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CC bond formation using ThDP-dependent lyases.

Michael Müller¹, Georg A Sprenger, Martina Pohl

¹Institute of Pharmaceutical Sciences, Albert-Ludwigs-Universität Freiburg, Albertstr. 25, 79104 Freiburg, Germany. michael.mueller@pharmazie.uni-freiburg.de

Current Opinion in Chemical Biology

|March 26, 2013

Summary

This summary is machine-generated.

Recent advances in enzymatic thiamine catalysis reveal new reactions and engineered variants of established enzymes like pyruvate decarboxylase (PDC). Novel thiamine diphosphate (ThDP)-dependent enzymes, including MenD, PigD, and YerE, expand catalytic capabilities for aldehydes and ketones.

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Area of Science:

Biochemistry
Enzymology
Organic Synthesis

Background:

Thiamine diphosphate (ThDP) is a crucial cofactor for various metabolic enzymes.
Established ThDP-dependent enzymes like BAL, PDC, and TK have well-defined catalytic roles.
Recent research has focused on expanding the scope and efficiency of ThDP-catalyzed reactions.

Purpose of the Study:

To review recent advancements in enzymatic thiamine catalysis over the past three years.
To highlight novel reactions and engineered variants of known ThDP-dependent enzymes.
To introduce newly discovered ThDP-dependent enzymes and their unique catalytic activities.

Main Methods:

Literature review of recent publications in enzymatic thiamine catalysis.
Analysis of enzyme engineering strategies for ThDP-dependent enzymes.
Characterization of novel ThDP-dependent enzymes and their reaction mechanisms.

Main Results:

Identification of new reactions catalyzed by established enzymes like BAL, PDC, and TK.
Engineering of enzyme variants to access stereoisomeric products.
Discovery and characterization of new ThDP-dependent enzymes: MenD, PigD (Stetter-like addition), and YerE (ketone acceptor).

Conclusions:

Enzymatic thiamine catalysis continues to evolve with new reactions and engineered enzymes.
Novel ThDP-dependent enzymes expand the toolkit for biocatalysis, particularly for aldehyde and ketone transformations.
Future research holds promise for further expanding the scope of ThDP-dependent biocatalysis.