L-gulonolactone oxidase L-gulonolactone oxidase -gulonolactone oxidase (EC 1.1.3.8) is an enzyme that produces vitamin C, but is non-functional in Haplorrhini (including humans), in some bats, and in guinea pigs. It catalyzes the reaction of -gulono-1,4-lactone with oxygen to -xylo-hex-3-gulonolactone and hydrogen peroxide. It uses FAD as a cofactor. The -xylo-hex-3-gulonolactone (2-keto-gulono-gamma-lactone) is able to convert to hexuronic acid (ascorbic acid) spontaneously, without enzymatic action. The non-functional gulonolactone oxidase pseudogene (GULOP) was mapped to human chromosome 8p21 that corresponds to an evolutionarily conserved segment on either porcine chromosome 4 (SSC4) or 14 (SSC14). GULO produces the precursor to ascorbic acid, which spontaneously converts
Chemistry of ascorbic acid from animal adrenal glands. In 1932 Charles Glen King confirmed that it was indeed the antiscorbutic factor. In 1933, sugar chemist Walter Norman Haworth, working with samples of "hexuronic acid" that Szent-Györgyi had isolated from paprika and sent him in the previous year, deduced the correct structure and optical-isomeric nature of the compound, and in 1934 reported its first synthesis. In reference to the compound's antiscorbutic properties, Haworth and Szent-Györgyi proposed to rename it "a-scorbic acid" for the compound, and later specifically -ascorbic acid. Because of their work, in 1937 the Nobel Prizes for chemistry and medicine were awarded to