Final answer:
The enzyme glyceraldehyde-3-phosphate dehydrogenase catalyzes the oxidation and phosphorylation of glyceraldehyde-3-phosphate, but does not involve a covalent intermediate or use an active site histidine as a proton acceptor.
Step-by-step explanation:
The enzyme glyceraldehyde-3-phosphate dehydrogenase catalyzes the oxidation of glyceraldehyde-3-phosphate by transferring high-energy electrons to NAD+ to produce NADH. This oxidation reaction does not involve a covalent intermediate.
The enzyme does not use an active site histidine to serve as a proton acceptor. Instead, during the reaction, a hydrogen molecule is split into a hydride ion (H-) and a proton (H+), and the H- ions reduce NAD+ to NADH.
The reaction catalyzed by glyceraldehyde-3-phosphate dehydrogenase does involve oxidation and phosphorylation of the substrate, as glyceraldehyde-3-phosphate is oxidized and phosphorylated to produce 1,3-bisphosphoglycerate.