4.1.1.18	pyridoxal 5'-phosphate	-	37284, 654982, 690395, 690597, 714832, 715142, 746801, 747039, 747357, 747358, 747369, 747396, 747444, 747594, 747655, 748380, 748382, 748386, 748418, 748513, 749226, 749315	
4.1.1.18	pyridoxal 5'-phosphate	0.1 mM	690269	
4.1.1.18	pyridoxal 5'-phosphate	best at 0.01 mM	746801	
4.1.1.18	pyridoxal 5'-phosphate	contains 1 mol of pyridoxal 5'-phosphate per mol of subunit	37283	
4.1.1.18	pyridoxal 5'-phosphate	contains 10 mol of pyridoxal 5'-phosphate per mol of enzyme	37295	
4.1.1.18	pyridoxal 5'-phosphate	dependent on	749366	
4.1.1.18	pyridoxal 5'-phosphate	dependent on, best at 0.025-0.1 mM in whole-cell assay	748377	
4.1.1.18	pyridoxal 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	
4.1.1.18	pyridoxal 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	
4.1.1.18	pyridoxal 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	
4.1.1.18	pyridoxal 5'-phosphate	required as cofactor	37300	
4.1.1.18	pyridoxal 5'-phosphate	sequence of the pyridoxal 5'-phosphate binding site	37292