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Results 1 - 10 of 11 > >>
EC Number Reaction Commentary Reference
Show all pathways known for 2.3.1.50Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.50palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2 formation of the external aldimine intermediate 487175
Show all pathways known for 2.3.1.50Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.50palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2 mechanism 487156, 487174
Show all pathways known for 2.3.1.50Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.50palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2 ordered bi-bi mechanism -, 487172
Show all pathways known for 2.3.1.50Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.50palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2 pyridoxal 5'-phosphate dependent reaction mechanism, key active site residues are His159, Asp231, His234, and Lys265 736305
Show all pathways known for 2.3.1.50Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.50palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2 the enzyme forms a pyridoxal 5'-phosphate-L-serine-aldimine intermediate during the reaction, His159 plays multiple roles in the reaction mechanism by exploiting the stereochemistry of Dunathan’s conjecture. His159 promotes both the Claisen-type condensation as an acid catalyst and the protonation at Calpha of the second quinonoid to form the pyridoxal 5'-phosphate-KDS aldimine, spectral analysis, overview 704483
Show all pathways known for 2.3.1.50Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.50palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2 the enzyme forms an external aldimine intermediate, as well as dunathan and quinoid intermediates, and followed by external beta-keto acid intermediate, and finally product quinoid and product external aldimine intermediates, reaction cycle, overview -, 704496
Show all pathways known for 2.3.1.50Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.50palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2 the enzyme forms an external aldimine intermediate, as well as dunathan and quinoid intermediates, followed by external beta-keto acid intermediate, and finally product quinoid and product external aldimine intermediates, reaction cycle, overview 704496
Show all pathways known for 2.3.1.50Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.50palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2 the reaction proceeds via a key carbanion/quinonoid species and an internal aldimine/PLP-bound form of the enzyme 735744
Show all pathways known for 2.3.1.50Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.50palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2 the reaction proceeds via several intermediate states, the pyridoxal 5'-phosphate cofactor binds to an active site lysine residue as an internal aldimine/Schiff’s base (I). The L-serine displaces the lysine residue (Lys265) to form the PLP-L-serine external aldimine (II). Deprotonation of II gives a carbanion/quinonoid species (III) which condenses in a Claisen-like manner with the acyl-CoA thioester substrate to form a PLP-beta-keto acid, which then decarboxylates to generate the PLP-KDS product quinonoid (IV). This then reprotonates to form PLP-KDS aldimine (V) which is finally displaced by Lys265. The step releasing CoA and CO2 and producing the quinonoid intermediate species is irreversible. Interaction between the hydroxyl group of the L-serine substrate and the 5'-phosphate group of pyridoxal 5'-phosphate occurs in the formation of the external aldimine II, overview 735932
Show all pathways known for 2.3.1.50Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.50palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2 using 1HNMR the exchange of the alpha-proton of L-serine with the solvent in the presence and absence of S-(2- oxoheptadecyl)-CoA, the structural analogue of palmitoyl-CoA is investagated. Results demonstrate the presence of substrate synergism, in which the alpha-proton of L-serine is activated by the binding of the second substrate palmitoyl-CoA 687795
Results 1 - 10 of 11 > >>