Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.22.32 (bromelain)
 1,025 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Transglutaminase from Streptomyces mobaraensis is an enzyme of unknown function that cross-links proteins to high molecular weight aggregates. Previously, we characterized two intrinsic transglutaminase substrates with inactivating activities against subtilisin and dispase. This report now describes a novel substrate that inhibits papain, bromelain, and trypsin. Papain was the most sensitive protease; thus, the protein was designated Streptomyces papain inhibitor (SPI). To avoid transglutaminase-mediated glutamine deamidation during culture, SPI was produced by Streptomyces mobaraensis at various growth temperatures. The best results were achieved by culturing for 30-50 h at 42 degrees C, which yielded high SPI concentrations and negligibly small amounts of mature transglutaminase. Transglutaminasespecific biotinylation displayed largely unmodified glutamine and lysine residues. In contrast, purified SPI from the 28 degrees C culture lost the potential to be cross-linked, but exhibited higher inhibitory activity as indicated by a significantly lower Ki (60 nM vs. 140 nM). Despite similarities in molecular mass (12 kDa) and high thermostability, SPI exhibits clear differences in comparison with all members of the wellknown family of Streptomyces subtilisin inhibitors. The neutral protein (pI of 7.3) shares sequence homology with a putative protein from Streptomyces lavendulae, whose conformation is most likely stabilized by two disulfide bridges. However, cysteine residues are not localized in the typical regions of subtilisin inhibitors. SPI and the formerly characterized dispase-inactivating substrate are unique proteins of distinct Streptomycetes such as Streptomyces mobaraensis. Along with the subtilisin inhibitory protein, they could play a crucial role in the defense of vulnerable protein layers that are solidified by transglutaminase.
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PMID:A novel transglutaminase substrate from Streptomyces mobaraensis inhibiting papain-like cysteine proteases. 2171 69

A classification of gluten polymer networks would support a better understanding of structure-function relationships of any gluten polymer material and thus, the control of processing properties. However, quantification and interpretation of the gluten network structures is challenging due to their complexity. Thus, the network formation was altered by specific gluten-modifying agents (glutathione, ascorbic acid, potassium bromate, glucose oxidase, transglutaminase, bromelain) in this study in order to clarify if structural alterations can be detected on a microstructural level and to specify different polymer arrangements in general. Microstructure analysis was performed by confocal laser scanning microscopy followed by quantification with protein network analysis. It was shown that alterations in gluten microstructure could be elucidated according to the kind of modification in cross-linking (disulphide, (iso) peptide, dityrosyl). Linear correlations of structural network attributes among each other were found, leading to an assertion in general: the higher the branching rate, the thinner the protein threads and the larger the interconnected protein aggregate. Considering the morphological attribute lacunarity, a quantitative classification of different gluten arrangements was established. These assertions were extended by using unspecific gluten-modifying agents in addition to the specific ones. Ultimately, five network types were proposed based on diverse polymer arrangements.
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PMID:Gluten Polymer Networks-A Microstructural Classification in Complex Systems. 3096 51