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Results 1 - 10 of 10
EC Number Reaction Commentary Reference
Show all pathways known for 2.4.2.3Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.3uridine + phosphate = uracil + alpha-D-ribose 1-phosphate binding isotope effects indicate ground-state stabilization in the Michaelis complex, such as bonding environment, ribosyl pucker, and natural bond orbital charges 721669
Show all pathways known for 2.4.2.3Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.3uridine + phosphate = uracil + alpha-D-ribose 1-phosphate mutational analysis supports for the push-pull model of catalysis, proposed catalytic mechanism of PcUP1, modeling, overview. Deprotonation of phosphate by Arg104, increases the negative charge on the phosphate oxygen, leading to repulsion between the electrons of phosphate oxygen and electron pairs of the endocylic ribosyl oxygen and the formation of an intermediate oxocarbenium ion. At the same time, the Gln206, Arg208 and Arg264-N1 hydrogen network-bond pulls electrons from the glycosidic bond onto the pyrimidine ring. These two actions work in concert to weaken the glycosidic bond. Arg39 pivots, to physically push the phosphate closer to the ribose moiety. After glycosidic bond cleavage, ribose-1-phosphate dissociates from the active pocket, and then an active water reprotonates the negatively charged purine. The final step is to release the neutral purine base -, 760136
Show all pathways known for 2.4.2.3Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.3uridine + phosphate = uracil + alpha-D-ribose 1-phosphate ordered bi-bi mechanism 638515, 638526, 638527
Show all pathways known for 2.4.2.3Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.3uridine + phosphate = uracil + alpha-D-ribose 1-phosphate ordered bi-bi mechanism, phosphate binds before uridine and alpha-D-ribose 1-phosphate is released after uracil 638457
Show all pathways known for 2.4.2.3Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.3uridine + phosphate = uracil + alpha-D-ribose 1-phosphate phosphate binds before uridine and ribose 1-phosphate is released after uracil 638526, 638527
Show all pathways known for 2.4.2.3Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.3uridine + phosphate = uracil + alpha-D-ribose 1-phosphate random mechanism 638520
Show all pathways known for 2.4.2.3Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.3uridine + phosphate = uracil + alpha-D-ribose 1-phosphate rapid-equilibrium random mechanism -, 638518
Show all pathways known for 2.4.2.3Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.3uridine + phosphate = uracil + alpha-D-ribose 1-phosphate sequential mechanism 638531, 638533, 638535
Show all pathways known for 2.4.2.3Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.3uridine + phosphate = uracil + alpha-D-ribose 1-phosphate sequential rather than ping-pong mechanism, addition of substrate is random 638454
Show all pathways known for 2.4.2.3Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.3uridine + phosphate = uracil + alpha-D-ribose 1-phosphate steady-state random kinetic mechanism. Reaction follows an ANDN/SN2 mechanism where chemistry contributes significantly to the overall rate-limiting step of the reaction. No kinetically significant proton transfer step is involved at the transition state. Proton transfer to neutralize the leaving group is not part of transition state formation, consistent with an enzyme-stabilized anionic uracil as the leaving group. Kinetic analysis as a function of pH indicates one protonated group essential for catalysis and for substrate binding 721654
Results 1 - 10 of 10