Fungal inhibitors of proteolytic enzymes: Classification, properties, possible biological roles, and perspectives for practical use

Dunaevsky, Yakov E.; Popova, Viara; Семенова, Т. А.; Белякова, Г.А.; Belozersky, M. A.

doi:10.1016/j.biochi.2013.12.007

Cited by 28 publications

(18 citation statements)

References 88 publications

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“…Many reviews on mushroom lectins and protease inhibitors have been published recently but mainly viewing their potential application in human medicine (Dunaevsky et al 2014;Erjavec et al 2012;Hassan et al 2015;Kobayashi and Kawagishi 2014;Wong et al 2010;Xu et al 2011). The present review focuses on fruiting body lectins and protease inhibitors that have been characterized at the genetic, molecular, structural, and functional levels and that exhibit toxicity to nematodes and/or insects (Table 1).…”

Section: Introductionmentioning

confidence: 99%

Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

Sabotič

Ohm

Künzler

2015

Appl Microbiol Biotechnol

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Fruiting bodies or sporocarps of dikaryotic (ascomycetous and basidiomycetous) fungi, commonly referred to as mushrooms, are often rich in entomotoxic and nematotoxic proteins that include lectins and protease inhibitors. These protein toxins are thought to act as effectors of an innate defense system of mushrooms against animal predators including fungivorous insects and nematodes. In this review, we summarize current knowledge about the structures, target molecules, and regulation of the biosynthesis of the best characterized representatives of these fungal defense proteins, including galectins, beta-trefoil-type lectins, actinoporin-type lectins, beta-propeller-type lectins and beta-trefoil-type chimerolectins, as well as mycospin and mycocypin families of protease inhibitors. We also present an overview of the phylogenetic distribution of these proteins among a selection of fungal genomes and draw some conclusions about their evolution and physiological function. Finally, we present an outlook for future research directions in this field and their potential applications in medicine and crop protection.

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Section: Introductionmentioning

confidence: 99%

Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

Sabotič

Ohm

Künzler

2015

Appl Microbiol Biotechnol

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“…However, inhibitors of cysteine peptidases show restricted distribution in fungi (Sabotiè and Kos, 2012). The caspase (C14) inhibitor I32 belongs to a group of inhibitor of apoptosis proteins (IAP) which regulate a wide range of cellular activities (Dubin, 2005;Sah et al, 2006;Dunaevsky et al, 2014). Although, the antiapoptotic activity of I32 homologs has been demonstrated in S. cerevisiae, the inhibitory effects on C14 has not been proven (Walter et al, 2006;Owsianowski et al, 2008).…”

Section: Metallopeptidases and Cysteine Proteases Are The Most Abundamentioning

confidence: 99%

“…The presence of C14 in the proteomes of all studied strains and restriction of I32 to four (mainly free living) strains may support the lack of association of the two proteins in fungi but instead, suggest a probable role in specific survival strategy in dynamic environments such as soil. Similarly, the precise function of the serine carboxypeptidase Y inhibitor (I51) remains largely obscure (Dunaevsky et al, 2014) but linked to various environmental stress responses such as heat shock and oxidative stress (Sabotiè and Kos, 2017). Unlike I32 and although, the homologs of the putative target S10 (serine carboxypeptidase) are prevalent in all the studied genomes, only 16 genomes, including those of the three sea (K. mangroviensis CBS 10435, CBS 8507 T and CBS 8886) and one plant (N. encephala UCDFST 68-887.2) isolates, harbor the specific serine carboxypeptidase Y (S10.001: MER0002010) homologs inhibited by I51.…”

Section: Metallopeptidases and Cysteine Proteases Are The Most Abundamentioning

confidence: 99%

In silico Proteomic Analysis Provides Insights Into Phylogenomics and Plant Biomass Deconstruction Potentials of the Tremelalles

Aliyu

Gorte

Zhou

et al. 2020

Front. Bioeng. Biotechnol.

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Basidiomycetes populate a wide range of ecological niches but unlike ascomycetes, their capabilities to decay plant polymers and their potential for biotechnological approaches receive less attention. Particularly, identification and isolation of CAZymes is of biotechnological relevance and has the potential to improve the cache of currently available commercial enzyme cocktails toward enhanced plant biomass utilization. The order Tremellales comprises phylogenetically diverse fungi living as human pathogens, mycoparasites, saprophytes or associated with insects. Here, we have employed comparative genomics approaches to highlight the phylogenomic relationships among thirty-five Tremellales and to identify putative enzymes of biotechnological interest encoded on their genomes. Evaluation of the predicted proteomes of the thirty-five Tremellales revealed 6,918 putative carbohydrate-active enzymes (CAZYmes) and 7,066 peptidases. Two soil isolates, Saitozyma podzolica DSM 27192 and Cryptococcus sp. JCM 24511, show higher numbers harboring an average of 317 compared to a range of 267-121 CAZYmes for the rest of the strains. Similarly, the proteomes of the two soil isolates along with two plant associated strains contain higher number of peptidases sharing an average of 234 peptidases compared to a range of 226-167 for the rest of the strains. Despite these huge differences and the apparent enrichment of these enzymes among the soil isolates, the data revealed a diversity of the various enzyme families that does not reflect specific habitat type. Growth experiment on various carbohydrates to validate the predictions provides support for this view. Overall, the data indicates that the Tremellales could serve as a rich source of both CAZYmes and peptidases with wide range of potential biotechnological relevance.

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“…63 Textile Industry: Most significant commercial application of the proteases is textile industry in which enzyme treatment gives finishing elegant texture. 64 A thermostable protease is used in removing gum and impurities present in the core protein fiber specially in silk used world widely as most precious fiber. Degumming of silk is a growing industry; it utilizes proteases in large amount and forms fine quality of silk.…”

Section: Figure 4: Enzyme Action On Proteinmentioning

confidence: 99%

Latest Overview of Proteases: A Review

Kumar¹,

Anjana²,

Poonam³

et al. 2019

AJABS

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INTRODUCTION: Enzymes are macromolecular biological catalysts that accelerate chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrate into different molecules known as product. The first enzyme to be discovered was amylase 1 in which was originally isolated from barley and catalysis the conversion of starch into sugars. Enzymes have been utilized for thousands of year in microbial processes. Microbes & their enzymes have been applied for preparations of wines, beer, cheese and other milk products. The role of enzyme in fermentation process has been known for less than two hundred years. Versatility of protein molecules present in their diverse functioning including catalytic capabilities and structural organization. Enzymes are considered biocatalyst as they are involved in producing these molecules. Both fungal and bacterial species produce these molecules. 2 Protease also known as proteinase or peptidase is an enzyme group which is involved in proteolysis. Proteolysis is the hydrolysis of peptide bonds. Peptide bonds help in formation of polypeptide chain by linking amino acids together. Proteases have industrial uses and include more than 70% of the industrial enzyme. 3 Fungi and bacteria are the major source of production of this enzyme. Proteases are eco-friendly as the sources of production are generally nonpathogenic and non-toxic. 4 Sources of Proteolytic Enzymes: Proteolytic enzymes are produced by all life forms such as plants, animals, and microorganisms.

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Fungal inhibitors of proteolytic enzymes: Classification, properties, possible biological roles, and perspectives for practical use

Cited by 28 publications

References 88 publications

Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

In silico Proteomic Analysis Provides Insights Into Phylogenomics and Plant Biomass Deconstruction Potentials of the Tremelalles

Latest Overview of Proteases: A Review

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