Part A: Enzyme Engineering and Biotechnology

Applied Biochemistry and Biotechnology

, Volume 136, Issue 3, pp 291-308

Substrate specificity of Streptomyces transglutaminases

  • James LangstonAffiliated withNovozymes, Inc.
  • , Alexander BlinkovskyAffiliated withNovozymes, Inc.
  • , Tony ByunAffiliated withNovozymes, Inc.
  • , Michael TerribiliniAffiliated withNovozymes, Inc.
  • , Darron RansbargerAffiliated withNovozymes, Inc.
  • , Feng XuAffiliated withNovozymes, Inc. Email author 

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Transglutaminase (TGase) is a multifunctional enzyme vital for many physiologic processes, such as cell differentiation, tissue regeneration, and plant pathogenicity. The acyl transfer function of the enzyme can activate primary amines and, consequently, attach them onto a peptidyl glutamine, a reaction important for various in vivo and in vitro protein crosslinking and modification processes. To understand better the structure-function relationship of the enzyme and to develop it further as an industrial biocatalyst, we studied TGase secreted by several Streptomyces species and Phytophthora cactorum. We purified the enzyme from S. lydicus, S. platensis, S. nigrescens, S. cinnamoneus, and S. hachijoensis. The pH and temperature profiles of S. lydicus, S. platensis, and S. nigrescens TGases were determined. The specificity of S. lydicus TGase toward its acyl-accepting amine substrates was characterized. Correlation of the electronic and steric features of the substrates with their reactivity supported the mechanism previously proposed for Streptomyces mobaraensis TGase.

Index Entries

Transglutaminase specificity Streptomyces Phytophthora cactorum acyl-accepting amines