Applied Biochemistry and Biotechnology

, Volume 136, Issue 3, pp 291–308

Substrate specificity of Streptomyces transglutaminases

  • James Langston
  • Alexander Blinkovsky
  • Tony Byun
  • Michael Terribilini
  • Darron Ransbarger
  • Feng Xu
Part A: Enzyme Engineering and Biotechnology

DOI: 10.1007/s12010-007-9027-5

Cite this article as:
Langston, J., Blinkovsky, A., Byun, T. et al. Appl Biochem Biotechnol (2007) 136: 291. doi:10.1007/s12010-007-9027-5

Abstract

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 

Copyright information

© Humana Press Inc 2007

Authors and Affiliations

  • James Langston
    • 1
  • Alexander Blinkovsky
    • 1
  • Tony Byun
    • 1
  • Michael Terribilini
    • 1
  • Darron Ransbarger
    • 1
  • Feng Xu
    • 1
  1. 1.Novozymes, Inc.Davis

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