in 10 Polyporales genomes

Ferreira¹,

Carro²,

Serrano³

et al. 2015

Mycologia

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“…BBLs belong to an oxidoreductase subfamily that includes BBE (Fig. 1) within a larger vanillyl-alcohol oxidase flavoprotein superfamily (Leferink et al, 2008). The three-dimensional x-ray crystal structures of BBE, glucooligosaccharide oxidase, 6-hydroxy-D-nicotine oxidase, and aclacinomycin oxidoreductase showed that the flavoproteins of the BBE subfamily comprise two domains: a conserved FAD-binding domain and an a/b-domain with a seven-stranded, antiparallel b-sheet forming the less-conserved substrate-binding domain.…”

Section: Discussionmentioning

confidence: 99%

Vacuole-Localized Berberine Bridge Enzyme-Like Proteins Are Required for a Late Step of Nicotine Biosynthesis in Tobacco1

et al. 2011

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Tobacco (Nicotiana tabacum) plants synthesize nicotine and related pyridine-type alkaloids, such as anatabine, in their roots and accumulate them in their aerial parts as chemical defenses against herbivores. Herbivory-induced jasmonate signaling activates structural genes for nicotine biosynthesis and transport by way of the NICOTINE (NIC) regulatory loci. The biosynthesis of tobacco alkaloids involves the condensation of an unidentified nicotinic acid-derived metabolite with the N-methylpyrrolinium cation or with itself, but the exact enzymatic reactions and enzymes involved remain unclear. Here, we report that jasmonate-inducible tobacco genes encoding flavin-containing oxidases of the berberine bridge enzyme family (BBLs) are expressed in the roots and regulated by the NIC loci. When expression of the BBL genes was suppressed in tobacco hairy roots or in tobacco plants, nicotine production was highly reduced, with a gradual accumulation of a novel nicotine metabolite, dihydromethanicotine. In the jasmonate-elicited cultured tobacco cells, suppression of BBL expression efficiently inhibited the formation of anatabine and other pyridine alkaloids. Subcellular fractionation and localization of green fluorescent protein-tagged BBLs showed that BBLs are localized in the vacuoles. These results indicate that BBLs are involved in a late oxidation step subsequent to the pyridine ring condensation reaction in the biosynthesis of tobacco alkaloids.

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“…Reoxidation of the reduced flavin coenzyme can take place via several processes, including the reaction with oxygen, as in the case of flavin oxidases. The flavin cofactors (generally, flavin mononucleotide [FMN] or flavin adenine dinucleotide [FAD]) often are tightly bound to these enzymes, and in selected examples, the coenzyme is covalently attached to the protein (11). Sequence comparisons of YgaF reveal this 422-amino-acid E. coli protein to be homologous to human mitochondrial L-2-hydroxyglutarate dehydrogenase (41% identity over 398 residues) (28), Helicobacter pylori malate:quinone oxidoreductase (24% identity over 421 residues) (33), Bacillus sp.…”

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confidence: 99%

Identification ofEscherichia coliYgaF as anl-2-Hydroxyglutarate Oxidase

Kalliri¹,

Mulrooney²,

Hausinger

2008

J Bacteriol

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YgaF, a protein of previously unknown function in Escherichia coli, was shown to possess noncovalently bound flavin adenine dinucleotide and to exhibit L-2-hydroxyglutarate oxidase activity. The inability of anaerobic, reduced enzyme to reverse the reaction by reducing the product ␣-ketoglutaric acid is explained by the very high reduction potential (؉19 mV) of the bound cofactor. The likely role of this enzyme in the cell is to recover ␣-ketoglutarate mistakenly reduced by other enzymes or formed during growth on propionate. On the basis of the identified function, we propose that this gene be renamed lhgO.The ygaF gene of Escherichia coli is located immediately downstream of csiD, which encodes a crystallographically characterized protein of unknown function (4), and just upstream of the gabDTP operon and csiR, which encode succinic semialdehyde dehydrogenase, ␥-aminobutyric acid (GABA) transaminase, a GABA-specific permease, and a repressor (Fig. 1). The first five genes, and perhaps all six (30), are coregulated by CsiR repression and cyclic AMP-cyclic AMP receptor protein and s induction acting at csiD p during carbon starvation and at stationary phase (14,18). Expression of gabDTP is additionally controlled by s binding to gabD p1 , which is triggered by multiple-stress induction (18), and by Nac/ 70 interaction with gabD p2 in response to nitrogen starvation (30). YgaF is not obviously involved in GABA metabolism (30), and its role is unknown.On the basis of its amino acid sequence, YgaF is likely to be a flavoenzyme. It has been estimated that 1 to 3% of the identified proteins in prokaryotic and eukaryotic cells contain flavin (5) and these abundant enzymes catalyze a wide range of reactions with a diverse set of substrates, including alcohols, aldehydes, ketones, amines, dithiols, amino acids, and hydroxy acids (34). Most of these enzymes transition between the fully oxidized and two-electron reduced forms of their cofactor, but in some cases, the one-electron reduced semiquinone species is stabilized. Reoxidation of the reduced flavin coenzyme can take place via several processes, including the reaction with oxygen, as in the case of flavin oxidases. The flavin cofactors (generally, flavin mononucleotide [FMN] or flavin adenine dinucleotide [FAD]) often are tightly bound to these enzymes, and in selected examples, the coenzyme is covalently attached to the protein (11). Sequence comparisons of YgaF reveal this 422-amino-acid E. coli protein to be homologous to human mitochondrial L-2-hydroxyglutarate dehydrogenase (41% identity over 398 residues) (28), Helicobacter pylori malate:quinone oxidoreductase (24% identity over 421 residues) (33), Bacillus sp. strain B-0618 creatinase and sarcosine oxidase (23% identity over 255 residues) (32), human mitochondrial dimethylglycine dehydrogenase (24% identity over 227 residues) (2), Bacillus subtilis glycine oxidase (25% identity over 146 residues) (9), human peroxisomal L-pipecolic acid oxidase (21% identity over 219 residues) (6), and many other flavoenzymes...

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The growing VAO flavoprotein family

Cited by 114 publications

References 74 publications

A survey of genes encoding H2O2-producing GMC oxidoreductases in 10 Polyporales genomes

A survey of genes encoding H2O2-producing GMC oxidoreductases in 10 Polyporales genomes

Vacuole-Localized Berberine Bridge Enzyme-Like Proteins Are Required for a Late Step of Nicotine Biosynthesis in Tobacco1

Identification ofEscherichia coliYgaF as anl-2-Hydroxyglutarate Oxidase

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