Substrate specificity of Streptomyces transglutaminases

• Published in: Applied biochemistry and biotechnology 2007-03, Vol.136 (3), p.291-308
• Main Authors: Langston, J, Blinkovsky, A, Byun, T, Terribilini, M, Ransbarger, D, Xu, F
• Format: Article
• Language: English
• Subjects: Amines; Amino Acid Sequence; bacterial proteins; Biological and medical sciences; Biotechnology; catalysts; Cell differentiation; enzyme activity; enzyme substrates; Enzymes; Flowers & plants; Fundamental and applied biological sciences. Psychology; fungal proteins; Hydrogen-Ion Concentration; Molecular Sequence Data; Pathogens; Phytophthora - enzymology; Phytophthora cactorum; protein-glutamine gamma-glutamyltransferase; purification; Sequence Homology, Amino Acid; Streptomyces; Streptomyces cinnamoneus; Streptomyces hachijoensis; Streptomyces lydicus; Streptomyces nigrescens; Streptomyces platensis; Streptomycetaceae - enzymology; Streptomycetaceae - genetics; Structure-Activity Relationship; structure-activity relationships; Studies; Substrate Specificity; Temperature; Transglutaminases - chemistry; Transglutaminases - isolation & purification; Transglutaminases - metabolism; Yeast
• ISSN: 0273-2289; 1559-0291
• DOI: 10.1007/s12010-007-9027-5

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.