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L-Ribose Fischer Projection. Ribose is a simple sugar and carbohydrate with molecular formula C 5 H 10 O 5 and the linear-form composition H−(C=O)−(CHOH) 4 −H. The naturally occurring form, d-ribose, is a component of the ribonucleotides from which RNA is built, and so this compound is necessary for coding, decoding, regulation and expression of genes.
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D-Ribose pyranase is an enzyme that catalyzes the interconversion of β-D-ribopyranose and β-D-ribofuranose. [1] This enzyme is an isomerase that has only been found in bacteria and viruses . It has two known functions of helping transport ribose into cells and producing β- D -ribofuranose, which can later be used to make ribose 5-phosphate ...
CD38 (cluster of differentiation 38), also known as cyclic ADP ribose hydrolase, is a glycoprotein [5] found on the surface of many immune cells (white blood cells), including CD4 +, CD8 +, B lymphocytes and natural killer cells. CD38 also functions in cell adhesion, signal transduction and calcium signaling. [6]
The term "2-deoxyribose" may refer to either of two enantiomers: the biologically important d-2-deoxyribose and to the rarely encountered mirror image l-2-deoxyribose. [3] d-2-deoxyribose is a precursor to the nucleic acid DNA. 2-deoxyribose is an aldopentose, that is, a monosaccharide with five carbon atoms and having an aldehyde functional group.
Carbon atoms from ribose in PRPP form the linear chain and part of the imidazole ring in histidine. [ 15 ] [ 16 ] [ 17 ] The same is true for the biosynthesis of tryptophan, with the first step being N-alkylation of anthranilic acid catalysed by the enzyme anthranilate phosphoribosyltransferase .
ATP + d-ribose ⇌ ADP + d-ribose 5-phosphate. Thus, the two substrates of this enzyme are ATP and d-ribose, whereas its two products are ADP and d-ribose 5-phosphate. The systematic name of this enzyme class is ATP: d-ribose 5-phosphotransferase. Other names in common use include deoxyribokinase, ribokinase (phosphorylating), and d-ribokinase.
The first published description of a structure of a prokaryotic phosphopentomutase was in 2011. [1] Structures of Bacillus cereus phosphopentomutase as it was purified, after activation, bound to ribose 5-phosphate and bound to glucose 1,6-bisphosphate are deposited in the PDB with accession codes 3M8W, 3M8Y, 3M8Z and 3OT9, respectively.