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Biochemistry & Molecular Biology

Molecular insights into the mechanism of substrate recognition of Streptomyces transglutaminases

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Pages 575-582 | Received 23 Oct 2019, Accepted 21 Nov 2019, Published online: 25 Nov 2019

References

  • Serafini-Fracassini D, Del Duca S. Transglutaminases: widespread cross-linking enzymes in plants. Ann Bot. 2008;102(2):145–152.
  • Aeschlimann D, Paulsson M. Transglutaminases: protein cross-linking enzymes in tissues and body fluids. Thromb Haemost. 1994;71(4):402–415.
  • Severina E, Nunez L, Baker S, et al. Factor XIIIa mediated attachment of S. aureus fibronectin-binding protein A (FnbA) to fibrin: identification of Gln103 as a major cross-linking site. Biochemistry. 2006;45(6):1870–1880.
  • Ando H, Adachi M, Umeda K, et al. Purification and characteristics of a novel transglutaminase derived from microorganisms. Agric Biol Chem. 1989;53:2613–2617.
  • Kieliszek M, Misiewicz A. Microbial transglutaminase and its application in the food industry. Rev Folia Microbiol (Praha). 2014;59(3):241–250.
  • Taghi Gharibzahedi SM, Koubaa M, Barba FJ, et al. Recent advances in the application of microbial transglutaminase crosslinking in cheese and ice cream products: A review. Int J Biol Macromol. 2018;107(Pt B):2364–2374.
  • Temiz H, Dağyıldız K. Effects of microbial transglutaminase on physicochemical, microbial and sensorial properties of kefir produced by using mixture cow’s and soymilk. Korean J Food Sci Anim Resour. 2017;37(4):606–616.
  • Li Q, Gui P, Huang Z, et al. Effect of transglutaminase on quality and gel properties of pork and fish mince mixtures. J Texture Stud. 2018;49(1):56–64.
  • Hu Y, Shao Y, Wu C, et al. γ-PGA and MTGase improve the formation of ε-(γ-glutamyl) lysine cross-links within hairtail (Trichiurus haumela) surimi protein. Food Chem. 2018;242:330–337.
  • Heil A, Ohsam J, van Genugten B, et al. Microbial transglutaminase used in bread preparation at standard bakery concentrations does not increase immunodetectable amounts of deamidated gliadin. J Agric Food Chem. 2017;65(32):6982–6990.
  • Lauber S, Henle T, Klostermeyer H. Relationship between the crosslinking of caseins by transglutaminase and the gel strength of yoghurt. Eur Food Res Technol. 2000;210(5):305–309.
  • Ozera B, Kirmacia HA, Oztekinb S, et al. Incorporation of microbial transglutaminase into non-fat yogurt production. Int Dairy J. 2007;17(3):199–207.
  • Marino M, Casale R, Borghini R, et al. The effects of modified versus unmodified wheat gluten administration in patients with celiac disease. Int Immunopharmacol. 2017;47:1–8.
  • C K M, Hertel TC, Pietzsch M. Random mutagenesis of a recombinant microbial transglutaminase for the generation of thermostable and heat-sensitive variants. J Biotechnol. 2008;136(3–4):156–162.
  • Melino G, Piacentini M. Tissue’ transglutaminase in cell death: a downstream or a multifunctional upstream effector? FEBS Lett. 1998;430(1–2):59–63.
  • Casadio R, Polverini E, Mariani P, et al. The structural basis for the regulation of tissue transglutaminase by calcium ions. Eur J Biochem. 1999;262(3):672–679.
  • Ohtsuka T, Ota M, Nio N, et al. Comparison of substrate specificities of transglutaminases using synthetic peptides as acyl donors. Biosci Biotechnol Biochem. 2000;64(12):2608–2613.
  • Langston J, Blinkovsky A, Byun T, et al. Substrate specificity of Streptomyces transglutaminases. Appl Biochem Biotechnol. 2007;136(3):291–308.
  • Taguchi S, Nishihama KI, Igi K, et al. Substrate specificity analysis of microbial transglutaminase using proteinaceous protease inhibitors as natural model substrates. J Biochem. 2000;128(3):415–425.
  • Hopwood DA, Bibb MJ, Chater KF, et al. Genetic manipulation of Streptomyces: a laboratory manual. Norwich: The John Inns Foundation; 1985. p. 70–84.
  • Wan K, Uraji M, Tokai S, et al. Enzymatic degradation of allergen peptides from bovine casein by a combination of Streptomyces aminopeptidases. Appl Biochem Biotechnol. 2018;187(2):570–582.
  • Gundersen MT, Keillor JW, Pelletier JN. Microbial transglutaminase displays broad acyl-acceptor substrate specificity. Appl Microbiol Biotechnol. 2014;98(1):219–230.
  • Zhu Y, Rinzema A, Tramper J, et al. Icrobial transglutaminase-a revew of its production and application in food processing. Appl Microbiol Biotechnol. 1995;44:277–282.
  • Taguchi S, Arakawa K, Yokoyama K, et al. Overexpression and purification of microbial pro-transglutaminase from Streptomyces cinnamoneum and in vitro processing by Streptomyces albogriseolus proteases. J Biosci Bioeng. 2002;94(5):478–481.
  • Tagami U, Shimba N, Nakamura M, et al. Substrate specificity of microbaial transglutaminase as revealed by three-dimensional docking simulation and mutagenesis. Protein Eng Des Select. 2009;22:747–752.

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