Fructose 1,6-bisphosphate aldolase/phosphatase may be an ancestral gluconeogenic enzyme.

摘要: Many thermophilic bacteria and archaea use carbon dioxide or monoxide as starting materials for the synthesis of organic material used cellular molecules. A central enzyme in this pathway has now been identified fructose 1,6-bisphosphate aldolase/phosphatase. This enzyme, which is missing most other eukaryotes, characteristics required a primordial autotrophic metabolism. adds supporting evidence hypothesis that life originated chemolithoautrophic thermophile glucogenesis evolved before glycolysis. robust may also be biotechnologically valuable producing engineered cells specialized production carbohydrates. Thermophilic making substances discovered, namely might represent ancestral gluconeogenic enzyme. Most archaeal groups deeply branching bacterial lineages harbour organisms with chemolithoautotrophic They live at high temperatures volcanic habitats expense inorganic substances, often under anoxic conditions1. These diverse fixation mechanisms generating acetyl-coenzyme A, from gluconeogenesis must start2,3,4. Here we show virtually all well contain bifunctional (FBP) aldolase/phosphatase both FBP aldolase phosphatase activity. Bacteria Eukaryota, heat-stabile even mesophilic marine Crenarchaeota. Its bifunctionality ensures heat-labile triosephosphates are quickly removed trapped stabile 6-phosphate, rendering unidirectional. We propose highly conserved, represents pace-making evolution preceded glycolysis5.