title: 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.
authors.affiliation: Novozymes, Inc., 1445 Drew Avenue, Davis, CA 95616, USA.
authors.forename: James
authors.initials: J
authors.lastname: Langston
authors.forename: Alexander
authors.initials: A
authors.lastname: Blinkovsky
authors.forename: Tony
authors.initials: T
authors.lastname: Byun
authors.forename: Michael
authors.initials: M
authors.lastname: Terribilini
authors.forename: Darron
authors.initials: D
authors.lastname: Ransbarger
authors.forename: Feng
authors.initials: F
authors.lastname: Xu
mesh_terms: D000595:Amino Acid Sequence; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D010838:Phytophthora / Q000201:enzymology; D017386:Sequence Homology, Amino Acid; D013306:Streptomycetaceae / Q000201:enzymology* / Q000235:genetics; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D013696:Temperature; D011503:Transglutaminases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D011503:Transglutaminases