Related Experiment Video
Updated: Jul 13, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
Substrate specificity of streptomyces transglutaminases
James Langston1, Alexander Blinkovsky, Tony Byun
1Novozymes, Inc., 1445 Drew Avenue, Davis, CA 95616, USA.
Transglutaminase (TGase) enzymes from Streptomyces species were purified and characterized. Their properties suggest potential as industrial biocatalysts for protein modification and crosslinking applications.
Area of Science:
- Biochemistry
- Enzymology
- Microbiology
Background:
- Transglutaminase (TGase) is a crucial enzyme involved in cell differentiation, tissue regeneration, and pathogenicity.
- Its acyl transfer function facilitates protein crosslinking and modification, vital for biological processes and industrial applications.
Purpose of the Study:
- To investigate the structure-function relationship of TGase from various Streptomyces species and Phytophthora cactorum.
- To evaluate the potential of these TGases as industrial biocatalysts.
Main Methods:
- Purification of TGase from S. lydicus, S. platensis, S. nigrescens, S. cinnamoneus, and S. hachijoensis.
- Determination of pH and temperature profiles for S. lydicus, S. platensis, and S. nigrescens TGases.
- Characterization of S. lydicus TGase specificity towards amine substrates.
Main Results:
- TGases were successfully purified from multiple Streptomyces species.
- Optimal pH and temperature conditions were identified for selected TGases.
- Substrate specificity analysis of S. lydicus TGase provided insights into its reaction mechanism, aligning with known mechanisms for Streptomyces mobaraensis TGase.
Conclusions:
- The characterized TGases exhibit properties suitable for further development as industrial biocatalysts.
- Understanding TGase specificity aids in optimizing protein crosslinking and modification processes.
More Related Videos
12:29Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility
Published on: March 11, 2022
09:47The Determination of Protease Specificity in Mouse Tissue Extracts by MALDI-TOF Mass Spectrometry: Manipulating PH to Cause Specificity Changes
Published on: May 25, 2018
Related Concept Videos
Tagging and Fusion Proteins
Allosteric Proteins-ATCase
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Ligand Binding and Linkage