Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.24.11 (CD10)
 9,792 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Proteolytic enzymes (EC 3.4) secreted by Trichoderma strains are receiving increasing attention because of their potential implication in the Trichoderma biocontrol abilities. We have used an expressed sequence tag (EST) approach to identify genes encoding extracellular peptidases in T. harzianum CECT 2413 grown under several biocontrol-related conditions. Based on BlastX results and Gene Ontology annotation, a total of 61 (among 3478) unique sequences (unisequences) were predicted to encode enzymes with peptidase activity, three corresponding to secreted peptidases already known from this Trichoderma strain (PAPA, PRA1 and P6281). Further manual screening based on the functional identity and cellular location of the best matches revealed ten unisequences encoding novel extracellular peptidases. We report the characterization of the corresponding genes as well as a potential orthologous gene of the intracellular peptidase PAPB from T. asperellum. In each case, full-length coding sequences were obtained, and deduced proteins were compared at phylogenetic level with peptidases from other organisms. T. harzianum CECT 2413 novel peptidases included six serine endopeptidases (EC 3.4.21) belonging to the families S1, S8 and S53, three aspartic endopeptidases (EC 3.4.23) of the family A1, one metallo-endopeptidase (EC 3.4.24) of the family M35, and one aminopeptidase (EC 3.4.11) of the family M28. Results obtained by Northern blot analyses demonstrated that the genes within a family are differentially regulated in response to different culture conditions, suggesting that they have diverse functional roles.
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PMID:Characterization of genes encoding novel peptidases in the biocontrol fungus Trichoderma harzianum CECT 2413 using the TrichoEST functional genomics approach. 1741 67

Many socially important fungi encode an elevated number of subtilisin-like serine proteases, which have been shown to be involved in fungal mutualisms with grasses and in parasitism of insects, nematodes, plants, other fungi, and mammalian skin. These proteins have endopeptidase activities and constitute a significant part of fungal secretomes. Here, we use comparative genomics to investigate the relationship between the quality and quantity of serine proteases and the ability of fungi to cause disease in invertebrate and vertebrate animals. Our screen of previously unexamined fungi allowed us to annotate and identify nearly 1000 subtilisin-containing proteins and to describe six new categories of serine proteases. Architectures of predicted proteases reveal novel combinations of subtilisin domains with other, co-occurring domains. Phylogenetic analysis of the most common clade of fungal proteases, proteinase K, showed that gene family size changed independently in fungi, pathogenic to invertebrates (Hypocreales) and vertebrates (Onygenales). Interestingly, simultaneous expansions in the S8 and S53 families of subtilases in a single fungal species are rare. Our analysis finds that closely related systemic human pathogens may not show the same gene family expansions, and that related pathogens and nonpathogens may show the same type of gene family expansion. Therefore, the number of proteases does not appear to relate to pathogenicity. Instead, we hypothesize that the number of fungal serine proteases in a species is related to the use of the animal as a food source, whether it is dead or alive.
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PMID:Independent subtilases expansions in fungi associated with animals. 2172 38