14689-84-0 Usage
General Description
D-ribulose 1,5-diphosphate, also known as RuDP or ribulose 1,5-bisphosphate, is a key intermediate in the Calvin cycle, a series of biochemical reactions that occur during photosynthesis. It is a highly reactive compound that is formed by the phosphorylation of d-ribulose 5-phosphate, and it plays a crucial role in the carbon fixation process. RuDP serves as the primary acceptor of carbon dioxide and serves as a substrate for the enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco), which catalyzes the addition of carbon dioxide to RuDP to produce two molecules of 3-phosphoglycerate. This makes RuDP a crucial molecule in photosynthetic carbon assimilation, and it is essential for the production of sugars and other organic compounds in plants.
Check Digit Verification of cas no
The CAS Registry Mumber 14689-84-0 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,4,6,8 and 9 respectively; the second part has 2 digits, 8 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 14689-84:
(7*1)+(6*4)+(5*6)+(4*8)+(3*9)+(2*8)+(1*4)=140
140 % 10 = 0
So 14689-84-0 is a valid CAS Registry Number.
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
14689-84-0Relevant articles and documents
Discovery of a cyclic phosphodiesterase that catalyzes the sequential hydrolysis of both ester bonds to phosphorus
Ghodge, Swapnil V.,Cummings, Jennifer A.,Williams, Howard J.,Raushel, Frank M.
, p. 16360 - 16363 (2013)
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.
