A Structural View on the Maturation of Lanthipeptides.

Area of Science:

• Biochemistry
• Molecular Biology
• Microbiology

Background:

• Lanthipeptides are ribosomally synthesized peptides with diverse bioactivities.
• Key features include thioether bonds forming (methyl-)lanthionine rings.
• These modifications are essential for their biological functions.

Purpose of the Study:

• To summarize recent insights into lanthipeptide modification mechanisms.
• To focus on the structures and mechanisms of the enzymes involved in dehydration and cyclization.
• To highlight the importance of these steps in lanthipeptide classification.

Main Methods:

• Review of recent literature on lanthipeptide biosynthesis.
• Focus on enzymatic mechanisms of dehydration and cyclization.
• Analysis of enzyme structures and their roles.

Main Results:

• Lanthipeptide modification involves a two-step process: dehydration of Ser/Thr residues and subsequent cyclization.
• Enzymes catalyze these steps via Michael-type addition of dehydrated residues to Cys residues.
• Enzyme classification is linked to the genes encoding them and the modification steps.

Conclusions:

• The dehydration and cyclization steps are fundamental to lanthipeptide diversity and classification.
• Understanding these enzymatic mechanisms provides insights into lanthipeptide bioactivity.
• Recent research has advanced our knowledge of the enzymes and their structural basis.