High impact information on GLYCERALDEHYDE 3-PHOSPHATE

• Measurements of the anabolic activities (reduction of 1,3-bisphosphoglycerate) in extracts from wild type and mutant cells show that Gap2 is a major enzyme with dual cosubstrate specificity for NAD and NADP, while Gap1 displays a minor NAD-specific GAPDH activity [1].
• However, if measured in the catabolic direction (oxidation of glyceraldehyde-3-phosphate) Gap2 activity is very low and increases three- to fivefold after gel filtration of extracts over Sephadex G25 [1].
• While Gap2 operates in the photosynthetic Calvin cycle and in non-photosynthetic gluconeogenesis, Gap1 seems to be essential only for glycolytic glucose breakdown, conditions under which the catabolic activity of Gap2 seems to be repressed by a specific low-molecular-weight inhibitor [1].
• In larvae reared on quartz substrate, the genes IGF-II and the beta-actin showed a lower expression, while the GADPH was totally suppressed and the expression of HSP70 increased [2].
• Murine mRNA of 3.1 kb size is expressed in all the tissue studied at a level independent of glyceraldehyde-3-phosphate dehydrogenase (GADPH) mRNA [3].

Gene context of GLYCERALDEHYDE 3-PHOSPHATE

• Insulin induces glyceraldehyde-3-phosphate dehydrogenase (GADPH) gene transcription in part by regulating one or more proteins that bind a cis-acting element, IRE-A [4].
• The genes (TWIK-1, TWIK-2, TASK-1, TASK-2, TASK-3, TREK-1, TREK-2, TRAAK and KCNK6) were quantified, relative to glyceraldehyde-3-phosphate dehydrogenase (GADPH), in all four chambers of adult rat hearts and in the ventricles of embryonic rat hearts [5].
• The complete deficiency was associated with marked elevation of fructose-1, 6-diphosphate (FDP) and dihydroxyacetonephosphate (DHAP) and a less marked rise in glyceraldehyde-3-phosphate (GA3P) among glycolytic intermediates in the RBC [6].

References