Related Experiment Video
Updated: Oct 3, 2026

Purification of Mitochondria from Yeast Cells
Published on: August 24, 2009
[Purification and several properties of dihydroxyacetone kinase from the methylotrophic yeast Candida boidinii]
Abstract:
A procedure for isolation of a homogeneous dihydroxyacetone kinase including fractionation by polyethylene glycol and ion-exchange chromatography on polyethylenimine-Biogel has been developed. The enzyme is a dimer with Mr = 139 000 (2.71 000 according to SDS disc electrophoresis) and has a pI of 4.64 and pH optimum of 7.8-8.2. The enzyme phosphorylates dihydroxyacetone and, in a lesser degree, glyceraldehyde. ATP is the most efficient phosphate group donor for the enzyme. When ITP, GTP, CTP and UTP are used, the dihydroxyacetone kinase activity is about 30%.
Related Concept Videos
Preparation of Diols and Pinacol Rearrangement
The reaction begins with transferring a proton from the acid catalyst to one of the hydroxyl groups, producing an oxonium ion.
Fates of Pyruvate
In aerobic organisms, pyruvate is metabolized via the citric acid cycle to produce reduced coenzymes NADH and FADH2. These coenzymes are then oxidized in the electron transport chain to produce ATP and, in the process, regenerate the NAD+ and FAD. As seen in some cell types and organisms, fermentation...
α-Hydroxy Ketones via Reductive Coupling of Esters: Acyloin Condensation Overview
Alkylation of β-Ketoester Enolates: Acetoacetic Ester Synthesis
Microbial Fermentation
Production of Alcohol

