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AgeMTPT, a Catalyst for Peptide N-Terminal Modification.

Ying Cong¹, Paul D Scesa¹, Eric W Schmidt¹

¹Department of Medicinal Chemistry, University of Utah, Salt Lake City, Utah 84112, United States.

ACS Synthetic Biology

|October 24, 2022

Summary

Synthetic biology advances peptide modification using AgeMTPT, an enzyme that protects peptide termini. Researchers elucidated its substrate scope and engineered it for broader applications in enzymatic peptide protection.

Keywords:

AgeMTPT aromatic amino acid prenylation linalyltransferase peptide modification prenyltransferase substrate selectivity

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Area of Science:

Synthetic biology
Enzymology
Protein engineering

Background:

Designed modification of peptides and proteins is a key goal in synthetic biology.
Enzymatic N- and C-terminal modification enzymes are essential tools, but options for peptide terminus protection are limited.
The prenyltransferase AgeMTPT modifies peptide termini but its substrate scope is largely unknown.

Purpose of the Study:

To investigate the substrate selectivity of the AgeMTPT prenyltransferase domain.
To demonstrate the enzyme's potential for peptide modification in synthetic biology.
To engineer AgeMTPT for an expanded substrate scope.

Main Methods:

Investigated substrate selectivity of the AgeMTPT prenyltransferase domain.
Performed enzymatic modification of leu-enkephalin.
Utilized active site mutagenesis to engineer AgeMTPT.

Main Results:

AgeMTPT requires N-terminal aromatic amino acids but tolerates diverse uncharged amino acids in other positions.
Enzymatic modification of leu-enkephalin at the N-terminus was achieved.
Mutagenesis expanded the enzyme's substrate scope, enabling reverse geranylation of peptide N-termini.

Conclusions:

The substrate selectivity of AgeMTPT has been elucidated, revealing key requirements for N-terminal modification.
Engineered AgeMTPT demonstrates expanded capabilities for enzymatic peptide modification.
These findings highlight potential applications of AgeMTPT in synthetic biology for peptide protection.