Convergent Evolution of Fungal Cysteine Dioxygenases

Flückger, Sebastian; Igareta, Nico V.; Seebeck, Florian P.

doi:10.1002/cbic.202000317

Cited by 8 publications

(6 citation statements)

References 67 publications

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“…We were intrigued about a potential connection between ergothioneine biosynthesis and thiol dioxygenation, because a number of ergothioneine biosynthetic sulfoxide synthases (EgtB homologs) catalyze cysteine dioxygenation as a significant side activity [5,17] . In certain fungi (agaricomycetes) the production of cysteine dioxide is dependent on the concomitant production of ergothioneine, adding evidence that the two compounds may participate in the same response to external signals [18] …”

Section: Resultsmentioning

confidence: 99%

“…However, as the following analysis revealed, the primary product of ETDO is ergothioneine sulfinic acid (5) This stability allowed us to determine the origin of the two oxygen atoms of 5. We found that ETDO-catalyzed oxidation of ergothioneine in a reaction containing > 90 % heavy water (H 2 18 O) produced no detectable heavy isotopolog of 5 ([C 9 H 14 N 3 O 3 18 OS] À m/z calc. : 262.0752, Figure S15), suggesting that both oxygen atoms that are attached during oxidation derive from O 2 (Scheme 2C).…”

Section: Angewandte Chemiementioning

confidence: 99%

“…[5,17] In certain fungi (agaricomycetes) the production of cysteine dioxide is dependent on the concomitant production of ergothioneine, adding evidence that the two compounds may participate in the same response to external signals. [18] To examine the in vitro activity of these actinobacterial TDO-like enzymes we produced representative homologs from Nocardioides sp.…”

Section: Identification Of Etdomentioning

confidence: 99%

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Enzyme‐Catalyzed Oxidative Degradation of Ergothioneine

Nalivaiko,

Vasseur,

Seebeck

2024

Angew Chem Int Ed

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Ergothioneine is a sulfur‐containing metabolite that is produced by bacteria and fungi, and is absorbed by plants and animals as a micronutrient. Ergothioneine reacts with harmful oxidants including singlet oxygen or hydrogen peroxide, and may therefore protect cells against oxidative stress. In this report we describe two enzymes from actinobacteria that cooperate in the specific oxidative degradation of ergothioneine. The first enzyme is an iron‐dependent thiol dioxygenase that produces ergothioneine sulfinic acid. A crystal structure of ergothioneine dioxygenase from Thermocatellispora tengchongensis reveals many similarities with cysteine dioxygenases, suggesting that the two enzymes share a common mechanism. The second enzyme is a metal‐dependent ergothioneine sulfinic acid desulfinase that produces Na‐trimethylhistidine and SO2. The discovery that certain actinobacteria contain the enzymatic machinery for O2‐dependent biosynthesis and O2‐dependent degradation of ergothioneine indicates that these organisms may actively manage their ergothioneine content

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Section: Resultsmentioning

confidence: 99%

Section: Angewandte Chemiementioning

confidence: 99%

Section: Identification Of Etdomentioning

confidence: 99%

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Enzyme‐Catalyzed Oxidative Degradation of Ergothioneine

Nalivaiko,

Vasseur,

Seebeck

2024

Angew Chem Int Ed

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“…Other mechanisms such as mechanical destruction by fungi may also be included in keratin degradation (Korniłłowicz-Kowalska and Bohacz, 2011 ). As the disulfide bonds link polypeptides to form fibrous structures, breaking the disulfide bonds may be the first step in microbial degradation (Kasperova et al, 2013 ; Lange et al, 2016 ; Mercer and Stewart, 2018 ; Flückger et al, 2020 ). This step can be catalyzed by the produced inorganic sulfite and disulfide reductase (Korniłłowicz-Kowalska and Bohacz, 2011 ).…”

Section: Microbial Degradation Of Keratinmentioning

confidence: 99%

Perspectives on Converting Keratin-Containing Wastes Into Biofertilizers for Sustainable Agriculture

2022

Front. Microbiol.

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Keratin-containing wastes become pollution to the environment if they are not treated properly. On the other hand, these wastes can be converted into value-added products applicable to many fields. Organic fertilizers and biofertilizers are important for sustainable agriculture by providing nutrients to enhance the growth speed of the plant and production. Keratin-containing wastes, therefore, will be an important resource to produce organic fertilizers. Many microorganisms exhibit capabilities to degrade keratins making them attractive to convert keratin-containing wastes into valuable products. In this review, the progress in microbial degradation of keratins is summarized. In addition, perspectives in converting keratin into bio- and organic fertilizers for agriculture are described. With proper treatment, feather wastes which are rich in keratin can be converted into high-value fertilizers to serve as nutrients for plants, reduce environmental pressure and improve the quality of the soil for sustainable agriculture.

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“…Some disulfide reductases involved in keratin degradation were shown ( Kasperova et al, 2013 ; Navone and Speight, 2018 ; Table 1 ). The roles of these enzymes in keratin degradation have been described in other literatures, which will not be described here ( Kasperova et al, 2013 ; Lange et al, 2016 ; Mercer and Stewart, 2018 ; Flückger et al, 2020 ).…”

Section: Mechanism Of Action For Keratinasementioning

confidence: 99%

Structure, Application, and Biochemistry of Microbial Keratinases

2021

Front. Microbiol.

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Keratinases belong to a class of proteases that are able to degrade keratins into amino acids. Microbial keratinases play important roles in turning keratin-containing wastes into value-added products by participating in the degradation of keratin. Keratin is found in human and animal hard tissues, and its complicated structures make it resistant to degradation by common proteases. Although breaking disulfide bonds are involved in keratin degradation, keratinase is responsible for the cleavage of peptides, making it attractive in pharmaceutical and feather industries. Keratinase can serve as an important tool to convert keratin-rich wastes such as feathers from poultry industry into diverse products applicable to many fields. Despite of some progress made in isolating keratinase-producing microorganisms, structural studies of keratinases, and biochemical characterization of these enzymes, effort is still required to expand the biotechnological application of keratinase in diverse fields by identifying more keratinases, understanding the mechanism of action and constructing more active enzymes through molecular biology and protein engineering. Herein, this review covers structures, applications, biochemistry of microbial keratinases, and strategies to improve its efficiency in keratin degradation.

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Convergent Evolution of Fungal Cysteine Dioxygenases

Cited by 8 publications

References 67 publications

Enzyme‐Catalyzed Oxidative Degradation of Ergothioneine

Enzyme‐Catalyzed Oxidative Degradation of Ergothioneine

Perspectives on Converting Keratin-Containing Wastes Into Biofertilizers for Sustainable Agriculture

Structure, Application, and Biochemistry of Microbial Keratinases

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