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- Title
Substrate Specificity of Streptomyces Transglutaminases.
- Authors
James Langston; Alexander Blinkovsky; Tony Byun; Michael Terribilini; Darron Ransbarger; Feng Xu
- Abstract
Transglutaminase (TGase) is a multifunctional enzyme vital for manyphysiologic processes, such as cell differentiation, tissue regeneration, andplant pathogenicity. The acyl transfer function of the enzyme can activateprimary amines and, consequently, attach them onto a peptidyl glutamine,a reaction important for various in vivo and in vitro protein crosslinking andmodification processes. To understand better the structure-function relationshipof the enzyme and to develop it further as an industrial biocatalyst,we studied TGase secreted by several Streptomyces species and Phytophthoracactorum. 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 ofS. lydicus TGase toward its acyl-accepting amine substrates was characterized.Correlation of the electronic and steric features of the substrateswith their reactivity supported the mechanism previously proposed for Streptomycesmobaraensis TGase.
- Subjects
TRANSGLUTAMINASES; ORGANIC compounds; CELL differentiation; AMINO acids
- Publication
Applied Biochemistry & Biotechnology, 2007, Vol 136, Issue 3, p291
- ISSN
0273-2289
- Publication type
Article
- DOI
10.1007/s12010-007-9027-5