Alcohol oxidase: A complex peroxisomal, oligomeric flavoprotein

Ozimek, Paulina; Veenhuis, Marten; Klei, Ida J. van der

doi:10.1016/j.femsyr.2005.06.005

Cited by 95 publications

(75 citation statements)

References 97 publications

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“…Methanol oxidase.-MOX is mostly known as a peroxysomal enzyme in methylotrophic ascomycetous yeasts, such as Pichia pastoris or C. boidinii (Ozimek et al 2005). The first basidiomycete MOX was purified and characterized from P. chrysosporium (Nishida and Eriksson 1987) and it is also known from Phlebiopsis gigantea (Danneel et al 1994).…”

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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“…Riboswitches are the nontranslated mRNAs that bind effectors (low-molecular-weight metabolites) using selective binding domains (otherwise called ligand-binding pockets or aptamers) without a requirement for any proteins. Regulation of gene 338 ABBAS AND SIBIRNY MICROBIOL. MOL.…”

Section: Transcriptional Regulation In Bacteria Using the Riboswitch mentioning

confidence: 99%

Genetic Control of Biosynthesis and Transport of Riboflavin and Flavin Nucleotides and Construction of Robust Biotechnological Producers

Abbas

Sibirny

2011

Microbiol Mol Biol Rev

325

272

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SUMMARY Riboflavin [7,8-dimethyl-10-(1′- d -ribityl)isoalloxazine, vitamin B 2 ] is an obligatory component of human and animal diets, as it serves as the precursor of flavin coenzymes, flavin mononucleotide, and flavin adenine dinucleotide, which are involved in oxidative metabolism and other processes. Commercially produced riboflavin is used in agriculture, medicine, and the food industry. Riboflavin synthesis starts from GTP and ribulose-5-phosphate and proceeds through pyrimidine and pteridine intermediates. Flavin nucleotides are synthesized in two consecutive reactions from riboflavin. Some microorganisms and all animal cells are capable of riboflavin uptake, whereas many microorganisms have distinct systems for riboflavin excretion to the medium. Regulation of riboflavin synthesis in bacteria occurs by repression at the transcriptional level by flavin mononucleotide, which binds to nascent noncoding mRNA and blocks further transcription (named the riboswitch). In flavinogenic molds, riboflavin overproduction starts at the stationary phase and is accompanied by derepression of enzymes involved in riboflavin synthesis, sporulation, and mycelial lysis. In flavinogenic yeasts, transcriptional repression of riboflavin synthesis is exerted by iron ions and not by flavins. The putative transcription factor encoded by SEF1 is somehow involved in this regulation. Most commercial riboflavin is currently produced or was produced earlier by microbial synthesis using special selected strains of Bacillus subtilis , Ashbya gossypii , and Candida famata . Whereas earlier RF overproducers were isolated by classical selection, current producers of riboflavin and flavin nucleotides have been developed using modern approaches of metabolic engineering that involve overexpression of structural and regulatory genes of the RF biosynthetic pathway as well as genes involved in the overproduction of the purine precursor of riboflavin, GTP.

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“…The characteristics of those AODs and the regulation of the gene encoding AODs have been studied in detail (Couderc and Baratti, 1980;Kato et al, 1976;Ozimek et al, 2005;Tani et al, 1972Tani et al, , 1985. In the production of AODs by filamentous fungi, Ko et al have recently reported that Thermoascus aurantiacus NBRC 31963 inductively produced two AODs by incubation with the pectin medium, and characteristics of both enzymes have been revealed by his group (Ko et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

Characterization of alcohol oxidase from Aspergillus ochraceus AIU 031

Isobe

Kato

Ogawa

et al. 2007

J. Gen. Appl. Microbiol.

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An alcohol oxidase (AOD) was found from Aspergillus ochraceus AIU 031, and its characteristics were revealed. This enzyme oxidized short-chain primary alcohols and ethylene glycol, and belonged to the same group as AOD from methylotrophic yeast. However, it differed in the following properties. The K m value for ethanol was larger and that for ethylene glycol was smaller than those of AODs derived from methylotrophic yeasts. The ethanol oxidation was optimal at pH 5-7 and 50-55°C. The molecular mass of this enzyme was 262 kDa and consisted of four identical subunits of 68 kDa, which were much smaller than those of methylotrophic yeasts.

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Alcohol oxidase: A complex peroxisomal, oligomeric flavoprotein

Cited by 95 publications

References 97 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

Genetic Control of Biosynthesis and Transport of Riboflavin and Flavin Nucleotides and Construction of Robust Biotechnological Producers

Characterization of alcohol oxidase from Aspergillus ochraceus AIU 031

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