| 背景 | GAPDH encodes a member of the glyceraldehyde-3-phosphate dehydrogenase protein family. Glyceraldehyde-3-phosphate dehydrogenase has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. The product of GAPDH catalyzes an important energy-yielding step in carbohydrate metabolism, the reversible oxidative phosphorylation of glyceraldehyde-3-phosphate in the presence of inorganic phosphate and nicotinamide adenine dinucleotide (NAD). Glyceraldehyde-3-phosphate dehydrogenase has additionally been identified to have uracil DNA glycosylase activity in the nucleus. Also, Glyceraldehyde-3-phosphate dehydrogenase contains a peptide that has antimicrobial activity against E. coli, P. aeruginosa, and C. albicans. Studies of a similar protein in mouse have assigned a variety of additional functions including nitrosylation of nuclear proteins, the regulation of mRNA stability, and acting as a transferrin receptor on the cell surface of macrophage. Many pseudogenes similar to this locus are present in the human genome. Alternative splicing results in multiple transcript variants. |
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