title: Stereospecificity of C4 nicotinamide hydrogen transfer of the NADP-dependent glyceraldehyde-3-phosphate dehydrogenase.
abstract: The stereospecificity of the reaction catalysed by the spinach chloroplast enzyme NADP-dependent glyceraldehyde-3-phosphate dehydrogenase (D-glyceraldehyde-3-phosphate: NADP+ oxidoreductase (phosphorylating), EC 1.2.1.13) with respect to the C4 nicotinamide hydrogen transfer was investigated. NADPH deuterated at the C4 HA position was synthesized using aldehyde dehydrogenase. 1H-NMR spectroscopy was used to examine the NADP+ product of the GPDH reaction for the presence or absence of the C4 deuterium atom. Chloroplast NADP-dependent glyceraldehyde-3-phosphate dehydrogenase retains the deuterium at the C4 HA position (removing the hydrogen atom), and is therefore a B (pro-S) specific dehydrogenase.
authors.affiliation: School of Biological Sciences, Queen Mary College, London, U.K.
authors.forename: L M
authors.initials: LM
authors.lastname: Levy
authors.forename: G F
authors.initials: GF
authors.lastname: Betts
mesh_terms: D002736:Chloroplasts / Q000201:enzymology; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D009249:NADP / Q000378:metabolism; D009536:Niacinamide / Q000378:metabolism; D010944:Plants / Q000201:enzymology*
chemical_list: D009536:Niacinamide; D009249:NADP; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases