Related Experiment Video
Updated: Aug 3, 2026

Nucleoside Triphosphates - From Synthesis to Biochemical Characterization
Published on: April 3, 2014
Studies on thiamine diphosphate-dependent enzymes
F J Leeper1, D Hawksley, S Mann
1University Chemical Laboratory, Lensfield Road, Cambridge CB2 1EW, UK. fjl1@cam.ac.uk
Abstract:
The 3-deaza analogue of TPP (thiamine diphosphate), a close mimic of the ylid intermediate, has been synthesized and is an extremely potent inhibitor of a variety of TPP-dependent enzymes, binding much more tightly than TPP itself. Results using deazaTPP complexed with the E1 subunit of PDH (pyruvate dehydrogenase) have led to a novel proposal about the mechanism of this enzyme. The 2-substituted forms of deazaTPP, which mimic other intermediates in the catalytic mechanism, can also be synthesized and 2-(1-hydroxyethyl)deazaTPP is also an extremely potent inhibitor of PDC (pyruvate decarboxylase). Attachment of such 2-substituents is expected to be a way to introduce selectivity in the inhibition of various TPP-dependent enzymes.
Related Concept Videos
Enzyme Kinetics
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
Riboswitches
The aptamer has high specificity for a particular metabolite which allows riboswitches to specifically regulate...
ATP Synthase: Mechanism
Role of Reduced Coenzymes NADH and FADH₂
Introduction to Enzyme Kinetics
The experimenter can then plot the initial reaction rate or velocity (Vo) of a given trial against the substrate concentration ([S]) to obtain a graph of the reaction properties. For many enzymatic reactions involving a...
Catalytically Perfect Enzymes

