Cytosolic glycolysis, the conversion of hexose to pyruvate, ...

created [InstanceEdit:1164949] Wu, Guanming, 2010-12-11
dbId 1119253
displayName Cytosolic glycolysis, the conversion of hexose to pyruvate, ...
modified [InstanceEdit:5157501] D'Eustachio, P, 2013-11-21
schemaClass Summation
text Cytosolic glycolysis, the conversion of hexose to pyruvate, proceeds with the notable feature that fructose 2,6-bisphosphate can be generated from fructose 6-phosphate either in a reaction that consumes ATP or in one that consumes pyrophosphate. As pyrophosphate can be present in substantial amounts (plant cells lack a cytosolic pyrophosphatase enzyme), this second reaction can be a major source of fructose 2,6-bisphosphate.

Experimental studies of glycolysis in rice are very limited, and all the reactions annotated here have been inferred from studies of orthologous proteins in Arabidopsis and other plant species. Analyses of orthology relationships between predicted rice proteins and those of Arabidopsis suggest that the rice genome encodes two or more isozymes of hexokinase, glucose 6-phosphate isomerase, 6-phosphofructokinase (ATP dependent), 6-phosphofructokinase (pyrophosphate dependent), fructose-bisphosphate aldolase, phosphoglycerate kinase, phosphoglycerate mutase, and enolase. The physiological roles of these rice isozymes are unknown, but data from other species suggest that their differential expression may play important roles in regulating development and function of specialized tissues and in stress responses (Plaxton 1996; Fernie et al. 2004).

Recent studies of Arabidopsis cells indicate that, while the enzymes of glycolysis are all present in substantial amounts in the cytosol, they can also be associated with the outer mitochondrial membrane, consistent with the hypothesis that the conversion of hexose to pyruvate may be localized, increasing the efficiency with which pyruvate is generated and enters mitochondria for conversion to acetyl CoA. (Giege et al. 2003).