1.2.1.79	succinate semialdehyde + NAD+ + H2O	the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+	
1.2.1.79	succinate semialdehyde + NADP+ + H2O	the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+	
1.2.1.79	succinate semialdehyde + NADP+ + H2O	-	
1.2.1.79	succinate semialdehyde + NADP+ + H2O	data from crystal structures provide details about the catalytic mechanism by revealing a covalent adduct of a cofactor with the catalytic cysteine in the binary complex and a proposed thiohemiacetal intermediate in the ternary complex	
1.2.1.79	succinic semialdehyde + NADP+ + H2O	chemical mechanism based on functional data and structural information proposed, 1H-NMR to probe the stereospecificity of GabD1 show a transfer of the deuteride to the pro-R position of NADP+ indicating GabD1 has A-type stereospecificity