ePrints@IIScePrints@IISc Home | About | Browse | Latest Additions | Advanced Search | Contact | Help

Triacylglycerol synthesis in developing seeds of groundnut (Arachis hypogaea): Pathway and properties of enzymes of sn-Glycerol 3-phosphate formation

Ghosh, Shobha and Sastry, PS (1988) Triacylglycerol synthesis in developing seeds of groundnut (Arachis hypogaea): Pathway and properties of enzymes of sn-Glycerol 3-phosphate formation. In: Archives of Biochemistry and Biophysics, 262 (2). pp. 508-516.

[img] PDF
Triacylglycerol_Synthesis_in.pdf - Published Version
Restricted to Registered users only

Download (1129Kb) | Request a copy
Official URL: http://dx.doi.org/10.1016/0003-9861(88)90402-X

Abstract

The enzymatic pathway for the synthesis of sn-glycerol 3-phosphate was investigated in developing groundnut seeds (Arachis hypogaea). Glycerol-3-phosphate dehydrogenase was not detected in this tissue but an active glycerokinase was demonstrated in the cytosolic fraction. It showed an optimum pH at 8.6 and positive cooperative interactions with both glycerol and ATP. Triosephosphate isomerase and glyceraldehyde-3-phosphate phosphatase were observed mainly in the cytosolic fraction while an active glyceraldehyde reductase was found mainly in the mitochondrial and microsomal fractions. The glyceraldehyde 3-phosphate phosphatase showed specificity and positive cooperativity with respect to glyceraldehyde 3-phosphate. The glyceraldehyde reductase was active toward glucose and fructose but not toward formaldehyde and showed absolute specificity toward NADPH. It is concluded that in the developing groundnut seed, sn-glycerol 3-phosphate is synthesized essentially by the pathway dihydroxyacetone phosphate ? glyceraldehyde 3-phosphate ?Pi glyceraldehyde ?NADPH glycerol ?ATP glycerol 3-phosphate. All the enyzmes of this pathway showed activity profiles commensurate with their participation in triacylglycerol synthesis which is maximal during the period 15�35 days after fertilization. Glycerokinase appears to be the rate-limiting enzyme in this pathway.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Elsevier science.
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 13 Oct 2010 09:04
Last Modified: 13 Oct 2010 09:04
URI: http://eprints.iisc.ernet.in/id/eprint/33060

Actions (login required)

View Item View Item