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Results 1 - 10 of 12 > >>
EC Number Cofactor Commentary Reference
Show all pathways known for 4.1.1.18Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.18pyridoxal 5'-phosphate - 37284, 654982, 690395, 690597, 714832, 715142, 746801, 747039, 747357, 747358, 747369, 747396, 747444, 747594, 747655, 748380, 748382, 748386, 748418, 748513, 749226, 749315
Show all pathways known for 4.1.1.18Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.18pyridoxal 5'-phosphate 0.1 mM 690269
Show all pathways known for 4.1.1.18Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.18pyridoxal 5'-phosphate best at 0.01 mM 746801
Show all pathways known for 4.1.1.18Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.18pyridoxal 5'-phosphate contains 1 mol of pyridoxal 5'-phosphate per mol of subunit 37283
Show all pathways known for 4.1.1.18Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.18pyridoxal 5'-phosphate contains 10 mol of pyridoxal 5'-phosphate per mol of enzyme 37295
Show all pathways known for 4.1.1.18Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.18pyridoxal 5'-phosphate dependent on 749366
Show all pathways known for 4.1.1.18Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.18pyridoxal 5'-phosphate dependent on, best at 0.025-0.1 mM in whole-cell assay 748377
Show all pathways known for 4.1.1.18Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.18pyridoxal 5'-phosphate enzyme solution exhibits absorption maxima at 279 and 415 nm, and the ratio of absorbance value at 415 nm to that at 279 nm i 0.158 728013
Show all pathways known for 4.1.1.18Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.18pyridoxal 5'-phosphate PLP, binding structure and binding mode, overview. The highly flexible active site contributes to the low affinity for pyridoxal 5'-phosphate in SrLDC. The cofactor affinity is increased in enzyme mutant A225C/T302C due to introduction of an artificial disulfide bond 749101
Show all pathways known for 4.1.1.18Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.18pyridoxal 5'-phosphate PLP, binding structure and binding mode, overview. The PLP cofactor binds mainly to the pocket formed at the barrel domain, and the catalytic residue Lys51 interacts with the aldehyde group of the pyridoxal ring. The pyridine ring is stabilized by hydrogen bond between N1 of the ring and the acidic residue Glu255. The phosphate moiety of PLP is mainly stabilized by strong hydrogen bonds with the side-chains of His179, Ser182, and Tyr352, and the main chains of Gly219, Gly257, and Arg258 are also involved in the stabilization of the moiety 749097
Results 1 - 10 of 12 > >>