Enzymatic Synthesis of Cytidine Diphosphate 3,6-Dideoxyhexoses
Year: 1969
Type: article
Abstract: Two protein fractions, designated E1 and E3, which are required for the TPNH-dependent reduction of cytidine diphosphate 4-keto-6-deoxy-d-glucose to an intermediate (presumed to be CDP-4-keto-3,6-dideoxy-d-glucose) have been partially purified from extracts of Pasteurella pseudotuberculosis 25 VO and Salmonella typhimurium LT-2. These fractions are free of thioredoxin and thioredoxin reductase. Both proteins are required, and no partial reaction has been observed under various conditions in the presence of either protein fraction alone. A mutant of S. typhimurium which cannot synthesize CDP-abequose was found to be missing E1. Some preliminary observations regarding the mechanism of the reaction are described and have been discussed.
Source: Journal of Biological Chemistry
Authors: H Pape, J L Strominger
Institution: University of Wisconsin–Madison
Language: English
Subfield: Organic Chemistry
Field: Chemistry
Domain: Physical Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W1634634725