Enzymatic Reduction of Alkyl and Acyl Derivatives of Dihydroxyacetone Phosphate by Reduced Pyridine Nucleotides

The reductions of either acyl or alkyl derivatives of dihydroxyacetone phosphate by enzymes from ascites tumor cell microsomes with NADPH were studied. The reaction rate was measured by determining the formation of labeled lipid from [4-3H]NADPH. The products were characterized as either 1-acyl or 1...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of biological chemistry 1972-09, Vol.247 (18), p.5825-5834
Main Authors: LaBelle, Edward F., Hajra, Amiya K.
Format: Article
Language:English
Subjects:
Acetone - metabolism
Acylation
Alkylation
Animals
Carcinoma, Ehrlich Tumor - enzymology
Chromatography, Thin Layer
Glycerophosphates - biosynthesis
Guinea Pigs
In Vitro Techniques
Lipids - biosynthesis
Mice
Microsomes - enzymology
Microsomes, Liver - enzymology
Mitochondria - enzymology
Mitochondria, Liver - enzymology
Mitochondria, Muscle - enzymology
NAD - metabolism
NADP - metabolism
Organophosphorus Compounds - metabolism
Osmolar Concentration
Oxidation-Reduction
Phospholipids - biosynthesis
Rats
Structure-Activity Relationship
Trioses - metabolism
Tritium
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The reductions of either acyl or alkyl derivatives of dihydroxyacetone phosphate by enzymes from ascites tumor cell microsomes with NADPH were studied. The reaction rate was measured by determining the formation of labeled lipid from [4-3H]NADPH. The products were characterized as either 1-acyl or 1-alkyl [2-3H]glycerol 3-phosphate formed from the corresponding keto derivatives. The enzymes were found to be distributed in both mitochondrial and microsomal fractions obtained from different organs, i.e. brain, liver, kidney, etc. When [4-3H]NADH was substituted for [4-3H]NADPH, very little formation of labeled lipid from the dihydroxyacetone phosphate derivatives was observed, showing that the enzymes are specific for NADPH as the coenzyme. The same results were obtained when the reduction was studied with nonradioactive NADH or NADPH and 32P-labeled acyl or alkyl dihydroxyacetone phosphate. Experiments with A-[4-3H]NADPH and B-[4-3H]NADPH proved that only the B-hydrogen from the nicotinamide ring was transferred to reduce the keto compounds. Some preliminary results indicated that one enzyme may be responsible for the reduction of both acyl and alkyl derivatives of dihydroxyacetone phosphate.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)44832-1