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Photo-Induced Cross-Linking of Unmodified Proteins (PICUP) Applied to Amyloidogenic Peptides

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Identification of the epsilon-(gamma-glutamyl)lysine cross-linking sites in alpha-lactalbumin polymerized by

Deuk-Sik Lee¹, Shinya Matsumoto, Yasuki Matsumura

¹Department of Tourism and Foodservice Industry, Donghae University, Jiheungdong, Donghae-shi, Kangwondo 240-713, Korea.

Journal of Agricultural and Food Chemistry

|November 28, 2002

Summary

This study identified specific lysine residues targeted by guinea pig liver transglutaminase (GTGase) and Streptoverticillium transglutaminase (MTGase) in alpha-lactalbumin. The enzymes commonly cross-linked Gln54, with differing lysine site usage influencing polymerization.

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Site-Specific Lysine Lactylation via Genetic Code Expansion in E. coli and Mammalian Cells

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Area of Science:

Biochemistry
Enzymology
Protein Chemistry

Background:

Transglutaminases (TGases) are enzymes catalyzing cross-linking reactions.
Understanding TGase site specificity is crucial for protein modification and engineering.

Purpose of the Study:

To determine the site specificity of guinea pig liver TGase (GTGase) and Streptoverticillium TGase (MTGase) on alpha-lactalbumin.
To identify the specific lysine and glutamine residues involved in TGase-mediated cross-linking.

Main Methods:

Alpha-lactalbumin was cross-linked using GTGase and MTGase.
Peptide fragments were generated by lysylendopeptidase and V8 protease digestion.
Peptide separation via reverse-phase HPLC and sequence analysis identified cross-linked sites.

Main Results:

GTGase targeted Lys16, Lys93, and Lys122, while MTGase targeted Lys5.
Both GTGase and MTGase commonly cross-linked Gln54 to specific lysine residues.
Differences in targeted lysine residues were observed between the two TGases.

Conclusions:

The distinct lysine residue targeting by GTGase and MTGase suggests differential enzyme mechanisms.
The identified cross-linking sites provide insights into the polymerization process of alpha-lactalbumin mediated by these TGases.