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D-ribose 5-phosphate, also known as ribose-5-phosphate or R5P, is an important organic compound and a key intermediate in the metabolic pathways of living organisms. It is a phosphorylated form of D-ribose, a five-carbon sugar, and plays a crucial role in various biochemical processes, including the synthesis of nucleotides, which are the building blocks of DNA and RNA. D-ribose 5-phosphate is generated during the pentose phosphate pathway, a metabolic route that produces NADPH, a vital reducing agent for cellular redox reactions and lipid synthesis. Additionally, it is involved in the Calvin cycle, a series of biochemical reactions that occur in plants, algae, and some microorganisms, facilitating the fixation of carbon dioxide into organic molecules. The compound is also a precursor in the synthesis of other essential biomolecules, such as the coenzymes flavin adenine dinucleotide (FAD) and nicotinamide adenine dinucleotide phosphate (NADP+), which are involved in numerous enzymatic reactions.

93-87-8

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93-87-8 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 93-87-8 includes 5 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 2 digits, 9 and 3 respectively; the second part has 2 digits, 8 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 93-87:
(4*9)+(3*3)+(2*8)+(1*7)=68
68 % 10 = 8
So 93-87-8 is a valid CAS Registry Number.

93-87-8Upstream product

93-87-8Relevant academic research and scientific papers

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 (2013/12/04)

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.

Practical Synthesis of 5-Phospho-D-ribosyl α-1-pyrophosphate (PRPP): Enzymatic Routes from Ribose 5-Phosphate or Ribose

Gross, Akiva,Abril, Obsidiana,Lewis Jerome M.,Geresh, Shimona,Whitesides, George M.

, p. 7428 - 7435 (2007/10/02)

This paper describes enzymatic syntheses of 5-phospho-D-ribosyl α-1-pyrophosphate (PRPP) on a 75-mmol scale.The reactions used PAN-immobilized PRPP synthetase as catalyst with in situ ATP-cofactor regeneration.In one procedure pure r-5-P was used as a starting material; in a second, r-5-P was synthesized by ribokinase-catalyzed phosphorilation of D-ribose and used in situ.The potential for use of PRPP as a starting material for the preparation of nucleotides was demonstrated by an enzymatic synthesis of UMP.This paper also describes several methods for the preparation of r-5-P: acid-catalyzed hydrolysis of AMP, acid-catalyzed hydrolysis of crude mononucleotide mixture obtained by digestion of RNA, chemical synthesis from D-ribose, and ribokinase-catalyzed synthesis from D-ribose.Procedures are described for the isolation of PRPP synthetase (from Salmonella typhimurium) and ribokinase (from Lactobacillus plantarum) and for immobilization of these enzymes in PAN.

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