Coenzyme-protein interactions since early life

Area of Science:

• Origin of Life Studies
• Biochemistry
• Evolutionary Biology

Background:

• Recent findings highlight the role of peptides in early life.
• Prebiotically plausible amino acids can form structures and bind RNA.
• The functional capacity of early peptides with limited amino acids is debated.

Purpose of the Study:

• To investigate the propensity of early peptides to bind organic cofactors.
• To analyze protein-coenzyme interactions in the Protein Data Bank (PDB).

Main Methods:

• Analysis of protein-coenzyme interactions across the PDB.
• Identification of amino acid composition in cofactor binding sites.

Main Results:

• Prebiotically plausible amino acids are abundant in ancient coenzyme binding sites.
• Early cofactor binding involved protein backbone atoms and metal ions.
• Examples of modern enzymes with coenzyme binding solely by prebiotically available amino acids were found.

Conclusions:

• Peptide-cofactor interactions were plausible before the Central Dogma and full protein evolution.
• This suggests a functional collaboration between peptides and cofactors in early life.
• Supports the role of simple peptides in the origin of life.