2.3.1.37	succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2	5-aminolevulinate synthase operates under the stereoelectronic control predicted by Dunathan’s hypothesis	687586	
2.3.1.37	succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2	covalent binding of pyridoxal 5'-phosphate and glycine to active site Lys131 is required for optimal activity	486849	
2.3.1.37	succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2	cysteine in heme-regulatory motif	486850	
2.3.1.37	succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2	Lys313 acts as a general base during formation of the quinonoid reaction intermediates	486859	
2.3.1.37	succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2	mechanism	-, 486813, 486819, 486820, 486821, 486826, 486845, 486850, 486859	
2.3.1.37	succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2	mechanism, aldimine linkage between pyridoxal 5’-phosphate and enzyme	-, 661787	
2.3.1.37	succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2	ordered bi-bi mechanism in which glycine binds first and 5-aminolevulinic acid dissociates last	-, 486845, 486850	
2.3.1.37	succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2	proposed chemical mechanism of enzyme ALAS2 via (I) internal aldimine complex, (II) glycine-external aldimine, (III) quinonoid intermediate I, (IV) glycine-succinyl-CoA condensation intermediate, (V) 2-amino-3-ketoadipate intermediate, (VI) enol intermediate, (VII) quinonoid intermediate II, and (VIII) 5-aminolevulinate-external aldimine	736491	
2.3.1.37	succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2	proposed chemical mechanism of enzyme ALAS2. via (I) internal aldimine complex, (II) glycine-external aldimine, (III) quinonoid intermediate I, (IV) glycine–succinyl-CoA condensation intermediate, (V) 2-amino-3-ketoadipate intermediate, (VI) enol intermediate, (VII) quinonoid intermediate II, and (VIII) 5-aminolevulinate-external aldimine	736116	
2.3.1.37	succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2	pyridoxal 5'-phosphate binding site, sequence and function of glycine-rich motif	486850, 486851	
2.3.1.37	succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2	the active site is located at the subunit interface and contains catalytically essential residues from the two subunits	486852	
2.3.1.37	succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2	the rate of 5-aminolevulinate release is controlled by a hysteretic kinetic mechanism initiated by conformational changes of the enzyme. The active site residue Thr148 modulates the enzyme's strict amino acid substrate specificity. Catalytic mechanism, overview	736454	
2.3.1.37	succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2	three-step kinetic process, ordered kinetic mechanism, reaction mechanism	486861	
2.3.1.37	succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2	Tyr121, Asp279, Arg439, and Lys313 are involved in substrate and cofactor binding, mechanism, subunit localisation	486849, 486851, 486852, 486855, 486856, 486857