14689-84-0

Usage

Uses

Used in Photosynthesis:
D-ribulose 1,5-diphosphate is used as a key intermediate in the Calvin cycle for the carbon fixation process. It serves as the primary acceptor of carbon dioxide and is a substrate for the enzyme Rubisco, which catalyzes the addition of carbon dioxide to RuDP, leading to the production of two molecules of 3-phosphoglycerate. This process is essential for the conversion of inorganic carbon into organic compounds, such as sugars, in plants.
Used in Plant Biology Research:
D-ribulose 1,5-diphosphate is used as a research tool in plant biology to study the mechanisms of photosynthesis and carbon assimilation. It helps researchers understand the role of RuDP in the Calvin cycle and its interactions with other molecules and enzymes involved in the process. This knowledge can contribute to the development of strategies to improve photosynthetic efficiency and crop productivity.
Used in Biochemical Education:
D-ribulose 1,5-diphosphate is used as a teaching aid in biochemical education to illustrate the process of photosynthesis and the role of the Calvin cycle in carbon fixation. It helps students understand the molecular mechanisms involved in the conversion of inorganic carbon into organic compounds in plants, which is a fundamental concept in plant biology and photosynthesis.

InChI:InChI=1/C5H12O11P2/c6-3-2(1-14-17(8,9)10)15-5(4(3)7)16-18(11,12)13/h2-7H,1H2,(H2,8,9,10)(H2,11,12,13)/t2-,3-,4-,5?/m1/s1

Upstream product

• 10139-18-1 6-phospho-α-D-glucopyranosyl-1-phosphate 
• 54946-48-4 benzyl-β-D-ribofuranoside 
• 130384-52-0 5-phosphorylribose-1-pyrophosphate 
• 7732-18-5 water 
• 85-32-5 Guanosine 5'-monophosphate 
• 18646-11-2 α-D-ribofuranosyl-1-phosphate 
• 119095-47-5 triethylammonium dibenzyl phosphate 
• 122174-79-2 benzyl-(O²,O³-carbonyl-O⁵-diphenoxyphosphoryl-β-D-ribofuranoside) 

Downstream Products

• 90275-36-8 5-phospho-α-D-ribofuranosyl-1,2-cyclic monophosphate 

Relevant academic research and scientific papers

Discovery of a cyclic phosphodiesterase that catalyzes the sequential hydrolysis of both ester bonds to phosphorus

The bacterial C-P lyase pathway is responsible for the metabolism of unactivated organophosphonates under conditions of phosphate starvation. The cleavage of the C-P bond within ribose-1-methylphosphonate-5-phosphate to form methane and 5-phospho-ribose-1,2-cyclic phosphate (PRcP) is catalyzed by the radical SAM enzyme PhnJ. In Escherichia coli the cyclic phosphate product is hydrolyzed to ribose-1,5-bisphosphate by PhnP. In this study, we describe the discovery and characterization of an enzyme that can hydrolyze a cyclic phosphodiester directly to a vicinal diol and inorganic phosphate. With PRcP, this enzyme hydrolyzes the phosphate ester at carbon-1 of the ribose moiety to form ribose-2,5-bisphosphate, and then this intermediate is hydrolyzed to ribose-5-phosphate and inorganic phosphate. Ribose-1,5-bisphosphate is neither an intermediate nor a substrate for this enzyme. Orthologues of this enzyme are found in the human pathogens Clostridium difficile and Eggerthella lenta. We propose that this enzyme be called cyclic phosphate dihydrolase (cPDH) and be designated as PhnPP.