Natural transaminase fusions for biocatalysis

Area of Science:

• Biocatalysis
• Enzyme Engineering
• Synthetic Biology

Background:

• Biocatalytic methods are crucial for synthesizing amines from readily available precursors.
• Novel enzymes and enzyme combinations are rapidly advancing the production of complex compounds.
• Natural multifunctional enzymes facilitate multi-step biosynthetic pathways, enhancing reaction rates and stability.

Purpose of the Study:

• To identify and analyze a natural transaminase fusion enzyme, PP_2782, from *Pseudomonas putida* KT2440.
• To investigate three thermophilic homologs of this transaminase fusion.
• To evaluate the substrate scope and potential industrial applications of these enzymes.

Main Methods:

• Identification and sequence analysis of transaminase fusion enzymes.
• Biochemical characterization of enzyme activity with various aldehydes, amines, and keto acids.
• Structural similarity analysis to identify fused domains.

Main Results:

• The natural transaminase fusion PP_2782 and its homologs were identified and analyzed.
• Both fusion enzymes and their truncated derivatives demonstrated broad activity with aliphatic/aromatic aldehydes and amines, and α-keto acids.
• The fused domain was identified as an acyl-[acyl-carrier-protein] reductase involved in reductive chain release.

Conclusions:

• Natural transaminase fusions, like PP_2782, exhibit significant biocatalytic potential.
• These enzymes are effective for amine synthesis from diverse substrates.
• The findings suggest promising industrial applications for these novel biocatalysts.