Substrate specificity of Streptomyces transglutaminases

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.

The zig‐zag‐zig in oomycete–plant interactions

“…, 1994). TGases are multifunctional enzymes vital for many physiological processes, such as cell differentiation and tissue regeneration (Langston et al. , 2007).…”

“…One of the first proteinaceous oomycete PAMPs to be identified is an abundant, calcium-dependent transglutaminase (TGase) named GP42 that functions in the cell wall of P. sojae Nürnberger et al, 1994). TGases are multifunctional enzymes vital for many physiological processes, such as cell differentiation and tissue regeneration (Langston et al, 2007). The acyl transferase activity of the enzyme performs various in vivo and in vitro protein cross-linking and modification functions .…”

Cloning of a Transglutaminase Gene from an Indonesian Streptomyces Strain

“…TGases of microbial origin (MTGases) have recently received increasing attention for industrial applications. The properties of MTGases offer more adv antages compared t o animal-deri v ed transglutaminases, such as no requirement of cofactor Ca 2+ for their activity, their stability across wide pH range, their ability to cross-link most food proteins, and lower production costs due to easy enzyme production and purification (Langston et al, 2006). Theref ore, TG ase production based on microorganisms is worthy to be pursued.…”

Production of transglutaminase byStreptomycesisolates in solid-state fermentation

“…Streptomyces species may produce high biodiversity of TGase differing from each other in structure (sequence) and mode of cross‐linking of most important food, agricultural and textile proteins (Cui et al. 2006; Langston et al. 2007; Bech et al.…”

“…Streptomyces species may produce high biodiversity of TGase differing from each other in structure (sequence) and mode of cross-linking of most important food, agricultural and textile proteins (Cui et al 2006;Langston et al 2007;Bech et al 2000;Motoki et al 1994;Lin et al 2003). By using SSF process, inexpensive crude (in situ) TGase may be produced, without downstream (purification) processes.…”